| Message: | Protein tyrosine phosphorylation plays an essential role in the regulation of many cellular processes, including cellular proliferation, differentiation, migration and tumorigenic transformation. The phosphorylation of proteins on tyrosine is catalyzed by numerous protein tyrosine kinases, and is rapidly and reversibly dephosphorylated by Protein tyrosine phosphatases (PTPases).The low molecular weight protein tyrosine phosphatase (LMW-PTP) is an 18-kDa cytosolic enzyme, also known as acidic protein phosphatase 1 (ACP1).LMW-PTP/ACP1 is specific for phosphotyrosine in peptides and proteins, but the enzyme shares very limited sequence homology with other PTPases. Although LMW-PTP/ACP1 has been showed as negative regulator of insulin- and platelet-derived growth factor (PDGF)-mediated mitotic and metabolic signaling, LMW-PTP/ACP1 is frequently overexpressed in transformed cell. Recent studies suggested that entopic overexpression of LMW-PTP/ACP1 is sufficient to confer transformation in epithelial cells and its oncogenic activities required EphA2. LMW-PTP/ACP1 negatively regulates EphA2 receptor tyrosine kinase. LMW-PTP/ACP1 is a positive regulator of both tumor onset and development through ephrin-EphA2 signaling process, and it is a potential target of anticancer drug development.
https://www.creativebiomart.net/protein-phosphatase-lmw-ptpacp1-fluorometric-human-assay-kit-463634.htm |
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