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Cytokine array iv

Product Method Size Catalog Price
Cytokine array iv B A T (evidence®) 4x45 (180 biochips) EV3659 POA
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INTENDED USE

The Evidence Cytokine Array IV is to be used for the in vitro simultaneous quantitative detection of multiple related cytokine immunoassays (in parallel) from a single human serum sample run on the automated biochip array analyzer, Evidence.

The Evidence Cytokine Array IV is for research use only and not for diagnostic procedures.

CLINICAL SIGNIFICANCE

Cytokine research has been performed by scientists in a multiplicity of fields so that now the field of cytokine research can be considered unique and interdisciplinary. The role of cytokines in the regulation of immune and inflammatory responses is clearly recognized with continuing cytokine research leading to their implication in other pathological conditions(1,2). This means that knowledge of the complexity of the cytokine network is critical in understanding normal and pathological processes.

An important part of the cytokine network belongs to the cytokine receptors, which exist in membrane bound and soluble forms. Often the soluble forms of the receptors bind their ligands with comparable affinity to the membrane bound receptor and can act as either antagonist or agonists(3). Therefore an understanding of cytokine receptor biology is essential in cytokine research.

Another major class of molecules that are functionally linked to certain cytokines are the proteases, which include the matrix metalloproteinases (MMPs)(4). MMPs play a central role in many biological processes and their strict regulation is critical in order to maintain extracellular matrix homeostasis(5).

Assaying a number of analytes in the one sample has become of increasing interest in laboratory medicine. The knowledge of the complexity of the cytokine network gained from multiple cytokine related analysis should increase understanding of normal and pathological processes. This increased understanding should pave the way to better diagnosis and disease management.

PRINCIPLE

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 proteases. A sandwich chemiluminescent immunoassay is employed for the cytokine IV 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 chemiluminescence 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 psent in the sample is calculated from the calibration curve.

Several different immunoassay based multi-analyte panels have been developed for use on Evidence. The Evidence Cytokine Array IV will quantitatively test for Soluble Interleukin-2 Receptor Alpha, Soluble Interleukin-6 Receptor, Soluble Tumor Necrosis Factor Receptor I, Soluble Tumor Necrosis Factor Receptor II and Matrix Metalloproteinase-9 simultaneously.

 

Soluble Interleukin-2 Receptor Alpha (sIL-2R α ) Assay

INTENDED USE

The Evidence Soluble Interleukin-2 Receptor Alpha (sIL-2Rα) assay has been designed for the quantitative measurement of sIL-2Rα in human serum samples.

CLINICAL SIGNIFICANCE

The IL-2 receptor (IL-2R) consists of three components the α, β and γ subunits. Only the α and β subunits bind to IL-2 with the γ subunit required for the transduction of proliferative signals(1). There are three forms of the receptor based on their affinity for the ligand. The very high affinity receptor is made up of the three components. The intermediate affinity receptor is made up of the β and γ components and the lowest affinity receptor is comprised of the α component. Only the βγ and the αβγ forms of the receptor can induce a signal following interaction with IL-2. The IL-2Rα is 55 kDa and is not a member of the cytokine superfamily of receptors. It is a protein composed of 251 amino acids with a 21 amino acid N-terminal signal peptide. The extracellular domain is made up of 219 amino acids that contain potential N- and O-linked glycosylation sites. The next 19 amino acids on the sequence are thought to repsent the membrane spanning region and the final domain repsents the cytoplasmic domain. IL-2Rα is not expssed on resting cells, but is inducible and is expssed by activated T cells, B cells and NK cells(2). A truncated version of the IL-2Rα membrane bound receptor can be released from activated lymphocytes upon activation and appears in the circulation as soluble IL-2Rα (sIL-2Rα). sIL-2Rα is 42 kDa and is thought to have significance as a marker of immune status(3) and is popularly favoured to measure the quantity of T lymphocytes activated by IL-2(1). It can also occur in the circulation as a dimer and is thought to repsent a regulatory element to control circulating IL-2 activity(3). It has been found to be an early marker of neoplastic diseases and also elevated levels have been found in diseases caused by infection, autoimmune disease and organ transplantation(1,3).

