CD45

CD45

UM16-6

Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant

Use 10ul of the suggested working dilution to label 106 cells in 100ul. Suggested

Required for T-cell activation through the antigen receptor. 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 an dephosphorylates SKAP1 and FYN.

Binds GANAB and PRKCSH (By similarity). Interacts with SKAP1.

The first PTPase domain interacts with SKAP1.

Defects in PTPRC are a cause of severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+)SCID) [MIM:608971]. SCID refers to a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity leukopenia and low or absent antibody levels. Patients with SCID present in infancy with recurrent persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development.

Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily.

Contains 2 tyrosine-protein phosphatase domains. 1. Symons. A. et al. (1999) Domain organization of the extracellular region of CD45. 2. Okumura. M. et al. (1996) Comparison of CD45 extracellular domain sequences from divergent vertebrate species suggests the conservation of three fibronectin type III domains. 3. Jung. E. J. et al. (1997) Phosphorylation of chicken protein tyrosine phosphatase 1 by casein kinase II in vitro. Experimental and Molecular Medicine 29(4): 229-233.