Human Chemerin
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| Amount : | 100 µg |
| Purification : | Reducing and Non-Reducing SDS PAGE at >= 95% |
| Content : | Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA) Sterile water at 0.1 mg/mL |
| Storage condition : | Store at -20°C |
| AA sequence : | MELTEAQRRG LQVALEEFHK HPPVQWAFQE TSVESAVDTP FPAGIFVRLE FKLQQTSCRK RDWKKPECKV RPNGRKRKCL ACIKLGSEDK VLGRLVHCPI ETQVLREAEE HQETQCLRVQ RAGEDPHSFY FPGQFAFS |
Source: Genetically modified E.coli.
Predicted MW: Monomer, 16 kDa (138 aa)
Chemerin is a chemoattractant adipokine that is expressed in white adipose, liver, skin, and lung tissues. Chemerin is a ligand for the G protein-coupled receptor chemokine-like receptor 1 (ChemR23), which is expressed on dendritic cells, macrophages, and adipocytes. Chemerin functions to recruit macrophages to sites of tissue damage and inflammation. Chemerin is also a regulator of glucose metabolism in the liver. Due to the roles of chemerin during metabolism and inflammation, it may be a key factor in obesity-related diseases such as type 2 diabetes mellitus.
Endotoxin: Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Centrifuge vial before opening, Suspend the product by gently pipetting the above recommended solution down the sides of the vial. DO NOT VORTEX. Allow several minutes for complete reconstitution. For prolonged storage, dilute to working aliquots in a 0.1% BSA solution, store at -80°C and avoid repeat freeze thaws. Upon reconstitution, a small amount of visible precipitate can be expected. A 10% overfill has been added to the total material vialed to compensate for this loss.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Secreted |
| Post transnational modification: | Secreted in an inactive precursor form, prochemerin, which is proteolytically processed by a variety of extracellular proteases to generate forms with differing levels of bioactivity. For example, the removal of six amino acids results in chemerin-157, which exhibits the highest activity, while removal of seven amino acids results in chemerin-156 which has slightly less activity. Some proteases are able to cleave at more than one site and chemerin forms may be sequentially processed by different enzymes to modulate activity levels. The coordinated expression and activity of chemerin-modifying enzymes is essential for regulating its bioactivation, inactivation and, consequently, biological function. Cathepsin G cleaves seven C-terminal amino acids from prochemerin (chemerin-156), elastase is able to cleave six (chemerin-157), eight (chemerin-155) or eleven (chemerin-152), plasmin cleaves five amino acids (chemerin-158), and tryptase cleaves five (chemerin-158) or eight (chemerin-155). Multiple cleavages might be required to fully activate chemerin, with an initial tryptase cleavage resulting in chemerin with low activity (chemerin-158), and a second cleavage by carboxypeptidase N or B producing highly active chemerin (chemerin-157). |
| Tissue Specificity: | Expressed at the highest levels in placenta, liver, and white adipose tissue (WAT), and to a lesser extent in many other tissues such as lung, brown adipose tissue, heart, ovary, kidney, skeletal muscle and pancreas. Within WAT, expression is enriched in adipocytes as compared to the stromal vascular fraction. Expression and secretion increases dramatically with adipogenesis. Highly expressed in skin (basal and suprabasal layers of the epidermis, hair follicles and endothelial cells). Expression is elevated in numerous metabolic and inflammatory diseases including psoriasis, obesity, type 2 diabetes, metabolic syndrome and cardiovascular disease. |
| BioGrid: | 111854. 4 interactions. |
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