PRINCIPLE

The Evidence sIL-2Rα assay is a sandwich chemiluminescent assay for the detection of sIL-2Rα in human serum.

REFERENCES

1. Murakami S., Sakata H., Tsuji Y., Okubo K., Takahashi T., Kikuchi M. and Hirayama R. (2003) Changes in the levels of serum-soluble interleukin-2 receptor after surgical stress. Surg. Today 33(8):565-70.

2. Waldmann T., Tagaya Y. and Bamford R. (1998) Interleukin-2, interleukin-15, and their receptors. Int Rev Immunol. 16(3-4):205-26.

3. Hanisch U.K. and Quirion R. (1995) Interleukin-2 as a neuroregulatory cytokine. Brain Res. Rev. 21(3):246-84.

 

Soluble Interleukin-6 (sIL-6R) Assay

INTENDED USE

The Evidence Soluble Interleukin-6 (sIL-6R) assay has been designed for the quantitative measurement of sIL-6R in human serum samples.

CLINICAL SIGNIFICANCE

The IL-6 receptor complex belongs to the hematopoietic receptor superfamily and mediates the biological activities of IL-6(1,2). It consists of two distinct membrane bound glycoproteins, an 80 kDa cognate receptor subunit (IL-6R) and a 130 kDa signal-transducing element (gp130). The gp130 subunit is expssed in almost all organs including heart, kidney, spleen, liver, lung, placenta and brain. The cellular distribution of the cognate IL-6R is limited and its expssion is pdominantly confined to hepatocytes and leukocyte subpopulations(2). A soluble form of the IL-6R (sIL-6R) at 55 kDa has been identified in serum and urine(3). This receptor binds IL-6 with the same affinity as the cognate receptor, which prolongs the plasma half-life of the IL-6. The sIL-6R/IL-6 complex is then able to activate cells via the membrane bound gp130. This means that the sIL-6R/IL-6 complex is an agonist for cell types that expss gp130, but not necessarily the IL-6 cognate subunit. Two different mechanisms have been described for the generation of soluble IL-6R. The first mechanism is by the proteolytic cleavage (shedding) of the membrane bound form and the second mechanism involves alternative mRNA splicing resulting in a transcript encoding a soluble receptor(2). Native sIL-6R derived by either of the mechanisms retains the same capacity to bind IL-6 and to complex with gp130. A large number of studies have been published on the different biological activities of the sIL-6R/IL-6 complex and it is thought to be particularly relevant as a pro-inflammatory mediator. Diseases in which sIL-6R levels have been elevated include HIV infection, multiple myeloma, cardiac failure, lung carcinoma and non-Hodgkin's lymphoma(4).

PRINCIPLE

The Evidence sIL-6R assay is a sandwich chemiluminescent assay for the detection of sIL-6R in human serum.

REFERENCES

1. Heinrich P.C., Graeve L., Rose-John S., Schneider-Mergener J., Dittrich E, Erren A., Gerhartz C., Hemann U., Lütticken C., Wegenka U., Weiergräber, O., Horn, F. (1995) Membrane-bound and soluble interleukin-6 receptor: studies on structure, regulation of expssion, and signal transduction. Ann. N. Y. Acad. Sci.; 762:222-36.

2. Jones S.A., Horiuchi S., Topley N., Yamamoto N. and Fuller G.M. (2001) The soluble interleukin 6 receptor: mechanisms of production and implications in disease. FASEB J. 15(1):43-58.

3. Chaidos A.I., Bai M.C., Kamina S.A., Kanavaros P.E., Agnantis N.J. and Bourantas K.L. (2002) Incidence of apoptosis and cell proliferation in multiple myeloma: correlation with bcl-2 protein expssion and serum levels of interleukin-6 (IL-6) and soluble IL-6 receptor. Eur. J. Hematol. 69(2):90-4.

