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Recombinant Human Chemerin Protein

Catalog #: 2324-CM
13 Citations Datasheet / COA / SDS

Carrier Free

Catalog # Availability Size / Price Qty
2324-CM-025/CF

With Carrier

Catalog # Availability Size / Price Qty
2324-CM-025
R&D Systems Recombinant Proteins and Enzymes
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Citations (13)
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human Chemerin Protein Summary

Product Specifications

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.
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.
Source
E. coli-derived human Chemerin protein
Glu21-Ser157, with an N-terminal Met
Accession #
Q99969
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
16 kDa

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2324-CM (with carrier)

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2324-CM/CF (carrier free)

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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.

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.

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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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
Entrez Gene IDs
5919 (Human); 71660 (Mouse)
Alternate Names
Chemerin; RARRES2; 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

Citations for Recombinant Human Chemerin Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

13 Citations: Showing 1 - 10
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  1. Refining Evaluation of Bone Mass and Adipose Distribution in Dunnigan Syndrome
    Authors: Moreira, MLM;de Araújo, IM;Fukada, SY;Venturini, LGR;Guidorizzi, NR;Garrido, CE;Rosen, CJ;de Paula, FJA;
    International journal of molecular sciences
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. The Chemerin/CMKLR1 Axis Is Involved in the Recruitment of Microglia to Abeta Deposition through p38 MAPK Pathway
    Authors: Y Chen, Z Liu, P Gong, H Zhang, Y Chen, S Yao, W Li, Y Zhang, Y Yu
    International Journal of Molecular Sciences, 2022-08-12;23(16):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. The antitumoral effects of chemerin are independent from leukocyte recruitment and mediated by inhibition of neoangiogenesis
    Authors: I Dubois-Ved, D Al Delbany, O De Henau, V Robert, M Vernimmen, F Langa, A Lefort, F Libert, V Wittamer, M Parmentier
    Oncotarget, 2021-09-14;12(19):1903-1919.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Novel CMKLR1 Inhibitors for Application in Demyelinating Disease
    Authors: V Kumar, M LaJevic, M Pandrala, SA Jacobo, SV Malhotra, BA Zabel
    Sci Rep, 2019-05-09;9(1):7178.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Chemerin/ChemR23 axis promotes inflammation of glomerular endothelial cells in diabetic nephropathy
    Authors: J Shang, L Wang, Y Zhang, S Zhang, L Ning, J Zhao, G Cheng, D Liu, J Xiao, Z Zhao
    J. Cell. Mol. Med., 2019-02-19;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Surface-enhanced Raman scattering for the detection of polycystic ovary syndrome
    Authors: A Momenpour, PDA Lima, YA Chen, CR Tzeng, BK Tsang, H Anis
    Biomed Opt Express, 2018-01-25;9(2):801-817.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  7. CMKLR1 activation ex vivo does not increase proportionally to serum total chemerin in obese humans
    Authors: Kerry B Goralski
    Endocr Connect, 2016-11-08;5(6):70-81.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  8. The role of chemerin and ChemR23 in stimulating the invasion of squamous oesophageal cancer cells
    Authors: JD Kumar, S Kandola, L Tiszlavicz, Z Reisz, GJ Dockray, A Varro
    Br. J. Cancer, 2016-04-19;114(10):1152-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Increased expression of chemerin in squamous esophageal cancer myofibroblasts and role in recruitment of mesenchymal stromal cells.
    Authors: 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
    PLoS ONE, 2014-08-15;9(7):e104877.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Chemerin C9 peptide induces receptor internalization through a clathrin-independent pathway.
    Authors: Zhou J, Liao D, Zhang S, Cheng N, He H, Ye R
    Acta Pharmacol Sin, 2014-03-24;35(5):653-63.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Development of a membrane-anchored chemerin receptor agonist as a novel modulator of allergic airway inflammation and neuropathic pain.
    Authors: Doyle J, Krishnaji S, Zhu G, Xu Z, Heller D, Ji R, Levy B, Kumar K, Kopin A
    J Biol Chem, 2014-03-21;289(19):13385-96.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  12. A multiplex immunoassay for human adipokine profiling.
    Authors: Schipper HS, De Jager W, van Dijk ME, Meerding J, Zelissen PM, Adan RA, Prakken BJ, Kalkhoven E
    Clin. Chem., 2010-06-08;56(0):1320.
    Applications: ELISA (Standard)
  13. Regulation of chemerin bioactivity by plasma carboxypeptidase N, carboxypeptidase B (activated thrombin-activable fibrinolysis inhibitor), and platelets.
    Authors: Du XY, Zabel BA, Myles T, Allen SJ, Handel TM, Lee PP, Butcher EC, Leung LL
    J. Biol. Chem., 2008-11-14;284(2):751-8.
    Applications: ELISA (Standard), Western Blot

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