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Cytokine array iii

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Cytokine array iii B A T (evidence investigatorâ„¢) 54 biochips EV3678 $9251.91
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The Evidence Investigator Cytokine Array III is to be used for the in vitro simultaneous quantitative detection of multiple related cytokine immunoassays from a single sample.

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


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.


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 III will quantitatively test for Interleukin-5 , Interleukin-15 , Tumor Necrosis Factor-beta, Granulocyte Macrophage Colony-Stimulating Factor and Macrophage Inflammatory Protein-1α simultaneously.


1. Primus FJ, Kelley EA, Hansen HJ, Goldenberg DM. "Sandwich"-Type Immunoassay of Carcinoembryonic Antigen in Patients Receiving Murine Monoclonal Antibodies for Diagnosis and Therapy. Clin Chem 1988;35:261

2. Hansen HJ, Solving the Problem of Antibody Interference in Commercial "Sandwich"-Type Immunoassay of Carcinoembryonic Antigen. Clin Chem 1989;35:146

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-5 (IL-5) Assay


The Evidence Investigator Interleukin-5 (IL-5) test has been designed for the quantitative measurement of IL-5 in human serum and plasma samples.


Interleukin-5 (IL-5) is a disulphide linked homodimer and belongs to a family of structurally related proteins that includes: interleukin-2, interleukin-4, macrophage colony-stimulating factor, granulocyte macrophage colony-stimulating factor and growth hormone. It is a glycoprotein with the apparent molecular weight of recombinant IL-5 produced by mammalian cells in the range 45 to 60 kDa. The large variation in the molecular weight caused predominantly by the addition of heterogeneous carbohydrate chains. Removal of the carbohydrate from the IL-5 causes loss of thermostability, but does not appear to affect its biological activity in vitro.

IL-5 is produced mainly by activated T-cells and mast cells. It interacts with the IL-5 receptor, which is made up of two subunits, an α chain and a β chain. Both of these receptor chains are members of the cytokine-hematopoietin superfamily. IL-5 acts selectively on eosinophils and it is now clear that IL-5 is the main controlling cytokine for eosinophilia. Eosinophilia is characteristic of a limited number of disease states, most notably parasitic infections and allergy. It has also been observed in a significant proportion of a wide range of human Tumors and in many cases the presence of eosinophils has been found to be of positive prognostic significance. The most pronounced effect of IL-5 on cells other than eosinophils in humans is the effect on basophils. It has been shown that IL-5 primes basophils for increased histamine production and leukotriene generation, and basophils in the blood clearly express the IL-5 receptor. Although studies with murine IL-5 have shown that it is a B-cell growth factor in vitro, no activity could be demonstrated in a wide range of human B-cell assay systems. The IL-5 receptor could not be detected on the surface of human B-cells (1,2).


The Evidence Investigator IL-5 assay is a sandwich chemiluminescent immunoassay for the detection of IL-5 in human serum and plasma.


1. Sanderson, C.J. (1998) Interleukin-5. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 175-195.

2. Koike, M., Takatsu, K. (1994) IL-5 and its receptor: which role do they play in the immune response? Int. Arch. Allergy Immunol. 104(1):1-9.


Interleukin-15 (IL-15) Assay


The Evidence Investigator Interleukin-15 (IL-15) test has been designed for the quantitative measurement of IL-15 in human serum and Plasma samples.


Interleukin-15 (IL-15) is a 14 to 15 kDa protein of 114 amino acids. It contains 2 disulphide bonds and 2 N-linked glycosylation sites at the C-terminus (1). IL-15 is expressed at the mRNA level in numerous normal human tissues in a broad range of cell types, including activated monocytes, dendritic cells, osteoclasts and fibroblasts. IL-15 signals through the heterotrimeric IL-15 receptor. The IL-15 receptor includes the IL-2Rβ chain and common γ chain together with a unique α chain, which is alternately spliced to yield three active forms each capable of high affinity binding to IL-15. The IL-15Rαβγ receptor complex signals through JAK1/3 and STAT3/5 (2). IL-15 has similar biologic properties in vitro to IL-2 which is consistent with their shared receptor signalling components. However, in vivo it is becoming increasingly evident that IL-2 and IL-15 exert differential effects on a number of different cells with the specific α chains of their receptors differentially expressed among tissues and cell types (3).

IL-15 has an essential role in natural killer (NK) cell development. It activates NK cell proliferation, cytotoxicity, and cytokine production and regulates NK cell/macrophage interaction. Studies have suggested that IL-15 may have a role in establishing innate immune responses and maintaining neutrophil-mediated inflammatory processes (1). IL-15 is a potent growth factor for activated T-cells, inhibiting apoptosis of cytokine-deprived activated T-cells and inducing their locomotion and directed migration. It can also induce cytokine production by T-cells (3) . Although IL-15 affects cells outside of the immune system, it is not thought to be critical to their development or function (1).

