Chemerin ELISA

产品名称：Chemerin ELISA
产    地：Demeditec 
产品货号：DEE0102
产品规格：96 Tests
产品说明：
Special remarks:
INTENDED USE
Measurement of human Chemerin in human serum and plasma samples.
INTRODUCTION
Chemerin, also known as tazarotene-induced gene 2 (TIG2) or retinoic acid receptor responder 2 (RARRES2), is synthesized as precursor protein of 163 amino acids including a N-terminal signal peptide of 20 amino acids, which is chipped of enduring secretion. The inactive, circulation proform of Chemerin contains six cystein residues and thus three intramolecular disulfide bridges are
suggested.
Prochemerin expression has been demonstrated for liver, lung, pituitary, lymph node, stomach and adipose tissue. It has been detected in blood, ascitic fluids from ovary and liver cancer and synovial fluids from arthritic patients. Different receptors have been found in spleen, lymph node, small intestine, lung tissue as well as in macrophages and immature dendritic cells.
Prochemerin is converted into its biologically active form by serine or cystein proteases, resulting in pro- or anti-inflammatory actions of the active protein, respectively. Proteolytic cleavage of Chemerin has been described for following serine proteases tryptase, plasmin, elastase, cathepsin G as well as for the cystein proteases cathepsin S and calpains.
The active protein is involved in innate and adaptive immune responses and for instance acts as a strong chemoattractant for immature dendritic cells and macrophages. It influences intracellular signaling by binding to its specific receptors. The C-terminal domain of Chemerin allows binding to the receptor ChemR23/CMKLR1 and elicits a pro-inflammatory stimulus by inducing Ca2+ influx and ERK1/2 activation. Further, the N-terminal domain of Chemerin binds to the CCRL2 receptor and allows presentation of the C-terminal domain to neighbor cells. In case of Prochemerin cleavage by cystein proteases the resulting peptides act inhibitory on the ChemR23/CMKLR1 receptors and thus have anti-inflammatory effects.
Recently, the relevance of Chemerin in adipogenesis and adipocyte metabolism has been discovered. Goralski et al. demonstrated in mice that Chemerin as well as receptor (ChemR23) expression is present in adipocytes of visceral and subcutaneous adipose tissue. The expression and secretion increases enduring adipocyte differentiation. The active Chemerin of 16 kDa has been found in the conditioned media of adipocytes. Intracellular signaling networks in adipocytes are also influenced by Chemerin e.g. stimulation of MAPK p42/44 (ERK1/2) phosphorylation was demonstrated. Further, the authors also show a post-differentiational effect of Chemerin on gene expression in adipocytes. Based on these results an influence of Chemerin on metabolic syndrome and insulin resistance was purposed. This studies reveal that Chemerin is more expressed by adipose tissue of obese patients and is able to impair insulin sensitivity of muscle cells and insulin mediated lipolysis and lipogenesis in adipocytes. It has been shown that Chemerin is associated with markers of inflammation and components of the metabolic syndrome as well as with renal function.
For the further investigation of Chemerin functions and its quality as biomarker in metabolic diseases reliable measurement of Chemerin in different body fluids is a prerequisite. Demeditec offers a sensitive and reproducible test system for the quantitative measurement of Chemerin. Based on highly specific antibodies total Chemerin is measured.
上海玉博生物技术有限公司在为生命科学领域提供丰富的产品与信息资源方面处于国内**地位，公司提供的产品涵盖了二十多个国家近五十万种产品，而且产品的数量与信息在不断的增长和更新，公司提供的产品能够使生命科学工作者加快对生物化学，分子生物学，细胞生物学以及蛋白质组学研究的认知，以及分子诊断和临床医学领域的应用。

产品留言

标题

联系人

联系电话

内容

验证码

点击换一张

注：1.可以使用快捷键Alt+S或Ctrl+Enter发送信息!
2.如有必要,请您留下您的详细联系方式!