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Cytokine array v

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Cytokine array v B A T (evidence investigatorâ„¢) 54 biochips EV3666 $9251.91
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INTENDED USE

The Evidence Investigator Cytokine Array V is to be used for the in vitro simultaneous quantitative detection of multiple related cytokine immunoassays (in parallel) from a single sample.

The Evidence Investigator Cytokine Array V 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 to be 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).

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.

PRINCIPLE

The Evidence Investigator Biochip Array technology is used to perform 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 array. Increased levels of cytokine in a specimen will lead to increased binding of antibody labeled with horseradish 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 Investigator .

The Evidence Investigator CTK Array V will quantitatively test for Interleukin-3, Interleukin-7, Interleukin-12p70, Interleukin-13 and Interleukin-23 simultaneously.

REFERENCES

1. Oppenheim, J.J. (1998) Foreword. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. xviii-xxii.

2. Vil?ek, J. (1998) The Cytokines: An Overview. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 1-20.

3. Schroff RW, Foon KA, Beatty SM, Oldham RK, Morgan AC Jr. Human Anti-Mouse Immunoglobulin Responses in Patients Receiving Monoclonal Antibody Therapy. Cancer Res 1985;45:879.

4. Boscato LM, Stuart MC. Heterophilic Antibodies: A Problem for all Immunoassays. Clin Chem 1998;34:27.

 

Interleukin-3 (IL-3) Assay

INTENDED USE

The Evidence Investigator Interleukin-3 (IL-3) test has been designed for the quantitative measurement of IL-3 in human serum or plasma samples.

CLINICAL SIGNIFICANCE

Interleukin-3 (IL-3) possesses diverse biological activities and was discovered independently in studies on its biological activities, which meant that it was described under a number of different names. Some of these names included: multi-colony stimulating factor, mast cell growth factor, persisting cell stimulating factor, histamine-producing cell stimulating factor, multilineage hemopoietic growth factor and Thy-1 inducing factor. Many other names have also been used.

IL-3 is a heavily glycosylated protein with a polypeptide chain of 133 amino acids. It occurs naturally in a diversity of glycoforms generated by the addition of carbohydrate groups which results in size heterogeneity from 28 to 45 kDa. The function of the extensive carbohydrate modifications of the IL-3 polypeptide is not known. Chemically synthesized or bacterial derived recombinant IL-3 exhibit all the biologic activities of the naturally occurring glycosylated IL-3. The IL-3 gene is located on chromosome 5 and is closely linked with the granulocyte-macrophage colony-stimulating factor gene. There is low amino acid sequence identity between human and mouse IL-3 and the biological activities of IL-3 are species specific.

IL-3 acts on numerous target cells within the hemopoietic system and has the broadest target specificity of any of the hemopoietic growth factors. The range of target cells includes progenitor cells of every lineage derived from pluripotent hemopoietic stem cells. Like other hemopoietic growth factors, IL-3 prevents death by apoptosis and promotes survival in vitro. The only source of IL-3 is cells of lymphohemopoietic origin with activated T lymphocyte being the major physiologic source. It can also be produced by mast cells when immunoglobulin E Fc receptors are cross-linked. Therefore IL-3 functions as a link between the T lymphocytes of the immune system and the hemopoietic system. It is thought that IL-3 is one of the mediators of the response of the hemopoietic system to stress rather than having a role in mediating steady-state hemopoiesis in the unperturbed state. It interacts with the IL-3 receptor, which is made up of two subunits, an α and a β chain each of which is a member of the hemopoietin receptor superfamily. It has been reported that IL-3 is undetectable in the blood of normal animals, with the half-life of intravenously injected IL-3 short at around 40 minutes. It does not appear to be bound to larger molecules in the serum and the major part of the IL-3 is destroyed in the kidney. It has also been reported that IL-3 can remain undetectable in the serum of animals undergoing immune responses (1,2). Hematopoietic cytokines can affect the growth and spread of cancer and as such IL-3 has been linked with various diseases including colorectal and pancreatic cancers (3,4).

PRINCIPLE

The Evidence Investigator IL-3 assay is a sandwich chemiluminescent immunoassay for the detection of IL-3 in human serum and plasma.

REFERENCES

1. Schrader, J.W. (1998) Interleukin-3. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 105-132.

2. Frendl, G. (1992) Interleukin 3: from colony-stimulating factor to pluripotent immunoregulatory cytokine. Int. J. Immunopharmacol. 14(3):421-30.

