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Cytokine array

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Cytokine array B A T (evidence®) 4x90 (360 biochips) EV3508 POA
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Intended Use

The Evidence Cytokine Array is to be used for the in vitro simultaneous quantitative detection of multiple related cytokine immunoassays (in parallel) from a single sample run on the automated biochip array analyzer, Evidence. The Evidence Cytokine Array is for research use only and not for diagnostic procedures.

Clinical Significance

The field of cytokine research has evolved from four independent study areas. The first and most significant area has been immunology, specifically the study of lymphokines. The second source of cytokine research has involved the interferons.   The hematopoietic growth factors or colony stimulating factors have been the third area of cytokine research with the study of non-hematopoietic growth factors the fourth source of cytokine research.  The role of cytokines in the regulation of immune and inflammatory responses is now clearly recognized but cytokine research has lead to their implication in other pathological conditions.

Knowledge of the complexity of the cytokine network and the role played by cytokines is critical in understanding normal and pathological processes.  Therefore assaying a number of cytokines in the one sample has become of increasing interest in laboratory medicine.   The knowledge gained from multiple cytokine analysis should allow better diagnosis and disease management.


The Evidence analyzer is a fully automated Biochip Array System. It performs simultaneous quantitative detection of multiple analytes from a single patient sample.

The core technology is the Randox Biochip, a solid-state device containing an array of discrete test regions of immobilized antibodies specific to different cytokines and growth factors. A sandwich chemiluminescent immunoassay is employed for the cytokine assays. Increased levels of cytokine in a specimen will lead to increased binding of antibody labeled with horse radish peroxidase (HRP) and thus an increase in the chemiluminescent signal emitted.

The light signal generated from each of the test regions on the biochip is detected using digital imaging technology and compared to that from a stored calibration curve. The concentration of analyte present in the sample is calculated from the calibration curve.

Several different immunoassay based multi-analyte arrays have been developed for use on Evidence. The Evidence Cytokine Array will quantitatively test for IL-1α, IL-1β, IL-2, IL-4, IL-6, IL-8, IL-10, VEGF, IFNγ, EGF, MCP-1 and TNFα simultaneously.

Interleukin-2 (IL-2) Assay

Intended Use

The Evidence Interleukin-2 (IL-2) test has been designed for the quantitative measurement of IL-2 in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

IL-2 is a glycoprotein with a molecular mass of 15-18 kDa which has varying degrees of glycosylation accounting for the observed molecular weight range.  IL-2 is synthesized as a precursor protein of 153 amino acids from which 20 amino acids are cleaved to produce the active form ((1)).  It has a single disulphide bond which is essential for biological activity.  The IL-2 receptor consists of three distinct membrane associated units which bind IL-2 with high affinity: a 55kDa α chain, a 70-75 kDa β chain and a 64 kDa γ chain. Soluble IL-2Rα and IL-2Rβ have been found in serum ((2,3)).

IL-2 is a lymphokine that is synthesized and secreted primarily by T-cells following their activation by mitogens or antigen-activated T-lymphocytes.  Transformed T-cells and B-cells, leukemia cells, lymphokine activated killer cells and natural killer cells also secrete IL-2 in small amounts((4,5)). Due to its effects on T-cells and B-cells IL-2 is a central regulator of immune responses ((6,7)). It stimulates proliferation of T-cells, activated B-cells, natural killer cells, monocytes, thymocytes and lymphokine activated killer cells. It causes differentiation of activated B-cells, monocytes and oligodendrocytes. It also stimulates the cytolytic activity and cytokine production by activated B-cells, monocytes, natural killer cells and thymocytes((4,5)). IL-2 supports the induction and secretion of immunoglobulins((8)).  It plays a role in anti-inflammatory reactions and in tumor surveillance((9)).  IL-2 stimulates the synthesis of IFNg and IL-4 by T-cells as well as inducing secretion of IL-1 and TNF-a((10,11)).  IL-2 is also a possible neuromodulator((12)) and growth regulator of glial cells,((13)) and has been found to damage the blood brain barrier ((14)).

IL-2 and IL-2R are elevated in Hodgkins disease, multiple sclerosis, rheumatoid arthritis, type 1 diabetes, AIDS, severe burn trauma and allograft rejection((15)). Antibodies against IL-2 and IL-2R may suppress immune responses and prevent rejection.


The Evidence IL-2 assay is a sandwich chemiluminescent assay for the detection of IL-2 in human serum and plasma.


1.  Tadatsugu, T. et al, Structure and exression of a cloned cDNA for human interleukin-2. Nature. 1983; 302(5906): 305-310.

2.  Waldmann, T.A., The IL-2/IL2 receptor system: a target for rational immune intervention. Immunol. Today. 1993; 14(6): 264-270

3.  Honda, M. et al, Identification of a soluble IL-2 receptor beta-chain from human lymphoid cell line cells. J. Immunol. 1990; 145(12): 4131-4135

4.  Hatakeyama, M. et al, Peptide growth factors and their receptors.  Sporn , MB and Roberts, AB (eds.), Springer-Verlag , New York . 1990; PP523

5.  Goldsmith, M.A. et al, The cytokine Handbook, second edition, Thomson, Academic education, Academic Press, New York . 1994; PP57.

6.  Mossman, T.R. et al, TH1 and TH2 cells:different patterns of lymphokine secretion lead to different functional properties. Annual Review of Immunology. 1989; 7: 145-173.

7.  Pericle, F. et al, Interleukin-2 prevention of apoptosis in human neutrophils. European Journal of Immunology. 1994; 24(2): 440-444

8.  Nakanishi, K. et al, Role and regulation of interleukin (IL-2) receptor alpha and beta chains in IL-2 driven B cell growth. Proc. Natl. Acad. Sci. USA. 1992; 89(8): 3551-3335

9.  Yang SC et al, Clinical and immunomodulatory effects of combination immunotherapy with low-dose interleukin-2 and tumor necrosis factor alpha in patients. Cancer Research. 1991; 51(14): 3669-3676

10. Farrar, J.J. et al, The biochemistry, biology, and role of interleukin 2 in the induction of cytotoxic T cell and antibody forming B cell responses. Immunol. Rev. 1982; 63:129-166

11. Howard, M et al, Interleukin 2 induces antigen-reactive T cell lines to secrete BCGF-I. J. Exp. Med. 1983; 158(6) 2024-2039

12. Nistico, G., Communications among central nervous system, neuroendocrine and immune systems: Interleukin-2. Progress in Neurobiology. 1993; 40(4): 463-475

13. Eitan, S et al, Recovery of visual response of injured adult rat optic nerves treated with transglutaminase. Science. 1994; 264(5166): 1764-1768

14.       Waguespack, P.J. et al, Interleukin-2 does not cross the blood-brain barrier by a saturable transport system. Brain Research Bulletin. 1994; 34(2): 103-109.

