Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P08575 |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | PTPRC (also known as CD45), T cells require the protein tyrosine phosphatase CD45 to detect and respond to antigen because it activates the Src family kinase Lck, which phosphorylates the T cell antigen receptor (TCR) complex. CD45 ativates Lck by opposing the negative regulatory kinase Csk. Paradoxically, CD45 has also been implicated in suppressing TCR signaling by dephosphorylating the same signaling motifs within the TCR complex upon which Lck acts. |
molecular weight | The protein has a predicted MW of 47.3 kDa. Due to glycosylation, the protein migrates to 80-110 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human CD45/PTPRC Protein 3165
$315.00 – $1,050.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Gln26-Ile416
Human CD45/PTPRC Protein 3165
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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PTPRC (also known as CD45),T cells require the protein tyrosine phosphatase CD45 to detect and respond to antigen because it activates the Src family kinase Lck, which phosphorylates the T cell antigen receptor (TCR) complex. CD45 ativates Lck by opposing the negative regulatory kinase Csk. Paradoxically, CD45 has also been implicated in suppressing TCR signaling by dephosphorylating the same signaling motifs within the TCR complex upon which Lck acts. |
Protein names Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (T200) (CD antigen CD45) |
Gene names PTPRC,PTPRC CD45 |
Protein family Protein-tyrosine phosphatase family, Receptor class 1/6 subfamily |
Mass 9606Da |
Function Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor (PubMed:35767951). 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 (By similarity).; (Microbial infection) Acts as a receptor for human cytomegalovirus protein UL11 and mediates binding of UL11 to T-cells, leading to reduced induction of tyrosine phosphorylation of multiple signaling proteins upon T-cell receptor stimulation and impaired T-cell proliferation. |
Catalytic activity #N/A |
Subellular location Cell membrane ; Single-pass type I membrane protein. Membrane raft. Synapse. Note=Colocalized with DPP4 in membrane rafts. |
Tissues Isoform 1: Detected in thymocytes. Isoform 2: Detected in thymocytes. Isoform 3: Detected in thymocytes. Isoform 4: Not detected in thymocytes. Isoform 5: Detected in thymocytes. Isoform 6: Not detected in thymocytes. Isoform 7: Detected in thymocytes. Isoform 8: Not detected in thymocytes. |
Structure Binds GANAB and PRKCSH (By similarity). Interacts with SKAP1 (PubMed:11909961). Interacts with DPP4; the interaction is enhanced in an interleukin-12-dependent manner in activated lymphocytes (PubMed:12676959). Interacts with CD53; this interaction stabilizes PTPRC on the membrane and is required for optimal phosphatase activity (PubMed:35767951).; (Microbial infection) Interacts with human cytomegalovirus protein UL11; the interaction is required for binding of UL11 to T-cells. |
Post-translational modification Heavily N- and O-glycosylated. |
Domain Th |
Target Relevance information above includes information from UniProt accession: P08575 |
The UniProt Consortium |
Data
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