3. Mroczko B, Szmitkowski M, Wereszczynska-Siemiatkowska U, Okulczyk B. (2005) Stem cell factor (SCF) and interleukin 3 (IL-3) in the sera of patients with colorectal cancer. Dig Dis Sci. 50(6):1019-24

4. Mroczko B, Szmitkowski M, Wereszczynska-Siemiatkowska U, Jurkowska G. (2005) Hematopoietic cytokines in the sera of patients with pancreatic cancer. Clin Chem Lab Med. 43(2):146-50

 

Interleukin-7 (IL-7) Assay

INTENDED USE

The Evidence Investigator Interleukin-7 (IL-7) test has been designed for the quantitative measurement of IL-7 in human serum or plasma samples.

CLINICAL SIGNIFICANCE

Interleukin-7 (IL-7) is classified as a type 1 short-chain cytokine of the hematopoietin family, a group that also includes IL-2, IL-3, IL-4, IL-5, GM-CSF, IL-9, IL-13, IL-15, M-CSF, and stem cell factor. The human gene for IL-7 is located on chromosome 8q12-13. The amino acid sequence of IL-7 predicts a molecular weight of 17.4 kDa, but glycosylation results in an active protein of 25 kDa (1). IL-7 is produced by nonhemopoietic stromal cells of multiple organs, including: thymus, lymphoid organs, skin, intestine, and liver among others. Immune cells play little, if any, role in IL-7 production (2).

IL-7 signals through the IL-7 receptor (IL-7R) (CD127), which has both high affinity and low affinity binding sites. It is composed of two subunits: the IL-7Rα chain and the common γ chain (γc), which is shared with receptors for IL-2, IL-4, IL-9 and IL-15 (3). In general, IL-7Rα can be identified on immature B-cells through early pre-B stage, on thymocytes, and on most mature T-cells with transient down-regulation upon activation. IL-7 signalling involves a number of nonreceptor tyrosine kinase pathways that associate with the cytoplasmic tail of the receptor. These include the Janus kinase/signal transducer and activator of transcription pathway, phosphatidylinositol 3-kinase, and Src family tyrosine kinases. IL-7 shares intracellular signalling molecules with a number of other cytokines and the exact mechanisms responsible for signalling specificity remain unclear (1).

IL-7 appears to be involved in the development of an effective immune system and also in the generation and maintenance of strong and effective cellular immune responses directed against cancer cells, or infectious diseases. It seems to serve as the major growth and differentiation factor for both thymic and extrathymic development of γδ (+) T lymphocytes. It promotes immune effector functions in T lymphocytes, natural killer cells and monocytes-macrophages, and modulates the quantity and quality of immune responses in vitro and in vivo (3).

IL-7 has been linked with various diseases including ovarian cancer and instability in coronary artery disease (4,5).

PRINCIPLE

The Evidence Investigator IL-7 assay is a sandwich chemiluminescent immunoassay for the detection of IL-7 in human serum and plasma.

REFERENCES

1. Fry, T.J., Mackall. C.L. (2002) Interleukin-7: from bench to clinic. Blood 99(11):3892-904.

2. Fry, T.J., Mackall. C.L. (2005) The many faces of IL-7: from lymphopoiesis to peripheral T cell maintenance. J. Immunol. 174(11):6571-6.

3. Maeurer, M.J. Edington, H.D., Lotze, M.T. (1998) Interleukin-7. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 229-269.

4. Xie X, Ye D, Chen H, Lu W, Cheng B, Zhong H. (2004) Interleukin-7 and suppression of local peritoneal immunity in ovarian carcinoma. Int J Gynaecol Obstet. 85(2):151-8.

5. Damas JK, Waehre T, Yndestad A, Otterdal K, Hognestad A, Solum NO, Gullestad L, Froland SS, Aukrust P. (2003) Interleukin-7-mediated inflammation in unstable angina: possible role of chemokines and platelets. Circulation. 107(21):2670-6

 

Interleukin-12p70 (IL-12p70) Assay

INTENDED USE

The Evidence Investigator Interleukin-12p70 (IL-12p70) test has been designed for the quantitative measurement of IL-12p70 in human serum or plasma samples.

CLINICAL SIGNIFICANCE

Interleukin-12 (IL-12) is a 75 kDa heterodimeric glycoprotein cytokine composed of disulphide linked p40 (40 kDa) and p35 (35 kDa) subunits that are derived from separate genes (1). p35 is expressed in a limiting and tightly regulated fashion by many different cell types, however the expression of p40, though in greater quantities than required for p70 formation, appears to be restricted to antigen presenting cells. Coexpression of both p35 and p40 in one cell is required for the formation of bioactive IL-12p70 (2,3). The actions of IL-12p70 are mediated by binding of the ligand to a high affinity IL-12 receptor (IL-12R). The IL-12R is expressed by natural killer cells, T-cells macrophages and dendritic cells (2) . IL-12p70 is primarily produced by monocyte-macrophages, dendritic cells and polymorphonuclear leukocytes (4).