It has been suggested that the deregulation of the normally strict controls over IL-15 production or secretion contributes to inflammatory and autoimmune diseases (3). Conditions that IL-15 is thought to have a role or potential role in include rheumatoid arthritis, sarcoidosis, inflammatory bowel disease, hepatitis C-induced liver diseases and multiple sclerosis. IL-15 is also thought to be involved in transplant rejection, viral and bacterial infections, and cancer (1). It has been reported that IL-15 is up-regulated in atherosclerosis and it has been suggested that it may be important in its pathogenesis (4).


The Evidence Investigator IL-15 assay is a sandwich chemiluminescent immunoassay for the detection of IL-15 in human serum and plasma.


1. Fehniger, T.A., Caligiuri, M.A. (2001) Interleukin 15: biology and relevance to human disease. Blood 97(1):14-32.

2. Liew, F.Y., McInnes, I.B. (2002) Role of interleukin 15 and interleukin 18 in inflammatory response. Ann. Rheum. Dis. 61 Suppl 2: ii100-2.

3. Kennedy, M.K., Park, L.S. & Paxton, R.J. (1998) Interleukin-15. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 443-464

4. Kaibe, M., Ohishi, M., Ito, N., Yuan, M., Takagi, T., Terai, M., Tatara, Y., Komai, N., Rakugi, H., Ogihara, T. (2005) Serum interleukin-15 concentration in patients with essential hypertension. Am. J. Hypertens. 18(8):1019-25.


Tumor Necrosis Factor Beta TNF-β Assay


The Evidence Investigator Tumor Necrosis Factor Beta (TNF-β) test has been designed for the quantitative measurement of TNF-β in human serum and plasma samples.


Tumor necrosis factor β (TNF-β, Lymphotoxin α (LTA)) (25 kDa) is a member if the TNF ligand superfamily. The TNF superfamily of cytokines are a family of type II transmembrane glycoproteins (1) involved with cell proliferation and death, inflammation and immunological and neuronal cell function. TNF-β is mostly synthesized by activated lymphocytes and is secreted since it lacks a transmembrane anchoring sequence. TNF-β is secreted as a homotrimer, but also exists in a heterotrimeric structure with 33 kDa membrane bound lymphotoxin β. TNF-β shows 28% amino acid sequence homology to TNF-α and both ligands bind to the same two receptors TNFRSF1A (TNFR1) and TNFRSF1B (TNFR2) (2). Binding of ligand to these receptors results in a cascade of intracellular processes with diverse and sometimes apparently contradictory effects (3). TNF-α and TNF-β both bind to soluble TNF-binding proteins found in human urine and serum. These TNF-binding proteins represent cleaved fragments of the full length receptors that are shed from the cell membrane by proteolytic cleavage. Binding of TNF to these binding proteins is believed to increase ligand half-life and also modulate TNF systemic and local effects by neutralizing the bioactivity of TNF (4). TNF-β mediates a large variety of inflammatory, immunostimulatory, and antiviral responses (5). TNF-β is also involved in the formation of secondary lymphoid organs during development (6) and plays a role in apoptosis (1).


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


1. Ware, C.F., Santee, S., and Glass, A. (1998). Tumor necrosis factor-related ligands and receptors. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 549-592.

2. Orlinick JR, Chao MV. (1998) TNF-related ligands and their receptors. Cell. Signal. 10(8):543-51.

3. McDermott, M.F. (2001) TNF and TNFR biology in health and disease. Cell. Mol. Biol. 47(4):619-35.

4. Olsson, I., Gatanaga, T., Gullberg, U., Lantz, M., Granger, G.A. (1993) Tumour necrosis factor (TNF) binding proteins (soluble TNF receptor forms) with possible roles in inflammation and malignancy. Eur. Cytokine Netw. 4(3):169-80.

5. Nakayama, T., Soma, M., Sato, N., Haketa, A., Kosuge, K., Aoi, N., Sato, M., Izumi, Y., Matsumoto, K., Kanmatsuse, K., Kokubun, S. (2004) An association study in essential hypertension using functional polymorphisms in lymphotoxin-α gene. Am. J. Hypertens. 17(11 Pt 1):1045-9.

6. Banks, T.A., Rouse, B.T., Kerley, M.K., Blair, P.J., Godfrey, V.L., Kuklin, N.A., Bouley, D.M., Thomas, J., Kanangat, S., Mucenski, M.L. (1995) Lymphotoxin-alpha-deficient mice. Effects on secondary lymphoid organ development and humoral immune responsiveness. J. Immunol. 155(4):1685-93.


