Recombinant Mouse Chemerin (aa 17-156) Protein Summary
Product Specifications
Thr17-Ser156
Analysis
Product Datasheets
Carrier Free
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.
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.
2325-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.
|
2325-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.
|
Reconstitution Calculator
Background: Chemerin
Mouse 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 (aa) (2, 3). Chemerin is synthesized as a 162 aa precursor that contains a hydrophobic N-terminal sequence, an intervening 140 aa cystatin-fold containing domain, and a six aa C-terminal prosegment (4 - 6). Within the cystatin-fold domain there are three intrachain disulfide bonds that contribute to the characteristic fold (4, 7). The precursor molecule is described as undergoing proteolytic processing at both termini by unknown proteases. The N-terminal 16 residue hydrophobic segment is described as being either a signal sequence or a transmembrane (TM) segment for a type II TM protein (5, 8). In either case it gives rise to a soluble proform that undergoes further processing at the C-terminus (5). In mouse, the C-terminal six residues are cleaved, giving rise to a monomeric, 16 kDa heparin-binding bioactive molecule (aa 17 - 156) (5 - 7). A shorter form has been described in human (7). The activity seems to be concentrated in the nine aa’s preceding the prosegment (aa 148 - 156). Retention of the prosegment blocks activity (4). The 140 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 (5). 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 mouse Chemerin shares 67%, 84% and 82% aa sequence identity to human, rat and hamster Chemerin, respectively (6). There is apparently cross-species activity for the protein (6).
- Nagpal, S. et al. (1997) J. Invest. Dermatol. 109:91.
- Storici, P. et al. (1996) Eur. J. Biochem. 238:769.
- Zanetti, M. (2004) J. Leukoc. Biol. 75:39.
- Wittamer, V. et al. (2004) J. Biol. Chem. 279:9956.
- Wittamer, V. et al. (2003) J. Exp. Med. 198:977.
- Busmann, A. et al. (2004) J. Chromatog. B 811:217.
- Meder, W. et al. (2003) FEBS Lett. 555:495.
- Yokoyama-Kobayashi, M. et al. (1999) Gene 228:161.
Citations for Recombinant Mouse Chemerin (aa 17-156) 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.
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Citations: Showing 1 - 10
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Expression of CCRL2 Inhibits Tumor Growth by Concentrating Chemerin and Inhibiting Neoangiogenesis
Authors: D Al Delbany, V Robert, I Dubois-Ved, A Del Prete, M Vernimmen, A Radi, A Lefort, F Libert, V Wittamer, S Sozzani, M Parmentier
Cancers, 2021-10-05;13(19):.
Species: Mouse
Sample Types: Whole Cells
Applications: Cell Culture -
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: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Loss of chemerin triggers bone remodeling in vivo and in vitro
Authors: L Han, Y Zhang, S Wan, Q Wei, W Shang, G Huang, P Fang, W Min
Molecular Metabolism, 2021-08-17;0(0):101322.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Discovery of chemerin as the new chemoattractant of human mesenchymal stem cells
Authors: I Kim, H Park, I Hwang, D Moon, H Yun, EJ Lee, HS Kim
Cell & bioscience, 2021-07-01;11(1):120.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Chemerin-induced macrophages pyroptosis in fetal brain tissue leads to cognitive disorder in offspring of diabetic dams
Authors: Z Liang, L Han, D Sun, Y Chen, Q Wu, L Zhang, M Zhou, D Chen
J Neuroinflammation, 2019-11-16;16(1):226.
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo -
Adipokine Chemerin Bridges Metabolic Dyslipidemia and Alveolar Bone Loss in Mice
Authors: Erivan S Ramos-Juni
J. Bone Miner. Res, 2017-03-01;0(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Targeting VEGF-A in myeloid cells enhances natural killer cell responses to chemotherapy and ameliorates cachexia
Nat Commun, 2016-08-19;7(0):12528.
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo -
The role of GPR1 signaling in mice corpus luteum
Authors: Jian V Zhang
J. Endocrinol., 2016-05-05;230(1):55-65.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
A novel CMKLR1 small molecule antagonist suppresses CNS autoimmune inflammatory disease.
Authors: Graham K, Zhang J, Lewen S, Burke T, Dang T, Zoudilova M, Sobel R, Butcher E, Zabel B
PLoS ONE, 2014-12-01;9(12):e112925.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Endothelial cell-derived chemerin promotes dendritic cell transmigration.
Authors: Gonzalvo-Feo S, Del Prete A, Pruenster M, Salvi V, Wang L, Sironi M, Bierschenk S, Sperandio M, Vecchi A, Sozzani S
J Immunol, 2014-01-27;192(5):2366-73.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
The chemoattractant chemerin suppresses melanoma by recruiting natural killer cell antitumor defenses.
J. Exp. Med., 2012-07-02;209(8):1427-35.
Species: Mouse
Sample Types: In Vivo, Whole Cells
Applications: Bioassay, In Vivo -
Chemerin peptides promote phagocytosis in a ChemR23- and Syk-dependent manner.
Authors: Cash JL, Christian AR, Greaves DR
J. Immunol., 2010-04-02;184(9):5315-24.
Species: Mouse
Sample Types: Cell Culture Supernates
Applications: Bioassay -
Mouse ChemR23 is expressed in dendritic cell subsets and macrophages, and mediates an anti-inflammatory activity of chemerin in a lung disease model.
Authors: Luangsay S, Wittamer V, Bondue B, De Henau O, Rouger L, Brait M, Franssen JD, de Nadai P, Huaux F, Parmentier M
J. Immunol., 2009-10-19;183(10):6489-99.
Species: Mouse
Sample Types: In Vivo, Whole Cells
Applications: Bioassay, In Vivo -
Synthetic chemerin-derived peptides suppress inflammation through ChemR23.
Authors: Cash JL, Hart R, Russ A, Dixon JP, Colledge WH, Doran J, Hendrick AG, Carlton MB, Greaves DR
J. Exp. Med., 2008-04-07;205(4):767-75.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay
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