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Home >Products> Reagents >Other Reagents> CD45RA His Tag Protein, Human
CD45RA His Tag Protein, Human
CD45RA His Tag Protein, Human
Origin of place Singapore
Model UA010812-100μg
Supplier ANT BIO PTE.LTD.
Price 604
Hits 0
Updated 8/25/2025
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Product Specification


SpeciesHuman
SynonymsB220, CD45, CD45R, GP180, IMD105, L-CA, LCA, LY5, T200,PTPRC
AccessionP08575-8
Amino Acid Sequence

Gln26-Lys482, with C-terminal His

Expression SystemHEK293
Molecular Weight

90-130kDa (Reducing)

Purity>95% by SDS-PAGE
Endotoxin<0.1EU/μg
ConjugationUnconjugated
TagHis Tag
Physical AppearanceLyophilized Powder
Storage Buffer

PBS, pH7.4.

Reconstitution

Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.

Stability & Storage

· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃.

· 3 months, -20 to -80℃ under sterile conditions after reconstitution.

· 1 week, 2 to 8℃ under sterile conditions after reconstitution.

· Please avoid repeated freeze-thaw cycles.

Reference

1.Anderson, J.N. et al. (2004) FASEB J. 18:8. 2.Streuli, M. et al. (1987) J. Exp. Med. 166:1548. 3.Hermiston, M.L. et al. (2003) Annu. Rev. Immunol. 21:107.

Background

Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. It is a variably glycosylated 180-220 kDa transmembrane protein that is abundantly expressed on all nucleated cells of hematopoietic origin.Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity.

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