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Manufactured by BioVendor

Chemerin Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Tezarotene induced gene 2, TIG2, Retinoic acid receptor responder 2, RERRES2
  • Species:Human
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Cat. No. Size Price

RBG10104005 5 µg
RBG10104025 25 µg
RBG10104100 100 μg
PubMed Product Details
Technical Data


Recombinant protein


Chemerin is a secreted chemoattractant protein that can signal through the chemokine-like receptor-1 (CMKLR1). It is expressed in various tissues, including white adipose tissue, and circulates in blood as an inactive 143 amino acid precursor protein. Biologically active Chemerin is generated by proteolytic removal of C-terminal residues by several circulating proteases. Chemerin acts as a chemoattractant for cells expressing the CMKLR1 receptor, which includes certain dendritic cells, macrophages, and adipocytes. Recombinant Human Chemerin is a 15.6 kDa protein consisting of 135 amino acid residues.

Amino Acid Sequence



E. coli



Biological Activity

Determined by its ability to chemoattract human immature dendritic cells using a concentration range of 1.0–100.0 ng/ml.


Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).


Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C




Research topic

Energy metabolism and body weight regulation

Summary References (7)

References to Chemerin

  • Bozaoglu K, Bolton K, McMillan J, Zimmet P, Jowett J, Collier G, Walder K, Segal D. Chemerin is a novel adipokine associated with obesity and metabolic syndrome. Endocrinology. 2007 Oct;148 (10):4687-94
  • Goralski KB, McCarthy TC, Hanniman EA, Zabel BA, Butcher EC, Parlee SD, Muruganandan S, Sinal CJ. Chemerin, a novel adipokine that regulates adipogenesis and adipocyte metabolism. J Biol Chem. 2007 Sep 21;282 (38):28175-88
  • MacDougald OA, Burant CF. The rapidly expanding family of adipokines. Cell Metab. 2007 Sep;6 (3):159-61
  • Parolini S, Santoro A, Marcenaro E, Luini W, Massardi L, Facchetti F, Communi D, Parmentier M, Majorana A, Sironi M, Tabellini G, Moretta A, Sozzani S. The role of chemerin in the colocalization of NK and dendritic cell subsets into inflamed tissues. Blood. 2007 May 1;109 (9):3625-32
  • Roh SG, Song SH, Choi KC, Katoh K, Wittamer V, Parmentier M, Sasaki S. Chemerin--a new adipokine that modulates adipogenesis via its own receptor. Biochem Biophys Res Commun. 2007 Nov 3;362 (4):1013-8
  • Takahashi M, Takahashi Y, Takahashi K, Zolotaryov FN, Hong KS, Kitazawa R, Iida K, Okimura Y, Kaji H, Kitazawa S, Kasuga M, Chihara K. Chemerin enhances insulin signaling and potentiates insulin-stimulated glucose uptake in 3T3-L1 adipocytes. FEBS Lett. 2008 Mar 5;582 (5):573-8
  • Wittamer V, Franssen JD, Vulcano M, Mirjolet JF, Le Poul E, Migeotte I, Brezillon S, Tyldesley R, Blanpain C, Detheux M, Mantovani A, Sozzani S, Vassart G, Parmentier M, Communi D. Specific recruitment of antigen-presenting cells by chemerin, a novel processed ligand from human inflammatory fluids. J Exp Med. 2003 Oct 6;198 (7):977-85
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