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Chemerin Human ELISA

Other names: Tezarotene induced gene 2, TIG2, Retinoic acid receptor responder 2, RERRES2 Product of BioVendor
Product: Size:
RD191136200R (regulatory status: RUO) 96 wells (1 kit)
Files: Datasheet PDF (RUO)MSDS (RUO)

Product details


Summary

Chemerin is a novel chemoattractant protein secreted as an 18-kDa inactive pro-protein. Active chemerin is abundant in ascetic fluid from ovariam cancer patients and synovial fluid from patients with arthritis. Signaling by chemerin is mediated by the seven-transmembrane-spanning G protein-coupled receptor, chemokine like receptor-1 (CMKLR1, ChemR23,) or chemerinR. Both chemerin and chemerinR mRNA expression dramatically increased during the differentiation of preadipocytes into adipocytes. Chemerin induced the phosphorylation of extracellular signal – regulated kinase 1/2 (ERK 1/2) and lipolysis in differentiated adipocytes and 3T3-L1 cells, stimulated intracellular calcium release and inhibited cAMP accumulation. Chemerin disruption has some effect on adipogenesis in vitro, but regulation of gene expression and lipolysis in mature adipocytes suggests a wider role in lipid and carbohydrate metabolisms, and perhaps insulin sensitivity. Local production of chemerin regulates adipogenesis and through its receptor or possible other receptor can modulate a variety of functions in mature adipocytes. Adipocytes purified from adipose tissue contain high levels of chemerin mRNA; however, substantial expression in stromal vascular cells suggest that production in nonadipocytes may also be important. Chemerin is essential in early differentiation processes and may contribute or regulate critical early events in adipogenesis. Results also indicate that chemerin and ChemerinR could have an important biological role in the formation of white adipose tissue during normal or in pathological states.

Features

  • It is intended for research use only.
  • The total assay time is less than 3.5 hours.
  • The kit measures chemerin in serum and plasma (EDTA, citrate, heparin).
  • Assay format is 96 wells.
  • Standard is recombinant protein based
  • Quality Controls are human serum based. No animal sera are used.
  • Components of the kit are provided ready to use, concentrated or lyophilized.

Research topic

Energy metabolism and body weight regulation


Assay format

Sandwich ELISA, Biotin-labelled antibody

Applications

Plasma, Serum

Sample requirements

5 μl

Storage/Shipping

Store the complete kit at 2–8°C.

Calibration Curve

Calibration range

0.25 – 8 ng/ml

Limit of detection

0.1 ng/ml

Intra-assay (Within-Run, n=8)

CV = 6.0%

Inter-assay (Run-to-Run, n=6)

CV = 7.6 %

Spiking Recovery

CV = 96.4%

Dilution Linearity

CV = 103.2%

Cross-Reactivity

Monkey, Rabbit


References to this product

  • Sell H, Divoux A, Poitou C, Basdevant A, Bouillot JL, Bedossa P, Tordjman J, Eckel J, Clement K. Chemerin Correlates with Markers for Fatty Liver in Morbidly Obese Patients and Strongly Decreases after Weight Loss Induced by Bariatric Surgery. J Clin Endocrinol Metab. 2010 Apr 7;
  • Sell H, Laurencikiene J, Taube A, Eckardt K, Cramer A, Horrighs A, Arner P, Eckel J. Chemerin is a novel adipocyte-derived factor inducing insulin resistance in primary human skeletal muscle cells. Diabetes. 2009 Dec;58 (12):2731-40
  • Stejskal D, Karpisek M, Hanulova Z, Svestak M. Chemerin is an independent marker of the metabolic syndrome in a Caucasian population--a pilot study. Biomed Pap Med Fac Univ Palack. 2008 Dec;152 (2):217-21
  • Pfau D, Stepan H, Kratzsch J, Verlohren M, Verlohren HJ, Drynda K, Lossner U, Bluher M, Stumvoll M, Fasshauer M. Circulating Levels of the Adipokine Chemerin in Gestational Diabetes Mellitus. Horm Res Paediatr. 2010 Apr 29;
  • Ress C, Tschoner A, Engl J, Klaus A, Tilg H, Ebenbichler CF, Patsch JR, Kaser S. Effect of bariatric surgery on circulating chemerin levels. Eur J Clin Invest. 2010 Jan 25;
  • Pfau D, Bachmann A, Lossner U, Kratzsch J, Bluher M, Stumvoll M, Fasshauer M. Serum levels of the adipokine chemerin in relation to renal function. Diabetes Care. 2010 Jan;33 (1):171-3

References to summary

  • 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
  • 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
  • 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
  • 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
  • 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

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