Recombinant Human Chemerin Protein


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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human Chemerin Protein Summary

Details of Functionality
Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human ChemR23. The ED50 for this effect is 4-20 ng/mL.
E. coli-derived human Chemerin protein
Glu21-Ser157, with an N-terminal Met
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
16 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Read Publications using
2324-CM in the following applications:

Packaging, Storage & Formulations

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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


This product and/or its use is the subject of European Patent 1 405 083 B1, US Patents 7,332,291; 7,419,658 and 7,842,453 as well as foreign equivalents licensed to R&D Systems Inc. The purchase of this product is intended for research purposes only, not including the screening of compounds for the development of therapeutic and/or diagnostic products. Buyers may require a separate license to the patent rights for applications beyond such research purposes.

For information on licensing please contact Euroscreen SA rue Adrienne Bolland n°47 B-6041 Gosselies Belgium. Phone: +32-71-348500, Fax: +32-71-348519, e-mail Attention: Dr. Vincent Lannoy.

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Chemerin Protein

  • Chemerin
  • RAR-responsive protein TIG2
  • retinoic acid receptor responder (tazarotene induced) 2
  • retinoic acid receptor responder protein 2
  • Tazarotene-induced gene 2 protein
  • TIG-2
  • TIG2HP10433


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).

  1. Nagpal, S. et al. (1997) J. Invest. Dermatol. 109:91.
  2. Storici, P. et al. (1996) Eur. J. Biochem. 238:769.
  3. Zanetti, M. (2004) J. Leukoc. Biol. 75:39.
  4. Wittamer, V. et al. (2004) J. Biol. Chem. 279:9956.
  5. Meder, W. et al. (2003) FEBS Lett. 555:495.
  6. Yokoyama-Kobayashi, M. et al. (1999) Gene 228:161.
  7. Wittamer, V. et al. (2003) J. Exp. Med. 198:977.
  8. Busmann, A. et al. (2004) J. Chromatog. B 811:217.

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Publications for Chemerin (2324-CM)(7)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 3 applications: Assay Standard, Bioassay, ELISA Standard.

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Showing Publications 1 - 7 of 7.
Publications using 2324-CM Applications Species
Kerry B Goralski CMKLR1 activation ex vivo does not increase proportionally to serum total chemerin in obese humans Endocr Connect, 2016;5(6):70-81. 2016 [PMID: 27881447] (Assay Standard) Assay Standard
JD Kumar, S Kandola, L Tiszlavicz, Z Reisz, GJ Dockray, A Varro The role of chemerin and ChemR23 in stimulating the invasion of squamous oesophageal cancer cells Br. J. Cancer, 2016;114(10):1152-9. 2016 [PMID: 27092781] (Bioassay, Human) Bioassay Human
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 Increased expression of chemerin in squamous esophageal cancer myofibroblasts and role in recruitment of mesenchymal stromal cells. PLoS ONE, 2014;9(7):e104877. 2014 [PMID: 25127029] (Bioassay, Human) Bioassay Human
Doyle J, Krishnaji S, Zhu G, Xu Z, Heller D, Ji R, Levy B, Kumar K, Kopin A Development of a membrane-anchored chemerin receptor agonist as a novel modulator of allergic airway inflammation and neuropathic pain. J Biol Chem, 2014;289(19):13385-96. 2014 [PMID: 24659779] (Bioassay, Human) Bioassay Human
Zhou J, Liao D, Zhang S, Cheng N, He H, Ye R Chemerin C9 peptide induces receptor internalization through a clathrin-independent pathway. Acta Pharmacol Sin, 2014;35(5):653-63. 2014 [PMID: 24658352] (Bioassay, Human) Bioassay Human
Schipper HS, De Jager W, van Dijk ME, Meerding J, Zelissen PM, Adan RA, Prakken BJ, Kalkhoven E A multiplex immunoassay for human adipokine profiling. Clin. Chem., 2010;56(0):1320. 2010 [PMID: 20530731]
Du XY, Zabel BA, Myles T, Allen SJ, Handel TM, Lee PP, Butcher EC, Leung LL Regulation of chemerin bioactivity by plasma carboxypeptidase N, carboxypeptidase B (activated thrombin-activable fibrinolysis inhibitor), and platelets. J. Biol. Chem., 2009;284(2):751-8. 2009 [PMID: 19010784] (ELISA Standard, N/A) ELISA Standard N/A

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Gene Symbol RARRES2