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SRP6002

Sigma-Aldrich

Chemerin human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC)

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Synonym(s):
HP10433, RARRES2, TIG2
CAS Number:

biological source

human

recombinant

expressed in E. coli

assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

mol wt

16.0 kDa

packaging

pkg of 25 μg

impurities

Endotoxin, tested

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... RARRES2(5919)

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Sigma-Aldrich

SRP6002

Chemerin human

Endostatin human recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

SRP3031

Endostatin human

Sigma-Aldrich

SRP3045

Follistatin human

Sigma-Aldrich

SRP4896

TSLP human

biological source

human

biological source

human

biological source

human

biological source

human

assay

≥98% (HPLC), ≥98% (SDS-PAGE)

assay

≥98% (HPLC), ≥98% (SDS-PAGE)

assay

≥98% (HPLC), ≥98% (SDS-PAGE)

assay

≥97% (HPLC), ≥97% (SDS-PAGE)

form

lyophilized

form

lyophilized

form

lyophilized

form

lyophilized

mol wt

16.0 kDa

mol wt

20.2 kDa

mol wt

31.5 kDa

mol wt

~15.0 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

Chemerin, which is also known as retinoic acid receptor responder 2 (RARRES2), is a chemoattractant expressed in white adipose, liver and lung tissues. It is an immunomodulating factor. The protein is a ligand for the G-protein coupled receptor known as ChemR23 (or chemokine-like receptor-1), which is expressed mainly on dendritic cells, macrophages and some adipocytes. The gene encoding it is localized on human chromosome 7q36.1. Recombinant human Chemerin, produced in Escherichia.coli, is a non-glycosylated protein containing 138 amino acids and having a total molecular mass of 16kDa.

Biochem/physiol Actions

Chemerin activates chemerin-like receptor 1 (CMKLR1) and stimulates chemotaxis in macrophages, natural killer cells and immature dendritic cells. It is also involved in the activation of extracellular signal-regulated kinases, stimulation of blood vessel formation, migration and invasion.

Physical form

Lyophilized from 0.2% TFA.

Reconstitution

Centrifuge the vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with sterile H?O to a concentration of 0.1mg/ml, which can be further diluted into other aqueous solutions.

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Association of Polymorphisms in STRA6 and RARRES2 Genes with Type 2 Diabetes in Southern Han Chinese.
Huang HW
BioMed Research International, 2016, 6589793-6589793 (2016)
Rui-Li Zhang et al.
Journal of cellular biochemistry, 120(12), 19621-19634 (2019-07-20)
Chemerin, a chemoattractant protein, is involved in endothelial dysfunction and vascular inflammation in pathological conditions. In a recent study, we observed the upregulation of chemerin in endothelial cells following in vitro treatment with Treponema pallidum. Here, we investigated the role
Urszula Godlewska et al.
Frontiers in microbiology, 11, 1819-1819 (2020-08-28)
Chronic inflammatory skin diseases like psoriasis alter the local skin microbiome and lead to complications such as persistent infection with opportunistic/pathogenic bacteria. Disease-associated changes in microbiota may be due to downregulation of epidermal antimicrobial proteins/peptides, such as antimicrobial protein chemerin.
Kamila Kwiecien et al.
Scientific reports, 10(1), 13702-13702 (2020-08-15)
Chemerin is a chemoattractant protein with adipokine properties encoded by the retinoic acid receptor responder 2 (RARRES2) gene. It has gained more attention in the past few years due to its multilevel impact on metabolism and immune responses. However, mechanisms
Jeremy Di Domizio et al.
Nature immunology, 21(9), 1034-1045 (2020-07-15)
Skin wounds heal by coordinated induction of inflammation and tissue repair, but the initiating events are poorly defined. Here we uncover a fundamental role of commensal skin microbiota in this process and show that it is mediated by the recruitment

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