15. Kirkman, R.A. et al, Administration of an anti-interleukin 2 receptor monoclonal antibody prolongs cardiac allograft survival in mice. J. Exp. Med. 1995; 162(1): 358-362

16. Rubin J.T., Interleukin 2: its biology and clinical applications in patients with cancer. Cancer Invest. 1993; 11(4): 460-472

Interleukin-4 (IL-4) Assay

Intended Use

The Evidence Interleukin-4 (IL-4) assay has been designed for the quantitative measurement of IL-4 in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

IL-4 is a glycoprotein synthesized as a precursor protein of 153 amino acids.  The first 24 amino acid residue signal peptide is cleaved to produce a 129 amino acid 15-19 kDa protein((1)).  IL-4 has two glycosylation sites at two arginine residues and contains six cysteine residues involved in disulphide bond formation, which are essential for biological activity. It exerts biological activity through a high affinity receptor expressed by cells of hemopoietic lineage.  The IL-4 receptor is produced as an 825 amino acid precursor glycoprotein that is cleaved to produce a mature protein of 800 amino acids which in turn has a 24 amino acid transmembrane domain, a 569 amino acid intracellular domain and a 207 amino acid extracellular domain((2,3)).

IL-4 is produced by activated T-cells, mast cells, eosinophils and peripheral basophils and its synthesis is induced by IL-2 and PAF and inhibited by TGFβ. IL-4 induces T cell differentiation and inhibits T cell cytokine production((4)). It also enhances the proliferation and differentiation of activated B-cells((5)). A further role of IL-4 is in the induction of IgE synthesis by B cells((6)) and the expression of class II MHC antigens.  IL-4 has also been shown to inhibit activation and proliferation of NK cells induced by IL-2 and inhibits the IL-2 dependant generation of LAK cells((7,8)). IL-4 also inhibits the synthesis of IL-1, IL-6, IL-8, IL-10, IL-12 and TNFα in macrophages((9)) and promotes proliferation of mast cells and enhances respiratory burst and phagocytic properties of neutrophils((10)). IL-4 is a chemoattractant for fibroblasts and induces the production of extracellular matrix proteins ((11)) and also induces proliferation of capillary endothelial cells ((12)).

IL-4 could possibly be an autocrine growth modulator for Hodgkin’s lymphomas, and disorders such as asthma produce IL-4((13)). IL-4 may be of clinical importance in the treatment of chronic inflammatory diseases, such as rheumatoid arthritis, and autoimmune disorders. It may also be useful in the treatment of solid tumours, of hematopoietic systemic diseases, and of immune defects((14)).


The Evidence IL-4 assay is a sandwich chemiluminescent assay for the detection of IL-4 in human serum and plasma.


1.  Yokota, T. et al, Isolation and characterisation of a human interleukin cDNA clone, homologous to mouse B-cell stimulatory factor 1.  Proceedings of the National Academy of Science. 1986; 83(16): 5894-5898

2.  Howard, M. et al, Guidebook to cytokines and their receptors. Oxford University Press, New York , 1994; 44

3.  Banchereau, J. et al, The Cytokine Handbook. Second edition. Thomson, A. (ed), Academic Press, New York . 1994; 99

4.  Barcena, A et al, A role for interleukin 4 in differentiation of mature T cell receptor gamma/delta + cells from human intrathymic T cell precursors. J. Exp. Med. 1990; 172(2): 439-446

5.  Karray, S. et al, Interleukin-4 counteracts the Interleukin-2-induced proliferation of monoclonal B cells. Journal of Experimental Medicine. 1988; 168(1): 85-94

6.  Geha, R. S. et al, Regulation of IgE synthesis in humans, Journal of Allergy Clinical Immunology. 1992; 90: 143-150

7.  Spits, H. et al, IL4 inhibits IL2 mediated induction of human lymphokine activated killer cells, but not the generation of antigen specific cytotoxic T lymphocytes in mixed leukocyte cultures. J. Immunol. 1988; 141:29-36

8.  Kawakami, Y. et al, IL4 regulates IL2 induction of lymphokine activated killer activity from human lymphocytes. J. Immunol. 1989; 142(10): 3452-3461

9.  Hart, P.H et al, Potential anti-inflammatory effects of interleukin 4: suppression of human monocytes, tumour necrosis factor alpha, interleukin 1 and prostaglandin E2. Proc. Natl. Acad. Sci. USA. 1989; 86(10): 3803-3807

10. Boey, H. et al, Interleukin 4 is a neutrophil activator. J. Allergy Clin. Immunol. 1989; 83(5): 978-984

11. Postlethwaite, A.E. et al, Human fibroblasts synthesize elevated levels of extracellular matrix proteins in response to interleukin 4. J. Clin. Invest. 1992; 90(4): 1479-1485

12. Toi, M. et al, Inhibition of colon and breast carcinoma cell growth by interleukin 4. Cancer Res. 1992; 52(2): 275-2799

13. Parronchi, P. et al, Allergen and bacterial antigen-specific T cell clones established from atopic donors show a different profile cytokine production. Proceedings of the National Academy of ScienceUSA . 1991; 88: 4538-4542

14.Obiri, N.I. et al, Expression of high affinity interleukin 4 receptors on human renal cell      carcinoma cells and inhibition of tumour cell growth in vitro by interleukin 4. J. Clin. Invest. 1993; 91(1): 88-93

Interleukin-6 (IL-6) Assay

Intended Use

The Evidence Interleukin-6 (IL-6) test has been designed for the quantitative measurement of IL-6 in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures

Clinical Significance

IL-6 is synthesized as a precursor protein of 212 amino acids.  The N-terminal 28 amino acid residue signal peptide is cleaved to produce a 21kDa protein.  It has two potential N-glycosylation sites which have no effect on bioactivity((1)).  Different post-translational alterations such as glycosylation and phosphorylation give various forms of IL-6 with molecular masses of 21.5-28 kDa.  The IL-6 receptor is a strongly glycosylated 80 kDa protein of 449 amino acids. Two different forms of the receptor have been described that bind IL-6 with differing affinities, a soluble form of the IL-6 receptor has also been described. The IL-6 receptor is expressed on T cells, mitogen activated B cells, peripheral monocytes and some macrophage and B cell derived tumour cell types((2)).

IL-6 influences antigen-specific immune responses and inflammatory reactions. It is mainly produced by stimulated monocytes, fibroblasts and endothelial cells, but also by macrophages, T-cells, B-lymphocytes, hepatocytes, granulocytes, smooth muscle cells, eosinophils, chondrocytes, osteoblasts, mast cells, glial cells and keratinocytes after stimulation((2-5)). IL-6 stimulates differentiation and antibody secretion of B-cells((1)) and also initiates IL-2 production and IL-2 receptor expression.  It also activates T cells and in the presence of IL-2 induces differentiation. Production of acute phase proteins by hepatocytes is also stimulated by IL-6((6)) and colony-stimulating activity on hematopoietic stem cells ((7)).  Additional bioactivities include induction of neuronal cell differentiation((8)), induction of the maturation of megakaryocytes and inhibition of the growth and induction of terminal differentiation of M1 myeloid leukemia cells((9)). IL-6 may also function as a growth modulator of various tumour types, some of which secrete IL-6 constitutively. On the other hand it can also block the growth of some tumours.

Measurement of IL-6 serum levels may be useful in monitoring the activity of myelomas and to calculate tumour cell masses. Excessive over-production of IL-6 has been observed in rheumatoid arthritis, multiple myeloma, Lennert syndrome, Kawasaki disease, Castlemans disease, cardiac myxomas and liver cirrhosis((10-13)). Very high levels of IL-6 have also been observed in the cerebrospinal fluid of bacterial and viral meningitis patients.


The Evidence IL-6 assay is a sandwich chemiluminescent assay for the detection of IL-6 in human serum and plasma.


