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Recombinant Human Chemerin Protein

Bio-Techne includes R&D Systems | Catalog # 2324-CM

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Carrier Free
2324-CM-025/CF

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With Carrier
2324-CM-025

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

E. coli-derived human Chemerin protein
Glu21-Ser157, with an N-terminal Met

Purity

>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

16 kDa

Activity

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.

Formulation, Preparation and Storage

Carrier Free
What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Carrier: 2324-CM
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage 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.
Carrier Free: 2324-CM/CF
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage 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.

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).

References

  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.

Long Name

Retinoic Acid Receptor Responder Protein 2

Alternate Names

RARRES2, TIG-2

Entrez Gene IDs

5919 (Human); 71660 (Mouse)

Gene Symbol

RARRES2

UniProt

Additional Chemerin Products

Product Documents for Recombinant Human Chemerin Protein

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Chemerin Protein

For research use only

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