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Description
Protein tyrosine phosphatases participate in the intracellular signaling pathways of mitosis, differentiation, migration, survival, transformation, and death. SHP-2, a SH-2 domain containing phosphotyrosine phosphatase, is a positive signal transducer of receptor tyrosine kinases (RTKs) and cytokine receptors. SIRPs (Signal-Regulatory Proteins) were identified as a result of their association with SHP-2. The 15+ members of this family consist of two subtypes based on the presence or absence of a cytoplasmic SHP-2-binding domain. SIRPα1 is a transmembrane polypeptide substrate of activated RTKs. When tyrosine-phosphorylated, SIRPα1 binds SHP-2, SHP-1, Grb2 through an SH2 interaction. The SIRP proteins also constitute a subfamily within the Ig superfamily because they contain transmembrane glycoproteins with three Ig-like extracellular domains. Additionally, SIRPs' cytoplasmic tails contain two ITI (immunoreceptor tyrosine-based inhibition motifs). Although SIRPs have been shown to inhibit signaling through RTKs, their function is yet to be determined.
Immunofluorescence, Western Blotting
Specifications
Specifications
| Antigen | SIRPα1 |
| Applications | Immunofluorescence, Western Blot |
| Classification | Monoclonal |
| Clone | 27 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Host Species | Mouse |
| Immunogen | Human SIRPα1 aa. 395-503 |
| Purification Method | Affinity Purified |
| Quantity | 50 μg |
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