1.  Hirano, T. et al, Complementary DNA for a novel human interleukin (BSF-2) that induces B lymphocytes. Nature. 1986; 324(6092): 73-76

2.  Kishimoto, T. et al, Interleukin-6 and its receptors: a paradigm for cytokines. Science. 1992; 258(5082): 593-597

3.  Hirano, T. et al, Biological and clinical aspects of Interleukin-6.  Immunology Today. 1990; 11(12): 443-449

4.  Hirano, T., Interleukin-6 and its relation to inflammation and disease, Clinical Immunology and Immunopathology, 1992; 62(1/2): 60-65

5.  Hirano, T. et al, Peptide growth factors and their receptors 1, Sporn, MB and Roberts, AB (eds), Springer-Verlag, New York. 1990; PP663

6.  Baumann, H. et al, Human keratinocytes and monocytes release factors which regulate the synthesis of major acute phase proteins in hepatic cells from man, rat and mouse. Journal of Biological Chemistry. 1984; 259(11): 7331-7342

7.  Wong, G. et al, Stimulation of murine hemopoietic colony formation by human IL-6. Journal of Immunology. 1988; 140(9): 3040-3044

8.  Satoh, T. et al, Induction of neuronal differentiation in PC12 cells by B cell stimulatory factor 2/IL-6, Molecular Cell Biology, 1988; 8(8): 3546-3549

9.  Shabo, Y et al, The myeloid blood cell differentiation-inducing MG1-2A is interleukin-6.  Blood.  1988; 72(6): 2070-2073

10. Leger-Ravet , MB . Et al, Interleukin-6 gene expression in Castlemans disease. Blood. 1991; 78: 2923-2930

11. Hirano, T et al, Human B cell differentiation factor defined by an anti-peptide antibody and its possible role in autoantibody production. Proc. Natl. Acad. Sci. USA. 1987; 84(1): 228-231

12. Bhardwaj, N et al, IL-6/IFN beta 2 in synovial effusions of patients with rheumatoid arthritis and other arthritides. Identification of several isoforms and studies of cellular sources. J. Immunol. 1989; 143(7): 2153-2159

13.  Kawano, M et al, Autocrine generation of requirement of BSF/IL6 for human multiple myelomas. Nature. 1988; 332(6159): 83-85

Interleukin-8 (IL-8) Assay

Intended Use

The Evidence Interleukin-8 (IL-8) assay has been designed for the quantitative measurement of IL-8 in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

IL-8 is a member of a structurally similar family of cytokines called chemokines, which demonstrate chemotactic activity for neutrophils. IL-8 is a non-glycosylated protein of 8 kDa and consists of 99 amino acids with a 22 residue signal peptide that is cleaved to generate a 77 amino acid sequence.  Proteases yield N-terminal variants.  It can form non-covalent dimers, but they are not necessary for biological activity((1)). Two classes of IL-8 receptors have been identified; CXCR-1 and CXCR-2, which are 7-transmembrane, G-protein-coupled receptors. One has high affinity for IL-8 and other chemokines and one has high affinity for IL-8 and low affinity for other chemokines((2)).

IL-8 is produced in response to proinflammatory stimuli.  It is produced by monocytes, macrophages, fibroblasts, endothelial cells, keratinocytes, melanocytes, hepatocytes, chondrocytes, T-cells, neutrophils, and astrocytes((3-8)). It activates neutrophil granulocytes ((9)) and antagonizes IgE production by B-cells((10)).  IL-8 is chemotactic for all known types of migratory immune cells and possesses anti-inflammatory activities.  It enhances metabolism of reactive oxygen species and increases chemotaxis and enhanced expression of adhesion molecules. 

Chemokines are important for the recruitment of leukocytes to site of infection, however the accumulation of leukocytes can contribute to several disorders such as glomerulonephritis, rheumatoid arthritis and ischemia-reperfusion-induced injury. IL-8 has also been detected in bodily fluids and tissues of patient with psoriasis, dermatitis, fibrosis, asthma, artherosclerosis, septic shock, meningitis, multiple sclerosis and many other pathological conditions.


The Evidence IL-8 assay is a sandwich chemiluminescent assay for the detection of IL-8 in human serum and plasma.


1.  Schmid, J. et al, Induction of mRNA for a serine protease and a Beta-thromoglobulin-like protein in mitogen-stimulated human leukocytes. Journal of Immunology. 1987; 139: 250-256

2.  Holmes, WE et al, Structure and functional expression of a human interleukin 8 receptor. Science. 1991: 253: 1278-1280

3.  Oppenheim, J. et al, Properties of the novel proinflammatory supergene ‘intercrine’ cytokine family.. Annual Review of Immunology. 1991; 9: 617-648

4.  Miller, M.D. et al, Biology and biochemistry of the chemokines: a family of chemotactic and inflammatory cytokines. Critical Review of Immunology. 1992; 12(1/2): 17-46

5.  Matsushima, K. et al, Interleukin-8 and MCAF: novel leukocyte recruitment and activating cytokines. Chemical Immunology. 1992; 51: 236-265

6.  Taub, D.D. et al, Review of the chemokine meeting: The Third International Symposium of Chemotactic Cytokines. Cytokine. 1993; 5(3): 175-179

7.  Vaddi, K. et al, The Chemokine Facts Book. Academic Press, 1997; PP23

8.  Hack, C.E. et al, Role of cytokines in sepsis. Advanced Immunology. 1997; 66: 101-195

9.  Baggiolini, M. et al, Neutrophil-activating peptide-1/Interleukin-8, a novel cytokine that activates neutrophils. Journal of Clinical Investigation. 1989; 84(4): 1045-1049

10.       Kimata, H. et al, Interleukin-8 selectively inhibits immunogloblin E production induced by IL-4 in human B cells. Journal of Experimental Medicine. 1992; 176(4): 1227-1231

Interleukin-10 (IL-10) Assay

Intended Use

The Evidence Interleukin-10 (IL-10) test has been designed for the quantitative measurement of IL-10 in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

Interleukin-10 (IL-10), alternatively known as B-cell-derived T-cell growth factor (B-TCGF), cytokine synthesis inhibitory factor (CSIF) or T-cell growth inhibitory factor is a homodimeric protein with a molecular weight of 18 kDa. It is produced as a 178 amino acid residue precursor, which is cleaved to give a mature protein of 160 amino acids. It also has two intrachain disulphide bonds, which are required for activity((1)). Receptors for IL-10 are all transmembrane glycoproteins about 110 kDa in size. The IL-10 receptor binds to its ligand with high affinity and it has been observed that most hemopoietic cells express them at low levels((2)).

IL-10’s primary function is as an anti-inflammatory agent, which inhibits cytokine production by T cells and natural killer cells caused by activation of monocytes/macrophages((3)).  IL-10 strongly inhibits the production of IL-1α, IL-1β, IL-6, IL-8, IL-10, IL-12, GM-CSF, G-CSF, M-CSF, TNFα, MIP-1α, MIP-2, RANTES and LIF by activated monocytes/macrophages((4)). It also inhibits the ability of monocytes/macrophages to modulate turnover of extracellular matrix((5)). It initiates growth and differentiation of B cells and induces histamine release by mast cells. IL-10 also expresses an anti-inflammatory response on neutrophils and an immunosuppressive effect on dendritic cells ((6,7)).

