Human Chemerin Antibody Summary
Glu21-Ser157
Accession # Q99969
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
Detection of Human Chemerin by Western Blot. Western blot shows lysates of human kidney tissue and human liver tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Chemerin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2324) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF019). A specific band was detected for Chemerin at approximately 18 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Human Chemerin by Simple WesternTM. Simple Western lane view shows lysates of human kidney tissue, loaded at 0.2 mg/mL. A specific band was detected for Chemerin at approximately 24 kDa (as indicated) using 50 µg/mL of Goat Anti-Human Chemerin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2324) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
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
Human 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 163 aa precursor that contains a hydrophobic 20 aa N-terminal sequence, an intervening 137 aa Cystatin-fold containing domain, and a six aa C-terminal prosegment (1, 4). Within the cystatin-fold domain there are three intrachain disulfide bonds that contribute to the fold, and three potential sites for phosphorylation and one for myristoylation (5). The precursor molecule undergoes proteolytic processing at both termini by unknown proteases. The N-terminal residue 20 aa hydrophobic segment is described as being either a signal sequence or a transmembrane (TM) segment for a type II TM protein (1, 6). In either case, it gives rise to a soluble proform that undergoes further processing at the C-terminus. In human, the C-terminal six residues are cleaved, giving rise to a monomeric, 16 kDa heparin-binding bioactive molecule (aa 21 - 157) (7). A shorter 134 aa form has been described (5). Bioactivity seems to be concentrated in the nine residues preceding the prosegment (aa 149 ‑ 157). Retention of the prosegment blocks activity (4). The 137 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 (7). 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 human Chemerin shares 67% aa sequence identity with mouse Chemerin (7). There is apparently cross-species activity for the protein (8).
- 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.
- Meder, W. et al., (2003) FEBS Lett. 555:495.
- Yokoyama-Kobayashi, M. et al., (1999) Gene 228:161.
- Wittamer, V. et al., (2003) J. Exp. Med. 198:977.
- Busmann, A. et al., (2004) J. Chromatog. B 811:217.
Product Datasheets
Citations for Human 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 Isoform-Specific Effects on Hepatocyte Migration and Immune Cell Inflammation
Authors: Susanne Feder, Astrid Bruckmann, Nichole McMullen, Christopher J. Sinal, Christa Buechler
International Journal of Molecular Sciences
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Surface-enhanced Raman scattering for the detection of polycystic ovary syndrome
Authors: A Momenpour, PDA Lima, YA Chen, CR Tzeng, BK Tsang, H Anis
Biomed Opt Express, 2018-01-25;9(2):801-817.
Species: Human
Sample Types: Follicular Fluid
Applications: Western Blot -
Expression of human chemerin induces insulin resistance in the skeletal muscle but does not affect weight, lipid levels, and atherosclerosis in LDL receptor knockout mice on high-fat diet.
Authors: Becker M, Rabe K, Lebherz C, Zugwurst J, Goke B, Parhofer KG, Lehrke M, Broedl UC
Diabetes, 2010-08-19;59(11):2898-903.
Species: Human
Sample Types: Serum
Applications: Western Blot -
Insulin and metformin regulate circulating and adipose tissue chemerin.
Authors: Tan BK, Chen J, Farhatullah S, Adya R, Kaur J, Heutling D, Lewandowski KC, O'Hare JP, Lehnert H, Randeva HS
Diabetes, 2009-06-05;58(9):1971-7.
Species: Human
Sample Types: Tissue Homogenates
Applications: Western Blot -
Regulation of chemerin bioactivity by plasma carboxypeptidase N, carboxypeptidase B (activated thrombin-activable fibrinolysis inhibitor), and platelets.
Authors: Du XY, Zabel BA, Myles T, Allen SJ, Handel TM, Lee PP, Butcher EC, Leung LL
J. Biol. Chem., 2008-11-14;284(2):751-8.
Species: Human
Sample Types: Plasma
Applications: ELISA Development -
Urinary chemerin as a potential biomarker for inflammatory bowel disease
Authors: Stefan Gunawan, Tanja Elger, Johanna Loibl, Tanja Fererberger, Stefanie Sommersberger, Arne Kandulski et al.
Frontiers in Medicine
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