Measured by its ability to neutralize Chemerin-induced chemotaxis in the BaF3 mouse pro‑B cell line transfected with human Chem R23. The Neutralization Dose (ND50) is typically 3-9 µg/mL in the presence of 100 ng/mL Recombinant Mouse Chemerin.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Chemotaxis Induced by Chemerin and Neutralization by Mouse Chemerin Antibody.
Recombinant Mouse Chemerin (Catalog # 2325-CM) chemoattracts the BaF3 mouse pro‑B cell line transfected with human Chem R23 in a dose-dependent manner (orange line). The amount of cells that migrated through to the lower chemotaxis chamber was measured by Resazurin (Catalog # AR002). Chemotaxis elicited by Recombinant Mouse Chemerin (100 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Mouse Chemerin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2325). The ND50 is typically 3-9 µg/mL.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Mouse Chemerin, also known as Tazarotene-induced Gene-2 (TIG2), is a new, but distant member of the cystatin superfamily (1-3). Members of this superfamily contain at least two intrachain disulfide bonds and an alpha -helical structure over a distance of about 100 amino acids (2, 3). Chemerin is synthesized as a 162 amino acid (aa) precursor that contains a hydrophobic N-terminal sequence, an intervening 140 aa cystatin-fold containing domain, and a six aa C-terminal prosegment (4-6). Within the cystatin-fold domain there are three intrachain disulfide bonds that contribute to the characteristic fold (4, 7). The precursor molecule is described as undergoing proteolytic processing at both termini by unknown proteases. The N-terminal 16 residue hydrophobic segment is described as being either a signal sequence or a transmembrane (TM) segment for a type II TM protein (5, 8). In either case it gives rise to a soluble proform that undergoes further processing at the C‑terminus (5). In mouse, the C-terminal six residues are cleaved, giving rise to a monomeric, 16 kDa heparin-binding bioactive molecule (aa 17-156) (5-7). A shorter form has been described in human (7). The activity seems to be concentrated in the nine aa’s preceding the prosegment (aa 148-156). Retention of the prosegment blocks activity (4). The 140 aa mature segment is known to bind to the G-protein coupled receptor termed ChemR23 (5, 7). Binding results in macrophage and immature dendritic cell chemotaxis (5). The distribution of this receptor is limited to immune APCs, and it is assumed that Chemerin is an inflammatory molecule. It is unclear which cells are actually producing Chemerin, but keratinocytes, endothelial cells and osteoclasts are potential candidates (1, 7). Mature mouse Chemerin shares 67%, 84%, and 82% aa sequence identity to human, rat, and hamster Chemerin, respectively (6). There is apparently cross-species activity for the protein (6).
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Meder, W. et al. (2003) FEBS Lett. 555:495.
Yokoyama-Kobayashi, M. et al. (1999) Gene 228:161.
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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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