Certain tumour cell lines including melanomas and a variety of carcinomas produce IL-10 ((8)) and it is also produced during septicemia and septic shock((9,10)). IL-10 is involved in development of inflammatory bowel disease((11)). Expression of IL-10 is detected in patients with multiple sclerosis and it has been suggested that it could potentially be a useful therapeutic agent for this disease((12)). IL-10 also contributes to immunosuppression seen in many infectious diseases such as Leprosy, Malaria and HIV, which show increased IL-10 production((13,14)). IL-10 alone and synergistically with IL-4 has been seen to reduce various symptoms observed with acute and chronic arthritis((15)) and daily administration of IL-10 inhibits spontaneous onset of insulin dependant diabetes mellitus in mice((16)).


The Evidence Il-10 assay is a sandwich chemiluminescent assay for the detection of Il-10 in human serum and plasma samples.


1.  Windsor, W.T. et al, Disulfide bond assignments and secondary structure analysis of human and murine interleukin 10. Biochemistry. 1993; 32(34): 8807-8815

2.  Wang, M. et al, Interleukin 24 (MDA-7/MOB-5) signals through two heterodimeric receptors, IL22R1/IL20R2 and IL20R1/IL20R2. J. Biol. Chem. 2002; 277(9): 7341-7347

3.  Moore , K.W. et al, Interleukin 10. Annu. Rev. Immunol. 1993; 11: 165-190

4.  de Waal Malefyt, R. et al, Interleukin 10 inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL10 produced by monocytes. J. Exp. Med. 1991a; 174(5): 1209-1220

5.  Lacraz, S. et al, IL10 inhibits metalloproteinase and stimulates TIMP-1 production in human mononuclear phagocytes. J. Clin. Invest. 1995; 96(5): 2304-10

6.  Wang, P. et al, Interleukin 10 inhibits interleukin 8 production in human neutrophils. Blood. 1994; 83(9): 2678-2683

7.  Wang, B. et al, Enhanced epidermal Langerhans cell migration in IL10 knockout mice. J. Immunol. 1999; 162(1): 277-283

8.  Drummer, W. et al, Interleukin 10 production in malignant melanoma: preferential detection of IL10 secreting tumour cells in metastatic lesions. Int. J. Cancer. 1996; 66(5): 607-610

9.  Marchant, A. et al. Interleukin 10 production during septicaemia. Lancet. 1994b; 343(8899): 707-708

10. Marchent, A. et al. Clinical and biological significance of interleukin 10 plasma levels in patients with septic shock. J. Clin. Immunol. 1995; 15(5): 266-273

11. Powrie, F. T cells in inflammatory bowel disease: protective and pathogenic roles. Immunity. 1995; 3(2): 171-174

12. Navickas, V. et al. Increased mRNA expression of IL10 in mononuclear cells multiple sclerosis and optic neuritis. Scand. J. Immunol. 1995; 41(2): 171-178

13.  Sieling, P.A. et al. Immunosuppressive roles for IL10 and IL4 in human infection. In vitro modulation of T cell responses in leprosy. J. Immunol. 1993; 150(12): 5501-5510

14. Peyron, F. et al. High levels of circulating IL10 in human malaria. Clin. Exp. Immunol. 1994; 95(2): 300-3

15. Joosten , LA. et al. Role of interleukin 4 and interleukin 10 in murine collagen induced arthritis. Protective effect of interleukin 4 and interleukin 10 treatment on cartilage destruction. Arthritis Rheum. 1997; 40(2): 249-260

16. Pennline, K.J. et al, Recombinant human IL10 prevents the onset of diabetes in the non-obese diabetic mouse. Clin Immunol. Immunopathol. 1994; 71(2): 169-175

Tumour Necrosis Factor α (TNFα) Assay

Intended Use

The EvidenceTumour Necrosis Factor (TNFa) assay has been designed for the quantitative measurement of TNFa in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

Tumour necrosis factor alpha (TNFα) is a 157 amino acid 26 kDa transmembrane protein which is secreted as a soluble mature 233 amino acid homotrimer of 17 kDa by proteolytic cleavage. Both forms of TNFα are biologically active. TNFα shares a 34% amino acid residue homology with TNFβ and binds to the same receptors and exhibits similar biological activity((1,2)). There are two distinct structurally homologous TNF receptors, which bind to both TNFα and TNFβ with high affinity; TNFR1 and TNFR2((3)). At least one receptor is expressed on nearly all cell types and soluble forms have been found in serum and urine ((4)).

TNFα has a role in host resistance to infection as a mediator of immune and inflammatory responses((5)). Various immune cells such as macrophages, monocytes, neutrophils, T cells and natural killer cells, following stimulation by lipopolysaccharide, secrete TNFα((1,6)).  Synthesis of TNFα is induced by interferons, IL-2, GM-CSF, SP, bradykinin, immune complexes, inhibitors of cyclooxygenase and PAF. TNFα production is inhibited by IL-6, TGFβ, VitD3, prostaglandin E2, dexamethasone, cyclosporin A, and antagonists of PAF((7)).

Increased production of TNFα leads to cachexia, septic shock following infection by gram-negative bacteria, autoimmune disorder and meningococcal septicemia((8,9)). Increased levels of TNFα are also seen in multiple sclerosis, rheumatoid arthritis, brain injury, meningococcal meningitis, HIV, and Alzheimers ((10-13)). Patients with advanced heart failure also exhibit high levels of TNFα((14)). TNFα is involved in the growth of malignant tumours and has been investigated as an antitumour drug but its use has been limited due to its systemic toxic side effects((15)). Anti TNFα has been shown to decrease inflammation in ulcerative colitis and is also useful in the treatment of sepsis and rheumatoid arthritis((9)).


The Evidence TNFα assay is a sandwich chemiluminescent assay for the detection of TNFα in human serum and plasma.


1.  Vilcek, J. and Lee, TH., Tumour necrosis factor. New insights into the molecular mechanisms of its multiple actions. J. Biol. Chem. 1991; 266(12): 7313-7316

2.  Jones, E.Y. et al, Structure of tumour necrosis factor. Nature. 1989; 338: 225-228

3.  Smith, R.A. and Baglioni, C.J., Characterisation of TNF receptors. Immunol. Ser. 1992; 56: 131-147

4.  Engelmann, H. et al, Two tumour necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumour necrosis factor receptors. J. Biol. Chem. 1990b; 265: 1531-1536

5.  Beutler, B. and Cerami, A., The biology of cachectin/TNF-a primary mediator of the host response.   Annu. Rev. Immunol. 1989; 7: 625-655

6.  Ruddle , N.H. , Tumour necrosis factor (TNF-alpha) and lymphotoxin (TNF-beta). Curr. Opinion. Immunol. 1992; 4(3): 327-332

7.  Bonavida, B., Immunomodulatory effect of tumour necrosis factor. Biotherapy. 1991; 3: 127-133

8.  Waage, A. et al, The complex pattern of cytokines in serum from patients with meningococcal septic shock. Association between interleukin 6, interleukin 1, and fatal outcome. J. Exp. Med. 1989a; 169: 333-338.