4. Montero-Julian F.A. (2001) The soluble IL-6 receptors: serum levels and biological function. Cell. Mol. Biol. (Noisy-le-grand). 47(4):583-97.

 

Soluble Tumor Necrosis Factor Receptor I (sTNFR I) Assay

INTENDED USE

The Evidence Soluble Tumor Necrosis Factor Receptor I (sTNFR I) test has been designed for the quantitative measurement of sTNFR I in human serum samples.

CLINICAL SIGNIFICANCE

Tumor necrosis factor receptor I (p55, p60, CD120a, TNFRSF1A)(1) (TNFRI) is one of two specific, high affinity cell surface receptors (TNFRI p55 and TNFRII p75) that function as transducing elements, providing the intracellular signal for cell responses to Tumor necrosis factor (TNF). TNF is a proinflammatory cytokine mainly produced by stimulated monocytes, macrophages and T-lymphocyte subsets. It has a key role in host defence and immunosurveillance, mediating complex cellular responses of a different, even contrasting nature(2,3). TNFRI has a molecular mass of 55 kDa(1) and is expssed by almost all cell types(2) especially those cells that are susceptible to the cytotoxic action of TNFα (3). TNF signalling to cells is chiefly mediated by TNFRI while the main function of the TNFRII is TNF psentation to the TNFRI. Both receptors participate in the induction of NF-κB and interleukin-6, in the generation of lymphocyte activated killer cells and the proliferation of natural killer cells as well as in anti-proliferation, cytoxicity and apoptosis. TNFRI is involved in interleukin-2 receptor induction, anti-viral activities, growth stimulation, HLA antigens expssion and endothelial cells adhesion(2).

Soluble forms of the two TNF receptors, which repsent the extracellular portions of the membrane associated receptors, have been found in serum, urine, and other body fluids(1). Neutrophils, activated T cells and monocytes in different secretion patterns are the main sources of sTNFRs. TNF itself leads to the shedding of TNFRs, which interfere with the binding of TNF to the cell surface-bound TNFR. TNFRs are detectable in normal serum, but their concentration increases significantly in inflammatory and non-inflammatory diseases. The kidney appears to be the major clearance organ of sTNFRs(3).

Some of the conditions that sTNFRI levels have been associated with include rheumatoid arthritis, systemic lupus erythematosus, meningococcal infections, sepsis(3) and recurrent spontaneous abortion(4). sTNFRI levels are increased in all clinical stages of HIV-infected patients, regardless of concurrent illness with the highest concentration in AIDS patients. Severe acute myocardial infarction causes the sTNFRI level to increase compared to patients without further complications(3). Increased levels have also been found in the serum of elderly people (5), in different cancers(6-8), and in those suffering from complications related to liver transplantation(9).

PRINCIPLE

The Evidence sTNFR I assay is a sandwich chemiluminescent assay for the detection of sTNFR I in human serum.

REFERENCES

1. Carpentier I., Coornaert B. and Beyaert R. (2004) Function and regulation of tumor necrosis factor type 2. Curr. Med. Chem. 11(16):2205-12.

2. Aderka D. (1996) The potential biological and clinical significance of the soluble tumor necrosis factor receptors. Cytokine Growth Factor Rev. 7(3):231-40.

3. Diez-Ruiz A., Tilz G.P., Zangerle R., Baier-Bitterlich G., Wachter H. and Fuchs D. (1995) Soluble receptors for Tumor necrosis factor in clinical laboratory diagnosis. Eur. J. Hematol. 54(1):1-8.

4. Chernyshov V.P., Vodyanik M.A. and Pisareva S.P. (2005) Lack of soluble TNF-receptors in women with recurrent spontaneous abortion and possibility for its correction. Am. J. Reprod. Immunol. 54(5):284-91.