IL-12 acts on resting and activated NK and T cells (5) and is involved in NK cell activation, T cell receptor-induced T cell proliferation, promotion of T cell cytokine production and regulator of B cell antibody production (6). IL-12 stimulates IFN-γ production, which is essential in resistance to intracellular protozoan, fungal and bacterial infections and, in addition, Tumor s (2). In some part due to the preferential expression of IL-12R by T(H1) CD4 (+) T cells, IL-12 facilitates a T(H1)-type biased, antigen specific, cellular immune response. IL-12 is also responsible for the preferential switching of antigen-specific immunoglobulin towards IgG(2a) and IgG (2b) isotypes that are believed to enhance phagocytic opsonisation, complement fixation and antibody-dependent cell-mediated cytoxicity based mechanisms for clearance of diseased or foreign tissue (7). Traditionally, IL-12 is accepted as an important mediator of autoimmunity and is involved in a number of autoimmune diseases including rheumatoid arthritis, psoriasis, inflammatory bowel disease and insulin-dependent diabetes mellitus (2).

In the past researchers have reported IL-12p35 or IL-12p40 levels as a measure of IL-12p70; however, this method may greatly overestimate the level of bioactive IL-12p70 due to the independent regulation of IL-12p35 and IL-12p40 and the ability of the p40 subunit to form bimolecular complexes other than IL-12 (8). It has also been suggested that the ratio of the IL-12p40 monomer to homodimer is an equally important yet underreported determinant of IL-12 bioactivity (9).

PRINCIPLE

The Evidence Investigator IL-12p70 assay is a sandwich chemiluminescent immunoassay for the detection of IL-12p70 in human serum and plasma.

REFERENCES

1. Gubler, U., Chuam, A.O., Schoenhaut, D.S., Dwyer, C.M., McComas, W., Motyka, R., Nabavi, N., Wolitzky, A.G., Quinn, P.M., Familletti, P.C., Gately, M.K. (1991) Coexpression of two distinct genes is required to generate secreted bioactive cytotoxic lymphocyte maturation factor. Proc. Natl. Acad. Sci. U.S.A. 88(10):4143-7.

2. Alber, G., Al-Robaiy, S., Kleinschek, M., Knauer, J., Krumbholz, P., Richter, J., Schoeneberger, S., Schuetze, N., Schulz, S., Toepfer, K., Voigtlaender, R., Lehmann, J., Mueller, U. (2006) Induction of immunity and inflammation by interleukin-12 family members. Ernst Schering Res. Found. Workshop (56):107-27.

3. Langrish, C.L., McKenzie, B.S., Wilson, N.J., de Waal Malefyt, R., Kastelein, R.A., Cua, D.J. (2004) IL-12 and IL-23: master regulators of innate and adaptive immunity. Immunol. Rev. 202(1):96-105.

4. Caspi, R.R. (1998) IL-12 in autoimmunity. Clin. Immunol. Immunopathol. 88(1):4-13.

5. Ma, X., Aste-Amezaga, M., Gri, G., Gerosa, F., Trinchieri, G. (1997) Immunomodulatory functions and molecular regulation of IL-12. Chem. Immunol. 68:1-22.

6. Beadling, C., Slifka, M.K. (2006) Regulation of innate and adaptive immune responses by the related cytokines IL-12, IL-23, and IL-27. Arch. Immunol. Ther. Exp. (Warsz). 54(1):15-24.

7. Storkus, W.J., Tahara, H., Lotze, M.T. (1998) Interleukin-12. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 391-425.

8. Watford, W.T., Moriguchi, M., Morinobu, A., O'Shea, J.J. (2003) The biology of IL-12: coordinating innate and adaptive immune responses. Cytokine Growth Factor Rev. 14(5):361-8.

9. Klinke, D.J. 2nd. (2006) The ratio of p40 monomer to dimer is an important determinant of IL-12 bioactivity. J. Theor. Biol. 240(2):323-35.

 

Interleukin-13 (IL-13) Assay

INTENDED USE

The Evidence Investigator Interleukin-13 (IL-13) test has been designed for the quantitative measurement of IL-13 in human serum or plasma samples.

CLINICAL SIGNIFICANCE

Interleukin-13 (IL-13) is a 12 kDa protein that folds into four α-helical bundles. It contains four potential N-glycosylation sites and four cysteine residues that form two intramolecular disulphide bonds. IL-13 shares a number of structural features and functional characteristics with IL-4. The IL-13 protein is approximately 25% homologous (1) with IL-4 and belongs to the same α-helix protein family (2). IL-13 production is restricted to activated T lymphocytes, especially T(H2) cells, mast cells and basophils. It has also been demonstrated that IL-13 can be produced in dendritic cells and natural killer cells (2).