9.  Waage, A. et al, Association between tumour necrosis factor necrosis factor in serum and fatal outcome in patients with meningococcal disease. Lancet. 1987; 1(8528): 355-357

10. Sharief, M.K. et al, Association between tumour necrosis factor alpha and disease progression in patients with multiple sclerosis. New Engl. J. Med. 1991; 325(7): 467-472

11. Waage, A. et al, Local production of tumour necrosis factor α, interleukin 1, and interleukin 6 in meningococcal meningitis. Relation to the inflammatory response. J. Exp. Med. 1989b; 170: 1859-1867

12. Grimaldi, L.M. et al, Elevated α-tumour necrosis factor levels in spinal fluid from HIV-1 infected patients with central nervous system involvement. Ann. Neurol. 1991; 29: 21-25

13. Fillit, H. et al, Elevated circulating tumour necrosis factor levels in Alzheimer’s disease. Neurosci. Lett. 1991; 129: 318-320

14. Dutka, D.P. et al, Tumour necrosis factor α in severe congestive cardiac failure. Br. Heart J. 1993; 70: 141-143

15. Tsutsumi, Y. et al, Molecular design of hybrid tumour necrosis factor α with polyethylene glycol increases its anti-tumour potency. Br. J. Cancer. 1995; 71: 963-968

Monocyte Chemoattractant Protein-1 (MCP-1) Assay

Intended Use

The Evidence Monocyte Chemoattractant Protein-1 (MCP-1) assay has been designed for the quantitative measurement of MCP-1 in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

Monocyte chemoattractant protein (MCP-1) is part of the chemotactic family of cytokines called chemokines. MCP-1 is also known as monocyte chemotactic and activating factor (MCAF), lymphocyte derived chemotactic factor (LDCF) or glioma derived chemotactic factor (GDCF). It is a 76 amino acid peptide and has a molecular weight of 8.6 kDa. This family of chemokines consists of four sub families based on the position of their cysteine residues. MCP-1 is a member of the β or CC subfamily of chemokines((1)). Two isoforms of the MCP-1 receptor have been identified which have two different carboxy-terminal tails((2)).

MCP–1 is expressed by normal cells and tissues such as leukocytes, fibroblasts, endothelial cells, smooth muscle cells, epithelial cells, melanocytes, keratinocytes, chondrocytes, osteblasts, mesothelial cells and mesangial cells as well as by various tumour cells((1,3-9)). MCP-1 is a pro-inflammatory cytokine involved in immune and inflammatory responses. Its main role is as an activator and chemoattractant of monocytes ((10)), but it is also a chemoattractant for leukocytes, CD4+ and CD8+ lymphocytes and T lympohocytes((11)). MCP-1 stimulates degranulation and respiratory burst in monocytes and also acts as a chemoattractant and a stimulator of histamine release from basophills((12)). IL-1, TNFα, PDGF, TGFβ and LIF induce synthesis of MCP-1 in articular chondrocytes confirming its role in inflammatory responses((8)). MCP-1 has been implicated in a wide variety of inflammatory diseases such as artherosclerosis, delayed hypersensitivity reactions, rheumatoid arthritis, alveotitis and idiopathic pulmonary fibrosis((3)).

MCP-1 can enhance the ability of monocytes to inhibit growth of certain tumour cells and activates tumouricidal activity of monocytes and macrophages. MCP-1 also induces activation and proliferation of killer cells (C-C-Chemokine-activated killer). MCP-1 regulates the expression of cell surface antigens CD11c and CD11b and cytokines IL-1 and IL-6((13)).


The Evidence MCP-1 assay is a sandwich chemiluminescent assay for the detection of MCP-1 in human serum and plasma.


1.  Miller, M.D. and Krangel, M.S., Biology and biochemistry of the chemokines: a family of chemotactic and inflammatory cytokines. Critical Rev. Immunol. 1992; 12(1-2): 17-46

2.  Charo, I.F. et al, Molecular cloning and functional expression of two monocyte chemoattractant protein 1 receptors reveals alternative splicing of the carboxyl-terminal tails. Proc. Natl. Acad. Sci. USA 1994; 91(7): 3652-3656

3.  Yoshimura, T. et al, Human monocyte chemoattractant protein 1. Full length cDNA cloning, expression in mitogen-stimulated blood mononuclear leukocytes, and sequence similarity to mouse competence gene JE. FEEBS Let. 1989; 244(2): 487-493

4.  Van Damme, J. et al, Structural and functional identification of two human, tumour derived monocyte chemotactic proteins (MCP2 and MCP3) belonging to chemokine family. J. Exp. Med. 1992; 176(1): 59-65

5.  Colotta, F. et al, Expression of monocyte chemotactic protein 1 by monocyte and endothelial cells exposed to thrombin. Am J. Pathol. 1994; 144(5): 975-985

6.  Gillitzer, R. et al, MCP-1 mRNA expression in basal keratinocytes of psoriatic lesions. J. Invest. Dermatol. 1993; 101(2): 127-131

7.  Marra, F. et al, Cultured human liver fat storing cells produce monocyte chemotactic protein-1. Regulation by proinflammatory cytokines. J. Clin. Invest. 1993; 92(4): 1674-1680

8.  Villiger, P.M. et al, Monocyte chemoattractant protein 1 expression in human articular cartilage. Induction by peptide regulatory factors and differential effects of dexamethasone and retino acid. J. Clin. Invest. 1992; 90(2): 488-496

9.  Williams, S.R. et al, Regulated expression of monocyte chemoattractant protein in normal human osteoblastic cells. Am. J. Physiol. 1992; 263(1): 194-199

10.       Matsushima, K. et al, Purification and characterisation of a novel monocyte chemotactic and activating factor produced by a human myelomonocytic cell line. J. Exp. Med. 1989; 169(4): 1485-1490

11.       Loetscher, P. et al, Monocyte chemotactic proteins MCP-1, MCP-2 and MCP-3 are major attractants for human CD4+ and CD8+ T lymphocytes. The FASEB J. 1994; 8(13): 1055-1060

12.       Bischoff, S.C. et al, Monocyte chemotactic protein 1 is potent activator of human basophils J. of Expt. Med. 1992; 175(5): 1271-1275

13.       Biswas, S.K. and Sodhi, A., In vitro activation of murine peritoneal macrophages by monocytes chemoattractant protein 1: upregulation of CD11b, production of proinflammatory cytokines, and the signal transduction pathway. J. Interferon Cytokine Res. 2002; 22(5): 527-538

Vascular Endothelial Growth Factor (VEGF) Assay

Intended Use

The Evidence Vascular Endothelial Growth Factor (VEGF) assay has been designed for the quantitative measurement of VEGF in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF), is secreted as a glycosylated homodimeric protein of 46 kDa that is made up of two 24 kDa subunits linked by disulphide bonds. Various molecular variants of VEGF have been identified depending on splicing of the mRNA: 121, 145, 165, 189 and 206 amino acids ((1)). There are three receptors in the VEGF family; VEGFR1, expressed on endothelial cells, trophoblasts and macrophages mediates motility and vascular permeability. VEGFR2, expressed on endothelial cells, hemopoietic stem cells, megakaryocytes and retinal cells is essentially involved in proliferation. VEGFR3 is expressed specifically on lymphatic endothelium and is important for lymphatic proliferation ((2,3)).

