Recombinant Human Chemerin protein (rFc Tag) (HPLC verified)

Species

Human

Purity

>90 %, SDS-PAGE
>90 %, SEC-HPLC

Tag

rFc Tag

Activity

not tested

Cat no : Eg3688

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Validation Data Gallery

• 

  Purity of Recombinant Human Chemerin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

• 

  The purity of Human Chemerin was greater than 90% as determined by SEC-HPLC.

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Product Information

• Purity: >90 %, SDS-PAGE; >90 %, SEC-HPLC
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Human Chemerin protein Glu21-Ser157 (Accession# Q99969) with a rabbit IgG Fc tag at the C-terminus.
• GeneID: 5919
• Accession: Q99969
• PredictedSize: 42.2 kDa
• SDS-PAGE: 42-48 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Chemerin, also named as TIG2 and RARRES2, is adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). It positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. RARRES2 have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases.

References:

1. Bozaoglu K, et al. (2007). Endocrinology, Oct;148(10):4687-94.
2. Ernst, M. C., et al. (2010). Trends Endocrinol Metab.Nov;21(11):660-667. 
3. Mattern A, et al. (2014). IUBMB Life. Jan;66(1):19-26.