Name :
VSIG4 Protein
Description :
VSIG4 (V-set and immunoglobulin domain containing 4), also known as complement receptor of the immunoglobulin superfamily (CRIg) and Z39Ig, is a type I transmembrane glycoprotein. It is a B7 family-related protein and an Ig superfamily member. In contrast to the B7 family members which contain two IgG domains, VSIG4 contains one complete V-type I g domain and a truncated C-type I g domain. VSIG4 is exclusively expressed on tissue resident macrophages and binds to multimers of C3b and iC3b that are covalently attached to particle surfaces. No VSIG4 expression appears to be present in T and B cells. VSIG4 functions as a negative regulator of T cell activation, and may be involved in the maintenance of peripheral T cell tolerance, and is also identified as a potent suppressor of established inflammation. Mouse VSIG4 is synthesized as a 28 amino acid precursor that contains a signal sequence, a V-type I g domain (aa 36-115), one potential N-linked glycosylation site, and a single transmembrane domain. The V-type I g domain of mouse VSIG4 shares 86% and 8% aa sequence identity with the V-type I g domains of rat and human VSIG4, respectively.
Species :
Human
Uniprotkb :
HEK293
Tag :
His
Synonyms :
Z39IG, CRIg, V-set and immunoglobulin domain containing 4
Construction :
A DNA sequence encoding the human VSIG4 (Q9Y279-1) extracellular domain (Met 1-Pro 283) was expressed, fused with a polyhistidine tag at the C-terminus.
Protein Purity :
≥ 96 % as determined by SDS-PAGE ≥ 95 % as determined by SEC-HPLC.
Molecular Weight :
Approxiamtely 30.5 kDa
Endotoxin :
Formulatione :
Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background :
VSIG4 (V-set and immunoglobulin domain containing 4), also known as complement receptor of the immunoglobulin superfamily (CRIg) and Z39Ig, is a type I transmembrane glycoprotein. It is a B7 family-related protein and an Ig superfamily member. In contrast to the B7 family members which contain two IgG domains, VSIG4 contains one complete V-type I g domain and a truncated C-type I g domain. VSIG4 is exclusively expressed on tissue resident macrophages and binds to multimers of C3b and iC3b that are covalently attached to particle surfaces. No VSIG4 expression appears to be present in T and B cells. VSIG4 functions as a negative regulator of T cell activation, and may be involved in the maintenance of peripheral T cell tolerance, and is also identified as a potent suppressor of established inflammation. Mouse VSIG4 is synthesized as a 28 amino acid precursor that contains a signal sequence, a V-type I g domain (aa 36-115), one potential N-linked glycosylation site, and a single transmembrane domain. The V-type I g domain of mouse VSIG4 shares 86% and 8% aa sequence identity with the V-type I g domains of rat and human VSIG4, respectively.
References and Literature :
1. Vogt, L. et al., 2006, J Clin Invest.116: 2817-2826. 2. Helmy, K. et al., 2006, Cell. 124:915-927. 3. Wiesmann, C. et al., 2006, Nature. 444:217-220. 4. Zang,X. et al., 2006, J Clin Invest. 116: 2590-2593. 5. Katschke, KJ. et al., 2007, J. Exp. Med. 204:1319-1325. 6. He,JQ. et al., 2008, Mol Immunol. 45: 4041-4047.
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