IL-13 signals through the IL-13 receptor, components of which are shared by the IL-4 receptor and differentially expressed on various cell types. This may account for the sharing of many biological functions of IL-13 by IL-4. IL-13 receptors are expressed on B cells, monocytes-macrophages, basophils, mast cells, endothelial cells and certain Tumor cells. The high-affinity IL-13 receptor complex comprises the 140 kDa IL-4Rα chain and an IL-13 binding protein. The IL-4Rα chain alone binds IL-4, but not IL-13. Two IL-13 binding proteins have been identified as IL-13Rα1 and IL-13Rα2. The IL-13Rα1 binds IL-13 with low affinity and with high affinity when in a heterodimeric receptor complex with IL-4Rα. The IL-13Rα2 binds IL-13 with high affinity in the absence of the IL-4Rα chain. Signal transduction after binding of IL-13 is initiated by binding of IL-13Rα1 and IL-13Rα2 to the IL-4Rα chain, which is the signal transducing receptor component (1,2).

IL-13 has important immunomodulating activities (1). IL-13 affects B cells and monocytes resulting in upregulation of class II expression, promotion of IgE class switching and inhibition of inflammatory cytokine production. IL-13 plays a dominant role in resistance to most gastrointestinal nematodes and also modulates resistance to intracellular organisms by regulating cell mediated immunity. IL-13 is the central mediator of allergic asthma, where it regulates eosinophilic inflammation, mucus secretion, and airway hyperresponsiveness. In some cancers IL-13 modulates apoptosis or Tumor cell growth and can also inhibit Tumor immunosurveillance. Also it has been revealed that IL-13 is a potent mediator of tissue fibrosis in both schistosomiasis and asthma, which indicates that it is a key regulator of the extracellular matrix (3).

PRINCIPLE

The Evidence Investigator IL-13 assay is a sandwich chemiluminescent immunoassay for the detection of IL-13 in human serum and plasma.

REFERENCES

1. de Waal Malefyt, R. & de Vries, J.E. (1998) Interleukin-13. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 427-442.

2. Brombacher, F. (2000) The role of interleukin-13 in infectious diseases and allergy. Bioessays. 22(7): 646-56.

3. Wynn, T.A. (2003) IL-13 effector functions. Annu. Rev. Immunol . 21:425-56.

 

Interleukin-23 (IL-23) Assay

INTENDED USE

The Evidence Investigator Interleukin-23 (IL-23) test has been designed for the quantitative measurement of IL-23 in human serum or plasma samples.

CLINICAL SIGNIFICANCE

Interleukin 23 (IL-23) is member of the IL-12 family. The IL-12 family consists of cytokines IL-12(p40p35), IL-23(p40p19) and IL-27(EBI13p28), and monomeric and homodimeric p40 (1). IL-23 is a heterodimeric cytokine composed of disulphide linked p19 and p40 subunits. The p40 subunit is common to both IL-23 and IL-12p70. The p19 protein exhibits homology to IL12p35, IL-6 and G-CSF (1-3), whereas p40 has the structure of a cytokine receptor (1). p19 is produced by activated dendritic cells and macrophages with co-expression of p40 required for its secretion. IL-23 binds to a receptor composed of IL-12Rβ1 and IL-23R. Like IL-12, IL-23 induces IFN-γ production in T cells and dendritic cells. However, IL-23 uniquely functions to preferentially induce proliferation of memory T-cells (2).

PRINCIPLE

The Evidence Investigator IL-23 assay is a sandwich chemiluminescent immunoassay for the detection of IL-23 in human serum and plasma.

REFERENCES

1. Alber, G., Al-Robaiy, S., Kleinschek, M., Knauer, J., Krumbholz, P., Richter, J., Schoeneberger, S., Schuetze, N., Schulz, S., Toepfer, K., Voigtlaender, R., Lehmann, J., Mueller, U. (2006) Induction of immunity and inflammation by interleukin-12 family members. Ernst Schering Res. Found. Workshop. (56):107-27.

2. Watford, W.T., Moriguchi, M., Morinobu, A., O'Shea, J.J. (2003) The biology of IL-12: coordinating innate and adaptive immune responses. Cytokine Growth Factor Rev. 14(5):361-8.

3. Lankford, C.S., Frucht, D.M. (2003) A unique role for IL-23 in promoting cellular immunity. J. Leukoc. Biol. 73(1):49-56.

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