VEGF is expressed by vascularised tissue such as pituitary, brain, lungs, kidneys, heart and adrenal glands, although it is assumed that all tissues have the potential to produce the growth factor((4)). VEGF is a specific mitogen and survival factor for endothelial cells and a key promoter of angiogenesis((1,5)). It also causes vasodilation, stimulates cell migration and inhibits apoptosis((6)). Synthesis of VEGF is stimulated when cells become deficient in oxygen or glucose or under inflammatory conditions((1)).

An increase in VEGF production has been observed in patients with preeclampsia, ischemic heart disease, sickle cell anemia, psoriasis, diabetes, rheumatoid arthritis, POEMS syndrome and Kawasaki disease((7-12)). Increased serum concentrations of VEGF have been observed in various types of cancer((13)). Drug development to block angiogenesis by interfering with VEGF function has been successful in many tumour treatments((14)). VEGF has also been used successfully in therapeutic angiogenesis in patients with end-stage coronary artery disease((15)).


The Evidence VEGF assay is a sandwich chemiluminescent assay for the detection of VEGF in human serum and plasma.


1.  Ferrara , N. and Davis-Smyth, T., The biology of the vascular endothelial growth factor (review). Endocr. Rev. 1997; 18: 4-25

2.  Neufeld, G. et al, Vascular endothelial growth factor VEGF and its receptors (review). FASEB J. 1999; 13: 9-22

3.  Shibuya, M. et al, Structure and function of vascular endothelial cell growth factor receptor-1 and –2. Curr. Top. Microbiol. Immunol. 1999; 237: 59-83

4.  Berse, B. et al, Vascular permeability growth factor gene is expressed differentially in normal tissues, macrophages and tumours. Mol. Biol. Cell. 1992; 3: 211-220

5.  Dvorak, H.F. et al, Vascular permeability factor/vascular endothelial growth factor, microvascular hyperpermeability, and angiogenesis (review). Am. J. Pathol. 1995; 18: 4-25

6.  Yang, R. et al, Effects of vascular endothelial growth factor on hemodynamics and cardiac performance.  J. Cardiovasc. Pharmacol. 1996; 27(6): 838-844

7.  Sharkey, A.M. et al, Maternal plasma levels of vascular endothelial growth factor in normotensive pregnancies and in pregnancies complicated by pre-eclampsia. Eur. J. Clin. Invest. 1996; 26: 1182-1185

8.  Seko, Y. et al, Serum levels of vascular endothelial growth factor in patients with acute myocardial infarction undergoing reperfusion therapy. Clin. Sci. (colch) 1997; 92: 453-454

9.  Solovey, A. et al, Sickle cell anemia as a possible state of enhanced anti-apoptotic tone: survival effect of vascular endothelial cell growth factor on circulating and unanchored endothelial cells. Blood. 1999; 93: 3824-3830

10.       McLaren, M., Elevated plasma vascular endothelial cell growth factor and thrombomodulin in juvenile diabetic patients. Clin Appl Thromb Hemost. 1999; 5: 21-24

11.       Soubrier, M. et al, Growth factors in POEMS syndrome: evidence for a marked increase in circulating vascular endothelial growth factor. Arthritis Rheum.  1997; 40: 786-7

12.       Terai, M., Vascular endothelial growth factor in acute Kawasaki disease. Am. J. Cardiol. 1999; 83: 337-339

13.       Kondo, S. et al, Vascular endothelial growth factor/vascular permeability factor is detectable in the sera of tumour-bearing mice and cancer patients. Biochem Biophys. Acta. 1994; 1221: 211-214

14.       Dachs, G.U. et al, Targeting gene expression to hypoxic tumour cells. Nat. Med. 1997; 3(5): 515-520

15.       Freedman, S.B. and Isner, J.M., Therapeutic angiogenesis for coronary artery disease (review). Annals of Int. Med. 2002; 136(1): 54-71

Epidermal Growth Factor (EGF) Assay

Intended Use

The Evidence Epidermal Growth Factor (EGF) assay has been designed for the quantitative measurement of EGF in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

Human EGF is produced as a long precursor protein of 1207 amino acids which is released by proteolytic cleavage to give a globular protein of 6.4 kDa consisting of 53 amino acids((1)). EGF contains three intramolecular disulfide bonds, which are essential for its biological activity. It is also known as Human Milk Growth Factor (HMGF), Prostatic Growth Factor (PGF) and Urogastone. EGF is produced by various organs including the brain, kidney, salivary gland and stomach, and is found in nearly all bodily fluids at low levels and at higher levels in saliva, milk, semen and urine((2)). 

EGF production is stimulated by progesterone and inhibited by oestrogen((1)) and is stored in platelets and released on degranulation((3)). It is mitogenic and chemotactic for epidermal and epithelial cells((2)) and also mitogenic for basal cells of olfactory epithelium and for endothelial cells and therefore plays an important role in angiogenesis((4)). EGF controls and stimulates proliferation of epidermal and epithelial cells such as fibroblasts, kidney epithelial cells, human glial cells, ovary granulosa cells and thyroid cells. It has been shown to act as a differentiation factor and increases turnover and synthesis of extra cellular matrix such as fibronectin, collagens, laminin and glycosaminoglycans. It may also influence the activity of GABAergic and dopaminergic neurons((5)).

EGF has various therapeutic applications such as the healing of burns, venous and diabetic ulcers, skin graft donor sites, corneal wounds, tympanic membrane perforations, gastric and duodenal ulcers and increasing sensitivity of malignancies to cytotoxic drugs((6,7)).

EGF has been shown to be elevated in patients with brain tumours and to induce differentiation in tumour cell lines. Also many epithelial cancers over-express the EGF receptor. Tumour aggressiveness is also associated with increased expression of EGF receptors. This expression is also high in invasive and disseminated tumours therefore many strategies to block the EGF receptor have been studied to inhibit tumour proliferation((8-11)). It has also been proposed that EGF plays an important role in male infertility, as there is a correlation between the level of circulating EGF, and the number of spermatids in the testis((12)).


The Evidence EGF assay is a sandwich chemiluminescent assay for the detection of EGF in human serum and plasma.


1.  Bell , G.I. et al, Human EGF precursor: cDNA sequence, expressed in vitro and gene organisation. Nucleic Acid Research. 1986; 14: 8427-8446

2.  Carpenter, G. and Wahl, M.I., “The Epidermal Growth Factor Family” in Peptide Growth Factors and Their Receptors I, Sporn MB . And Roberts AB. Eds. Springer-Verlag, New York . 1990; pp 69

3.  Pesonen, K. et al, Characterisation of material with epidermal growth factor immunoreactivity in human serum and platelets. J. Clin. Endocrin. Metab. 1989; 68(2): 486-491

4.  Schreiber, A.B. et al, Transforming growth factor alpha: a more potent angiogenesis mediator than epidermal growth factor. Science. 1986; 232(4755): 1250-1253

5.  Ferrari, G. et al, Epidermal growth factor exerts neuronotrophic effects on dopaminergic and GABAergic CNS neurons: Comparison with basic fibroblast growth factor. J. Neurosci. Res. 1991; 30: 493-497

6.  Schultz, G. et al, EGF and TGF-alpha in wound healing and repair. J. Cellular Biochem. 1991; 45(4): 436-452

7.  Gridley, D.S. et al, Pilot evaluation of cytokine levels in patients undergoing radiotherapy for brain tumour. Cancer Detection and Prevention. 1998; 22(1): 20-29