5. Hasegawa Y., Sawada M., Ozaki N., Inagaki T. and Suzumura A. (2000) Increased soluble tumor necrosis factor receptor levels in the serum of elderly people. Gerontology 46(4):185-8.

6. Brenne A.T., Romstad L.H., Gimsing P., Juliusson G., TuressonI., Romundstad P., Borset M., Sundan A. and Waage A. (2004) A low serum level of soluble tumor necrosis factor receptor p55 pdicts response to thalidomide in advanced multiple myeloma. Hematologica 89(5):552-6.

7. Kaminska J., Nowacki M.P., Kowalska M., Rysinska A., Chwalinski M., Fuksiewicz M., Michalski W. and Chechlinska M. (2005) Clinical significance of serum cytokine measurements in untreated colorectal cancer patients: soluble tumor necrosis factor receptor type I--an independent prognostic factor. Tumor Biol. 26(4):186-94.

8. Aderka D., Englemann H., Hornik V., Skornick Y., Levo Y., Wallach D. and Kushtai G. (1991) Increased serum levels of soluble receptors for tumor necrosis factor in cancer patients. Cancer Res. 51(20):5602-7.

9. Grenz A., Schenk M., Zipfel A. and Viebahn R. (2000) TNF-alpha and its receptors mediate graft rejection and loss after liver transplantation. Clin. Chem. Lab. Med. 38(11):1183-5.

 

Soluble Tumor Necrosis Factor Receptor II (sTNFR II) Assay

INTENDED USE

The Evidence Soluble Tumor Necrosis Factor Receptor II (sTNFR II) assay has been designed for the quantitative measurement of sTNFR II in human serum samples.

CLINICAL SIGNIFICANCE

Tumor necrosis factor receptor II (p75, p80, CD120b, TNFRSF1B)(1) (TNFRII) is one of two specific, high affinity cell surface receptors (TNFRI p55 and TNFRII p75) that function as transducing elements, providing the intracellular signal for cell responses to Tumor necrosis factor (TNF). TNF is a proinflammatory cytokine mainly produced by stimulated monocytes, macrophages and T-lymphocyte subsets. It has a key role in host defence and immunosurveillance, mediating complex cellular responses of a different, even contrasting nature(2,3). TNFRII has a molecular mass of 75 kDa(1). Although TNFRII is expssed by almost all cell types, it is expssed primarily by cells of the immune system, cells of myeloid origin and endothelial cells(2). TNF induced effects mediated by TNFRII include proliferation of peripheral blood mononuclear cells, natural killer cells, B cells, oligodendrocyte pcursors, thymocytes and peripheral T cells, and also production of granulocyte macrophage colony stimulating factor by T cells and the production of NO and iNOS in macrophages. TNFRII is involved in TNF-induced killing of T-cells and several Tumor cells and has a role in neuronal survival. TNFRII has also been implicated in the inhibition of early hematopoiesis, the regulation of vascular permeability, and T cell dependent hepatocyte apoptosis. Soluble forms of the two TNF receptors, which repsent the extracellular portions of the membrane associated receptors, have been found in serum, urine, and other body fluids(1). Neutrophils, activated T cells and monocytes in different secretion patterns are the main sources of sTNFRs. TNF itself leads to the shedding of TNFRs which interfere with the binding of TNF to the cell surface-bound TNFR. TNFRs are detectable in normal serum, but their concentration increases significantly in inflammatory and non-inflammatory diseases. The kidney appears to be the major clearance organ of sTNFRs(3).

Conditions in which sTNFRII levels correlate with disease progression include rheumatoid arthritis, systemic lupus erythematosus, sepsis, chronic hepatitis virus infection, acute pancreatitis, acute respiratory distress syndrome and AIDS. Increased levels have also been found in the serum of elderly people, in different cancers, and in those suffering from complications with bone marrow transplantation or graft versus host disease. sTNFRII can act as an antagonist, which may be a general compensatory mechanism designed to down regulate inflammation, and also may act as an agonist by prolonging the half-life of TNF in the circulation. sTNFR has been used as an immunotherapeutic agent with Etanercept (sTNFRII linked to the F (c) portion of human immunoglobin) having been used in the treatment of rheumatoid arthritis patients(1).

