ELISA

Insulin-like growth factor(IGF)-binding protein-3(IGFBP-3) is a major determinant of circulating levels of the IGFs and is clinically useful for the evaluation of GH deficiency and for predicting the response to GH treatment. The circulating level of IGFBP-3 is inversely related to the risk of several common cancers, and that antiproliferative agents such as antiestrogens and retinoids act in part by up-regulating IGFBP-3 gene(IGFBP3) expression. Insulin-like growth factor-binding protein(IGFBP)-3, well characterized as the carrier of insulin-like growth factor(IGF), has been reported to have intrinsic bioactivity that is independent of IGF binding. IGFBP-3 has an IGF-independent, antiproliferative effect in undifferentiated and early differentiated but not in terminally differentiated chondrocytes. IGFBP-3 possesses both growth-inhibitory and potentiating effects on cells that are independent of IGF action and are mediated through specific. IGFBP-3 binding proteins/receptors locate at

Insulin-like growth factor-binding protein 4 is a protein that in humans is encoded by the IGFBP4gene. This gene is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma in both glycosylated and non-glycosylated forms. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. In addition, IGFBP-4 is a unique protein and it consistently inhibits several cancer cells in vivo and in vitro. Its inhibitory action has been shown in vivo in prostate and colon. It is secreted by all colon cancer cells.

Interleukin-1 alpha(IL-1 alpha) and interleukin-1 beta(IL-1 beta) are two biochemically distinct, but distantly related, polypeptidic cytokines that play a key role in inflammation, immunologic reactions, and tissue repair. IL-1 alpha has been implicated in the pathogenesis of infectious, autoimmune and inflammatory diseases. Recently, it has been shown that IL-1 alpha is identical to hematopoietin 1, which is described as a hematopoietic growth factor acting on early progenitor cells in synergy with other hematopoietic growth factors. The human interleukin 1 alpha gene is assigned to chromosome 2. Genetic polymorphisms at interleukin(IL)-1alpha and IL-1beta have been recently suggested to be associated with severity of adult periodontitis. The murine IL-1 alpha and IL-1 beta genes encode structurally and evolutionarily related cytokines that exert a regulatory role in numerous physiological processes including hemopoiesis. The standard product used in this kit is recombinant human IL-

Interleukin-1 alpha(IL-1 alpha) and interleukin-1 beta(IL-1 beta) are two biochemically distinct, but distantly related, polypeptidic cytokines that play a key role in inflammation, immunologic reactions, and tissue repair. IL-1 alpha has been implicated in the pathogenesis of infectious, autoimmune and inflammatory diseases. Recently, it has been shown that IL-1 alpha is identical to hematopoietin 1, which is described as a hematopoietic growth factor acting on early progenitor cells in synergy with other hematopoietic growth factors.1 The human interleukin 1 alpha gene is assigned to chromosome 2. Genetic polymorphisms at interleukin(IL)-1alpha and IL-1beta have been recently suggested to be associated with severity of adult periodontitis. The murine IL-1 alpha and IL-1 beta genes encode structurally and evolutionarily related cytokines that exert a regulatory role in numerous physiological processes including hemopoiesis. The standard product used in this kit is recombinant rat IL-1

Interleukin-1 alpha(IL-1 alpha) and interleukin-1 beta(IL-1 beta) are two biochemically distinct, but distantly related, polypeptidic cytokines that play a key role in inflammation, immunologic reactions, and tissue repair. IL-1 alpha has been implicated in the pathogenesis of infectious, autoimmune and inflammatory diseases. Recently, it has been shown that IL-1 alpha is identical to hematopoietin 1, which is described as a hematopoietic growth factor acting on early progenitor cells in synergy with other hematopoietic growth factors.1 The human interleukin 1 alpha gene is assigned to chromosome 2. Genetic polymorphisms at interleukin(IL-1alpha and IL-1beta) have been recently suggested to be associated with severity of adult periodontitis. The murine IL-1 alpha and IL-1 beta genes encode structurally and evolutionarily related cytokines that exert a regulatory role in numerous physiological processes including hemopoiesis. The standard product used in this kit is recombinant mouse IL

Interleukin-1beta(IL-1beta) is a potent stimulator of bone resorption whose gene is mapped to 2q14, and has been implicated in the pathogenesis of high bone turnover and osteoporosis. IL-1beta, a prominent microglia-derived cytokine, caused oligodendrocyte death in coculture with astrocytes and microglia, but not in pure culture of oligodendrocytes alone. It also can cause nuclear export of a specific NCOR corepressor complex, resulting in derepression of a specific subset of nuclear factor-kappa-B(NFKB)-regulated genes. Furthermore, Microenvironmental IL-1beta and, to a lesser extent, IL-1alpha are required for in vivo angiogenesis and invasiveness of different tumor cells. Additional, the cooperation of IL-1beta and PDGFB induces contractile-to-synthetic phenotype modulation of human aortic smooth muscle cells in culture. Moreover, the association with disease may be explained by the biologic properties of IL-1beta, which is an important proinflammatory cytokine and a powerful inhibi

The Interleukin 1 family is a group of 11 beta trefoil cytokines. Interleukin-1, produced mainly by blood monocytes, mediates the panoply of host reactions collectively known as acute phase response . Interleukin-1beta(IL-1beta) is a potent stimulator of bone resorption, and has been implicated in the pathogenesis of high bone turnover and osteoporosis. IL-1beta belongs to proinflammatory cytokines, promote cancer cell adhesion and liver metastases by up-regulating the expression of vascular cell adhesion molecule-1(VCAM-1) on hepatic sinusoidal endothelium(HSE).

Interleukin-1beta(IL-1beta) is a potent stimulator of bone resorption whose gene is mapped to 2q14, and has been implicated in the pathogenesis of high bone turnover and osteoporosis. IL-1beta, a prominent microglia-derived cytokine, caused oligodendrocyte death in coculture with astrocytes and microglia, but not in pure culture of oligodendrocytes alone1. It also can cause nuclear export of a specific NCOR corepressor complex, resulting in derepression of a specific subset of nuclear factor-kappa-B(NFKB)-regulated genes2. Furthermore, Microenvironmental IL-1beta and, to a lesser extent, IL-1alpha are required for in vivo angiogenesis and invasiveness of different tumor cells3. Additional, the cooperation of IL-1beta and PDGFB induces contractile-to-synthetic phenotype modulation of human aortic smooth muscle cells in culture4. Moreover, the association with disease may be explained by the biologic properties of IL-1beta, which is an important proinflammatory cytokine and a powerful in

Interleukin 1 receptor, type I(IL1R1), also known as CD121a(Cluster of Differentiation 121a), is an interleukin receptor. The protein encoded by this gene is a cytokine receptor that belongs to the interleukin-1 receptor family. IL1R1 along with interleukin 1 receptor, type II(IL1R2), interleukin 1 receptor-like 2(IL1RL2), and interleukin 1 receptor-like 1(IL1RL1) form a cytokine receptor gene cluster in a region mapped to chromosome 2q12. This protein is a receptor for interleukin 1 alpha(IL1A), interleukin 1 beta(IL1B), and interleukin 1 receptor antagonist(IL1RA). It is an important mediator involved in many cytokine induced immune and inflammatory responses.