8.  Saloman, D.S. et al, Epidermal growth factor-related peptides and their receptors in human malignancies. Crit. Rev. Oncol. Hematol. 1995; 19: 183-232

9.  Sainsbury, J.R. Epidermal growth factor receptors in human breast cancer. Lancet I. 1985; 364-366

10.       Neal, D.E. Epidermal growth factor receptors in human bladder cancer: Comparison of invasive and superficial tumours. Lancet I. 1985; 366-368

11.       Modjahedi, H. et al, EGFR blockade by tyrosine kinase inhibitor or monoclonal antibody inhibits growth, directs terminal differentiation and induces apoptosis in human squamous cell carcinoma. Int. J. Oncol. 1998; 13: 335-342

12.       Tsutsumi, O. et al, A physiological role of epidermal growth factor in male reproduction function. Science. 1986; 223: 975-977

Interleukin-1α (IL-1α) Assay

Intended Use

The Evidence Interleukin-1a (IL-1a) assay has been designed for the quantitative measurement of IL-1a in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

Interleukin-1 (IL-1) is a regulatory and inflammatory cytokine, which exists in two forms, IL-1a and IL-1b, which share 25% homology at amino acid level.  IL-1α is produced as a biologically active 31 kDa precursor, which undergoes proteolytic cleavage yielding a 17 kDa protein of 159 amino acids.((1, 2))  There are two cell surface binding proteins for IL-1 expressed on various cells, IL-1R1 and IL-1R2, and one non-binding receptor accessory protein IL-1-Racp. IL-1a and IL-1b bind to both receptor types but IL-1a binds better to IL-1R1 than IL-1R2.  IL-1Ra is an 80 kDa glycoprotein, which has been isolated from T-cells, fibroblasts, keratinocytes, endothelial cells, synovial lining cells, chondrocytes and hepatocytes and IL-1R2 has been found in B-cells, neutrophils and bone marrow cells((3)).

In healthy people cells of the central nervous system, some epithelial cells and skin keratinocytes produce IL-1α. It is also produced by macrophage and many other cell types in response to stimuli by inflammatory agents, infections or microbial endotoxins.((2, 3) )IL-1 has been shown to induce synthesis of endothelial cell-surface factors and activate endothelial cells.((4)  )In the liver, it initiates an increase in hepatic protein synthesis and decreased albumin production.((5))  IL-1 also induces collagenase production((6)) and has been found to be chemotactic and stimulatory for neutrophils.((7)  )IL-1 also affects the endocrine system and is mitogenic for B-lymphocytes.((8))  It also plays an important role in immune functions by activating macrophages, NK cells and T-cells((9)) and by inducing B-cell proliferation and maturation and LAK production.((10))

IL-1α is not commonly found circulating except during severe disease where the cytokine is released from dying cells.((11) )Colonic tissue levels of IL-1α correlate to severity of inflammatory bowel disease.((12)) IL-1 production is increased in sepsis, rheumatoid arthritis, leukemia, diabetes and artherosclerosis.((3,13) )IL-1a and IL-1b were also found to induce fever.((14))


The Evidence IL-1a assay is a sandwich chemiluminescent assay for the detection of IL-1a in human serum and plasma.


1.  Bazan, J.F. et al, A newly defined interleukin-1? Nature. 1996; 379: 391

2.  Gubler, U. et al, Recombinant human interleukin-1-a: purification and biological characterisation. Journal of Immunology. 1986; 136(7): 2492-2497

3.  Dinarello, C.A., Interleukin-1 and interleukin-1 antagonism. Blood. 1991; 77(8): 1627-1652

4.  Bevilacqua, M.P. et al, Recombinant TNF induces procoagulant activity in cultured human vascular endothelium. Proceedings of the national Academy of Science. 1986; 83(12): 4533-4537

5.  Ramadori, G. et al, Pretranslational modulation of acute phase hepatic protein synthesis by murine recombinant IL-1 and purified human IL-1. Journal of Experimental Medicine. 1985; 162(3): 930-942

6.  Dayer, J.M. et al, Human recombinant IL-1 stimulates collagenase and prostaglandin E2 production by human synovial cells. Journal of Clinical Investigation. 1986; 77(2): 645-648

7.  Kampschmidt, R.F. et al, Neutrophil release after injections of endotoxin or leukocytic endogenous mediator into rats. Journal of Reticuloendothelium society. 1980; 28(2): 191-201

8.  Chiplunkar, S. et al, Stimulation of B cell growth and differentiation by murine recombinant IL-1. Journal of Immunology. 1986; 137(12): 3748-3752

9.  Kaye, J. et al, Induction of receptors for Il-2 requires T cell Ag:Ia receptor crosslinking and interleukin 1. Lymphokine Research. 1984; 3(4): 175-182

10.       Aribia, M.B. et al, rIL 2-induced proliferation of human circulating NK cells and T lymphocytes: synergistic effects of IL 1 and IL 2. Journal of Immunology. 1987; 139(2): 443-451

11.       Wakabayaski, G. Staphylococcus epidermidis induces complement activation, tumour necrosis factor and interleukin-1, a shock-like state and tissue injury in rabbits without endotoxemia. J. Clin. Invest. 1991; 87: 1925-1935

12.       Cominelli, F. et al, Interleukin-1 gene expression, synthesis and effect of specific IL-1 receptor blockade in rabbit immune complex colitis. J. Clin. Invest. 1990; 86: 972-980

13.       Dinarello ,C.A. and Wolff SM. The role of interleukin-1 in disease. New Engl. J. Med. 1993; 328: 106

14.       Dinarello ,C.A. , An update on human IL-1 from molecular biology to clinical relevance. Journal of Clinical Immunology. 1985; 5(5): 287-297

Interleukin-1β (IL-1β) Assay

Intended Use

The Evidence Interleukin-1b (IL-1b) test has been designed for the quantitative measurement of IL-1b in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

There are two forms of IL-1, IL-1a and IL-1b, which share 25% homology at amino acid level. IL-1b is synthesized as a biologically inactive precursor of 269 amino acids with a molecular mass of 31 kDa, which undergoes proteolytic cleavage by IL1β converting enzyme (ICE), which yields a 17kDa protein of 153 amino acids((1,2)).

There are two cell surface binding proteins for IL-1 expressed on various cells, IL-1R1 and IL-1R2, and one non-binding receptor accessory protein IL-1-Racp. IL-1a and IL-1b bind to both receptor types but IL-1β has a higher affinity for IL-1R2 than IL-1R1.  IL-1RI has been isolated from T-cells, fibroblasts, keratinocytes, endothelial cells, synovial lining cells, chondrocytes and hepatocytes and IL-1R2 has been found in B-cells, neutrophils and bone marrow cells((3)).

IL-1β plays a central role in acute and chronic inflammation, both locally and systemically. It is produced by monocytes, macrophages, astrocytes, oligodendroglia, adrenal cortical cells, NK cells, endothelial cells, keratinocytes, platelets, neurons, neutrophils, oesteoblasts, Swhwann cells, trophoblasts and fibroblasts and affects nearly every cell type((4)). IL-1 activates macrophages((5)), induces fibroblast proliferation((6)), and induces expression of matrix metalloproteinases, leading to extracellular matrix degradation, monocyte migration and degradation of IL-1β, which acts as a negative feedback mechanism((7,8)).

