Mouse Chemerin Antibody Summary
Thr17-Ser156
Accession # Q9DD06
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Chemotaxis Induced by Chemerin and Neutralization by Mouse Chemerin Antibody. Recombinant Mouse Chemerin (Catalog # 2325-CM) chemo-attracts 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 (AR002). Chemotaxis elicited by Recombinant Mouse Chemerin (100 ng/mL) is neutralized (green line) by increasing concentrations of Rat Anti-Mouse Chemerin Monoclonal Antibody (Catalog # MAB2325). The ND50 is typically 1-5 µg/mL.
Reconstitution Calculator
Preparation and Storage
- 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.
Background: Chemerin
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 (aa) (2, 3). Chemerin is synthesized as a 162 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).
- Nagpal, S. et al. (1997) J. Invest. Dermatol. 109:91.
- Storici, P. et al. (1996) Eur. J. Biochem. 238:769.
- Zanetti, M. (2004) J. Leukoc. Biol. 75:39.
- Wittamer, V. et al. (2004) J. Biol. Chem. 279:9956.
- Wittamer, V. et al. (2003) J. Exp. Med. 198:977.
- Busmann, A. et al. (2004) J. Chromatog. B 811:217.
- Meder, W. et al. (2003) FEBS Lett. 555:495.
- Yokoyama-Kobayashi, M. et al. (1999) Gene 228:161.
Product Datasheets
Citations for Mouse Chemerin Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. 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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Chemerin regulates formation and function of brown adipose tissue: Ablation results in increased insulin resistance with high fat challenge and aging
Authors: Yiqiang Zhang, Wen‐Jun Shen, Shuo Qiu, Pinglin Yang, Garrett Dempsey, Lei Zhao et al.
The FASEB Journal
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The role of chemerin and ChemR23 in stimulating the invasion of squamous oesophageal cancer cells
Authors: JD Kumar, S Kandola, L Tiszlavicz, Z Reisz, GJ Dockray, A Varro
Br. J. Cancer, 2016-04-19;114(10):1152-9.
Species: Human
Sample Types: Whole Cells
Applications: Neutralization -
Increased expression of chemerin in squamous esophageal cancer myofibroblasts and role in recruitment of mesenchymal stromal cells.
Authors: Kumar, J Dinesh, Holmberg, Chris, Kandola, Sandhir, Steele, Islay, Hegyi, Peter, Tiszlavicz, Laszlo, Jenkins, Rosalind, Beynon, Robert J, Peeney, David, Giger, Olivier, Alqahtani, Ahlam, Wang, Timothy, Charvat, Trevor T, Penfold, Mark, Dockray, Graham J, Varro, Andrea
PLoS ONE, 2014-08-15;9(7):e104877.
Species: Mouse
Sample Types: Whole Cells
Applications: Neutralization
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