PRINCIPLE

The Evidence sTNFR II assay is a sandwich chemiluminescent assay for the detection of sTNFR II in human serum.

REFERENCES

1. Carpentier I., Coornaert B. and Beyaert R. (2004) Function and regulation of tumor necrosis factor type 2. Curr. Med. Chem. 11(16):2205-12.

2. Aderka D. (1996) The potential biological and clinical significance of the soluble tumor necrosis factor receptors. Cytokine Growth Factor Rev. 7(3):231-40.

3. Diez-Ruiz A., Tilz G.P., Zangerle R., Baier-Bitterlich G., Wachter H. and Fuchs D. (1995) Soluble receptors for Tumor necrosis factor in clinical laboratory diagnosis. Eur. J. Hematol. 54(1):1-8.

4. Naismith J.H. and Sprang S.R. (1995-96) Tumor necrosis factor receptor superfamily. J. Inflamm. 47(1-2):1-7.

 

Matrix Metalloproteinase-9 (MMP-9) Assay

INTENDED USE

The Evidence Matrix Metalloproteinase-9 (MMP-9) test has been designed for the quantitative measurement of MMP-9 in human serum samples.

CLINICAL SIGNIFICANCE

Matrix metalloproteinase-9 (MMP-9) (gelatinase B) (92 kDa) is a member of the matrix metalloproteinase (MMP) family. The MMPs are endopeptidases that selectively degrade the components of various extracellular matrices(1,2). They are characterized by the psence of conserved protein domains: a prodomain, an active domain and a zinc binding domain. Most members contain an additional carboxyterminal hemopexin domain. MMP-9 has a gelatine-binding fibronectin domain and is the largest and most complex member of the MMP family. In many cell types MMP-9 is produced as a mixture of monomers and homodimers. Also neutrophils produce a third form that is a covalent complex of MMP-9 with neutrophil gelatinase B-associated lipocalin (NGAL). MMP-9 is synthesized and secreted as a zymogen or proenzyme, which remains inactive unless it is activated by removal of the propeptide. Different proteases are known to activate MMP-9. Once MMP-9 has been secreted and activated, its activity can still be regulated by degradation or inhibition. It is inhibited by α(2)-macroglobulin and more specifically by tissue inhibitors of metalloproteinases (TIMPs). TIMPs are stable glycoproteins with 4 TIMPs having been identified. TIMP-1 binds to MMP-9 with high affinity. As MMP-9 has an important role in the remodelling of extracellular matrix components, it is implicated in various physiological functions. However, any unbalance in the regulation of MMP-9 or in the degradation of the extracellular matrix components or other substrates leads to pathological conditions. Some of the physiological functions that MMP-9 is involved in are reproduction, growth and development, leukocyte mobilisation, inflammation and wound healing. Pathological conditions that MMP-9 has been associated with include inflammation, infectious diseases, degenerative diseases, vascular diseases and cancers(3).

PRINCIPLE

The Evidence MMP-9 assay is a sandwich chemiluminescent assay for the detection of MMP-9 in human serum samples.

REFERENCES

1. Kim W.U., Min S.Y., Cho M.L., Hong K.H., Shin Y.J., Park S.H. and Cho C.S. (2005) Elevated matrix metalloproteinase-9 in patients with systemic sclerosis. Arthritis Res. Ther. 7(1):R71-9.

2. Hibbs M.S., Hasty K.A., Seyer J.M., Kang A.H. and Mainardi C.L. (1985) Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J. Biol. Chem. 260(4):2493-2500.

3. Van den Steen P.E., Dubois B., NelissenI., Rudd P.M., Dwek R.A. and Opdenakker G. (2002) Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit. Rev. Biochem. Mol. Biol. 37(6):375-536.

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