IL-1 has a cytotoxic effect on normal cells and the IL-1β form is growth-inhibitory and cytocidal for certain melanoma cells.   IL-1b has been shown to inhibit insulin release and reduce the insulin and glucagons content of islets and therefore may play a role in the development of autoimmune insulin-dependent (type 1) diabetes mellitus((9)).  It is also involved in bone remodelling by stimulating bone resorption and inhibiting bone collagen synthesis((10)). The production of IL-1b is increased in sepsis, rheumatoid arthritis, leukemia, diabetes and artherosclerosis((3,11)).


The Evidence IL-1b assay is a sandwich chemiluminescent assay for the detection of IL-1b in human serum and plasma.


1.  March, C. J. et al, Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs. Nature. 1985; 315(6021): 641-647

2.  Thornberry, N. A. et al, A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature. 1992; 356(6372): 768-774

3.  Dinarello, C.A., Interleukin-1 and interleukin-1 antagonism. Blood. 1991; 77(8): 1627-1652

4.  Wewers, M.D. et al, IL-1 beta-converting enzyme (ICE) is present and functional in human alveolar macrophages: macrophage IL-1 beta release limitation is ICE independent. Journal of Immunology. 1997; 159(12): 5964-5972

5.  Billiau, A., Interferon-gamma: biology and role in pathogenesis. Advanced Immunology.1996; 62: 61-130

6.  Gaffney, E.V. et al, Lymphocyte-activating and growth-inhibitory activities for several sources of native and recombinant IL-1. Cancer Research. 1986; 46(8): 3834-3837

7.  Ito, A. et al, Degradation of interleukin-1-beta by matrix metalloproteinases. Journal of Biological Chemistry. 1996; 271(25): 14657-14660

8.  Plata-Salaman, C.R. et al, Interleukin-1beta-induced modulation of the hypothalamic IL-1beta system, tumour necrosis factor-alpha, and transforming growth factor-beta-1 mRNAs in obese (fa/fa) and lean (Fa/Fa) Zucker rats: implications to IL-1beta feedback systems and cytokine-cytokine interactions. Journal of Neuroscience Research. 1997; 49(5): 541-550

9.  Bendtzen, K. et al, Cytotoxicity of human pI 7 interleukin-1 for pancreatic islets of langerhans. Science. 1986; 232(4757): 1545-1547

10.       DeWhirst, F.E. et al, Purification and partial sequence of human osteoclast-activating factor: Identity with interleukin-1-beta. Journal of Immunology. 1985; 135(4): 2562-2568

11.       Dinarello CA. and Wolff SM. The role of interleukin-1 in disease. New Engl. J. Med. 1993. 328: 106

Interferon γ (IFNγ) Assay

Intended Use

The Evidence Interferon Gamma (IFNg) assay has been designed for the quantitative measurement of IFNg in human serum or plasma samples. This test is for research use only. Not for use in diagnostic procedures.

Clinical Significance

Biologically active interferon gamma (IFNγ) is a 20 or 25 kDa glycoprotein depending on its glycosylation state((1)). This lymphokine is synthesized as a 166 amino acid sequence but is cleaved to give a 143 amino acid residue with low sequence homology to IFNα or β((2)). It binds to a single chain 90 kDa glycoprotein receptor that has a high degree of specificity and is expressed on all types of human cells((3)). Binding of IFNγ to its receptor induces expression of various proteins specific to IFNγ stimulation((4)).

IFNγ is produced by mitogen activated T lymphocytes and natural killer cells and its main role is its involvement in the regulation of immunological functions essential to host defence mechanisms((5)). It has anti-viral and antiparasitic properties. It modulates growth and differentiation of T lymphocytes and influences cell-mediated mechanisms of cytotoxity. It increases macrophage-mediated killing of extra-cellular parasites and inhibits viral replication((6)). IL2, bFGF and EGF induce IFNγ synthesis in T lymphocytes. Knock out studies have shown that IFNγ is not essential for the development of the immune response but is essential for resistance to viral infections((7)).

IFNγ decreases clinical symptoms in severe atopic dermatitis((8)). It also decreases joint pain and is effective in the treatment of chronic polyarthritis((9)). Treatment of malignancies by IFNγ has been disappointing but combination treatment with other interferons has been more successful((10)). IFNγ may also be useful in the treatment of infections in immunosuppressed patients((11)). Decreased levels of IFNγ are observed in acute and asymptomatic asthma and are associated with severe airway obstructions((12)). Cells derived from the skin and peripheral blood supply of cutaneous T cell lymphoma patients have depressed levels of IFNγ((13)). Studies have also observed an age related increase in IFNγ production((14)).


The Evidence IFNg assay is a sandwich chemiluminescent assay for the detection of IFNg in human serum and plasma.


1.  Zoon, K.C., Human interferons: structure and function. Interferon. 1987; 9: 1-12

2.  DeGrado, W.F. et al, Sequence and structural homologies among type I and type II interferons. Nature. 1982; 300(5890): 379-381

3.  Fischer, D.G. et al, Two molecular forms of the human interferon gamma receptor. Ligand binding, internalisation, and down regulation. J.Biol. Chem. 1988; 263(6): 2632-2637

4.  Weil, J. et al, A unique set of polypeptides is induced by gamma interferon in addition to those induced in common with alpha and beta interferons. Nature. 1983; 301(5899): 437-439

5.  Celis, E. et al, Isolation and characterisation of human T cell lines and clones reactive to rabies virus: antigen specificity and production of interferon gamma. J. Immunol. 1986; 136(2): 692-697

6.  Ijzermans, J.M. and Marquet, R.L., Interferon-gamma: a review. Immunobiol. 1989; 179(4-5): 456-473

7.  Weck, K.E. et al, Murine gamma herpesvirus 68 causes severe large vessel arteritis in mice lacking interferon gamma responsiveness: a new model for virus-induced vascular disease. Nature Med. 1997; 3: 1346-1353

8.  Wang, L.F. et al, Local but not systemic administration of IFN-gamma during the sensitisation phase protein antigen immunization to suppress Th2 development in a murine model of atopic dermatitis. Cytokine. 2002; 19(3): 147-152

9.  Fierlbeck, G. and Rassner, G., Gamma interferon in psoriatic arthritis. Dtsch. Med. Wochenschr. 1986; 111(35): 1313-1316

10.       Einhorn, S. and Stander, H., Interferon treatment of human malignancies – a short review. Med. Oncol. Tumour Pharmacother. 1993; 10(1-2): 25-29

11.       Douglas , M.S. et al, Blockade of the interaction between interferon-gamma and endothelial glycosaminoglycans: a novel strategy for immunosuppression. Transplant Proc. 1997; 29(1-2): 1086-1088

12.       Lee, Y.C. et al, Serum levels of IL4, IL5, IL13 and IFNγ in acute asthma. J. of Asthma. 2001; 38(8): 665-71

13.       Vowels, B.R. et al, Th2 cytokine mRNA expressed in skin in cutaneous T cell lymphoma. J. Invest. Dermatol. 1994; 103: 669-673

14.       Rea, I.M. et al, CD69, CD25, and HLA-DR activation antigen expression of CD3+ lymphocytes and relationship to serum TNFα, IFNγ and sIL2R levels in aging. Exp. Gerontol. 1999; 34(1): 79-93

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