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The protein encoded by PTPRM is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping Protein Tyrosine Phosphatase, Receptor Type, M Antibodies (64) and many more products for this protein.
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Study determined that, in addition to the furin (show FURIN Proteins)-processed form of PTPmicro, a pool of 200 kDa full-length PTPmicro exists at the plasma membrane that is cleaved directly by ADAM to generate a larger shed form of the PTPmicro extracellular segment.
Decreased expression of PTPRM in breast cancer is correlated with poor prognosis and inversely correlated with disease-free survival.
Results suggest that miR (show MLXIP Proteins)-221 and -222 regulate glioma tumorigenesis at least in part through the control of PTPmu protein expression.
Loss of protein tyrosine phosphatase (show ACP1 Proteins) receptor type mu is associated with glioma cell migration and progression.
interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs (show PTPRS Proteins)
RPTPmu may play a role in the regulation of cardiovascular functions
PTPmu may regulate Rho-GTPase (show RACGAP1 Proteins)-dependent functions of IQGAP1 (show IQGAP1 Proteins)
a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions is described
BCCIP (show BCCIP Proteins) is phosphorylated by the Src (show SRC Proteins) tyrosine kinase (show TXK Proteins) and dephosphorylated by the PTPmu tyrosine phosphatase; neurite outgrowth assays suggest that BCCIP (show BCCIP Proteins) and PTPmu are in a common signal transduction pathway.
histochemical analysis showed that within bone, RPTPmu is expressed exclusively in early-stage osteocytes and therefore is a new marker for osteocytes
differentiation into adipocytes is controlled by RPTPmu
RPTPmu is involved in the mechanotransduction or accessory signaling pathways that control shear stress responses in mesenteric resistance arteries.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP has been shown to mediate cell-cell aggregation through the interaction with another molecule of this PTP on an adjacent cell. This PTP can interact with scaffolding protein RACK1/GNB2L1, which may be necessary for the downstream signaling in response to cell-cell adhesion. Alternative splicing results in multiple transcripts encoding distinct isoforms.
receptor-type tyrosine-protein phosphatase mu
, protein tyrosine phosphatase, receptor type, M
, receptor-type tyrosine-protein phosphatase mu-like
, protein tyrosine phosphatase mu
, protein tyrosine phosphatase, receptor type, mu polypeptide
, protein-tyrosine phosphatase mu
, protein tyrosine phosphatase, receptor-type, M
, protein tyrosine phosphatase receptor-type M