Granulocyte-Macrophage Colony Stimulating Factor ( GMCSF) Assay


The Evidence Investigator Granulocyte-Macrophage Colony Stimulating Factor (GMCSF) test has been designed for the quantitative measurement of GM-CSF in human serum and plasma samples.


Granulocyte-macrophage colony stimulating factor (GMCSF) isolated from human sources is glycosylated with an apparent molecular mass of 23 kDa. The mature protein has 127 amino acids and is preceded by a hydrophobic leader sequence of 25 amino acids. It has two potential N-linked glycosylation sites at different locations with glycosylation not essential for activity (1). GMCSF has two intrachain disulphide bonds which maintain biological activity (2). GMCSF can be produced by a number of different cell types including T- and B-lymphocytes, macrophages, osteoblasts, endothelial cells, fibroblasts, stromal cells, leukaemic and various solid organ Tumor cells. Stimulation of the producer cell is often required for production of GM-CSF. Stimuli include antigens in T and B cells, lipopolysaccharide, IL-1 and Tumor necrosis factor in macrophages, fibroblasts or endothelial cells (1).

GMCSF signals through the GMCSF receptor, which is composed of two components that together generate a ligand specific, high-affinity receptor. GMCSF receptors are found on hematopoietic cells and non-hematopoietic cells such as trophoblasts, endothelial cells, oligodendrocytes and on various malignant cells, such as those associated with leukemia and renal carcinoma but not on T- and B- lymphocytes (1).

In vitro studies have identified GMCSF activities that range from regulation of differentiation and proliferation of hematopoietic progenitors, to the regulation of survival and function of mature cells such as neutrophils, macrophages or dentritic cells. These in vitro activities would suggest a prominent role for GMCSF in hematopoiesis, antimicrobial defense and immune response (1). It has been suggested that the major role for GMCSF in vivo apart from alveolar macrophage development may be its ability to govern the properties of the more mature cells of the granulocyte and macrophage lineages, particularly during host defence and inflammatory reactions. However, the precise proinflammatory role of GMCSF in disease has yet to be determined (2).


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


1. Quesniaux, V.F.J. & Jones, T.C. (1998) Granulocyte-Macrophage Colony Stimulating Factor. In The Cytokine Handbook, 3 (rd) ed. Thomson, A. (ed.), Academic Press, San Diego, pp. 637-670.

2. Fleetwood, A.J., Cook, A.D., Hamilton, J.A. (2005) Functions of granulocyte-macrophage colony-stimulating factor. Crit. Rev. Immunol. 25(5):405-28.


Macrophage Inflammatory Protein-1 α MIP-1 α Assay


The Evidence Investigator Macrophage Inflammatory Protein-1α (MIP-1α) test has been designed for the quantitative measurement of MIP-1α in human serum and plasma samples.


Macrophage inflammatory protein-1α (MIP-1α, CCL3) is a member of the CC chemokine subfamily whose members are known for chemotactic and proinflammatory effects and also for the promotion of homeostasis. MIP-1α is synthesized as a 92 amino acid precursor that is proteolytically processed to a mature protein of about 70 amino acids. MIP-1α secretion is induced by inflammatory agents including LPS, substance P, viral infection, TNFα, IFNγ, and IL-1. MIP-1α is generally secreted after activation of monocytes-macrophages, T- and B-lymphocytes, neutrophils, dendritic cells, mast cells, NK cells, platelets, osteoblasts, astrocytes, microglia, epithelial cells and fibroblasts. The effects of MIP-1α are mediated via binding to CC chemokine G-protein coupled receptors at the cell membrane. The effects of MIP-1α include chemotaxis, degranulation, phagocytosis and mediator synthesis. Consequently, MIP-1α has roles in inflammatory responses at sites of injury or infection by recruiting proinflammatory cells, including T-cells, monocytes, dendritic cells and NK cells. MIP-1α has been shown to reversibly inhibit the proliferation of certain hematopoietic stem cells in vitro and in vivo. Interactions involving CD4 and MIP-1α receptor CCR5 are required for HIV infection of macrophages and CD4+ T cells. The binding of MIP-1α to the CCR5 receptor has been found to block HIV-1 entry into permissive cells. Changes in MIP-1α levels have been reported for rheumatoid arthritis, multiple sclerosis, allergic asthma, ulcerative colitis, myeloid leukemia, multiple myeloma, sepsis, acute coronary syndrome and many other disease states (1,2).


The Evidence Investigator MIP-1α assay is a sandwich chemiluminescent immunoassay for the detection of MIP-1α in human serum and plasma.


1. Maurer, M., von Stebut, E. (2004) Macrophage inflammatory protein-1. Int. J. Biochem. Cell Biol. 36(10):1882-6.

2. Menten, P., Wuyts, A., Van Damme, J. (2002) Macrophage inflammatory protein-1. Cytokine Growth Factor Rev. 13(6):455-81.

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