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The protein encoded by PTPRB is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPRB Antibodies (24) and PTPRB Kits (22) and many more products for this protein.
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PTPRB was down-regulated in non-small-cell lung cancer patients and was associated with patient overall survival.
STIM1 (show STIM1 Proteins)-induced Ca(2 (show CA2 Proteins)+) signaling activates Pyk2 (show PTK2B Proteins) to inhibit the interaction of VE-PTP and VE-cadherin (show CDH5 Proteins) and hence increase endothelial permeability.
Results provide evidence that PTPRB and PLCG1 (show PLCG1 Proteins) mutations are driving events in a subset of secondary angiosarcomas.
VE-PTP activates TIE2 (show TEK Proteins) and stabilizes retinal and choroidal blood vessels
these results suggest that the polarized redistribution of VE-PTP in response to shear stress plays an important role in the regulation of endothelial cells function by blood flow.
The endothelial phosphatase PTPRB, a negative regulator of vascular growth factor tyrosine kinases, harbored predominantly truncating mutations in 10 of 39 angiosarcoma tumors.
zinc(II) ions regulate receptor protein-tyrosine phosphatase (show PTPRT Proteins) beta activity at picomolar concentrations.
vascular endothelial protein tyrosine phosphatase contributes to endothelial morphogenesis. Silencing of VE-PTP expression was accompanied by increased VEGF receptor-2 tyrosine phosphorylation and activation of downstream signaling pathways.
Suggest that VE-PTP, in cooperation with integrins, regulates the spreading and migration of endothelial cells during angiogenesis.
The PTP1B (show PTPN1 Proteins) has been observed over expressed in human breast cancer patients, suggesting its role in cell proliferation.
VEPTP (vascular endothelial protein tyrosine phosphatase) determines TIE2 (show TEK Proteins) response to ANGPT2 (show ANGPT2 Proteins). VEPTP is absent from lymphatic endothelium in mouse in vivo, permitting ANGPT2 (show ANGPT2 Proteins)/TIE2 (show TEK Proteins)-mediated lymphangiogenesis.
PTPRB regulates branching morphogenesis in the mammary epithelium by modulating the response of the FGFR (show FGFR2 Proteins) signalling pathway to FGF stimulation
In the absence of Tie-2 (show TEK Proteins), VE-PTP inhibition destabilizes endothelial barrier integrity in agreement with the VE-cadherin (show CDH5 Proteins)-supportive effect of VE-PTP.
The Lewis X (show FUT4 Proteins) epitope is mainly expressed on phosphacan (show PTPRZ1 Proteins)/receptor protein tyrosine phosphatase (show PTPRT Proteins) beta (RPTPbeta) in the developing mouse brain.
We suggest that lymphocyte binding to vascular cell adhesion molecule 1 (show VCAM1 Proteins) triggers a signaling process that enables a VE-PTP substrate to dissociate VE-PTP from VE-cadherin (show CDH5 Proteins), thereby facilitating efficient transmigration.
We conclude that the role of Tie2 (show TEK Proteins) in maintenance of vascular quiescence involves VE-PTP-dependent dephosphorylation of VEGF receptor-2, and that VEGF receptor-2 activity regulates VE-cadherin (show CDH5 Proteins) tyrosine phosphorylation, endothelial cell polarity
IGFBP-2 bound receptor protein tyrosine phosphatase (show PTPRT Proteins) beta, which led to its dimerization and inactivation. Analysis of aortas obtained from IGFBP-2(-/-) mice showed that receptor protein tyrosine phosphatase (show PTPRT Proteins) beta was activated.
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 contains an extracellular domain, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to receptor type PTP. The extracellular region of this PTP is composed of multiple fibronectin type_III repeats, which was shown to interact with neuronal receptor and cell adhesion molecules, such as contactin and tenascin C. This protein was also found to interact with sodium channels, and thus may regulate sodium channels by altering tyrosine phosphorylation status. The functions of the interaction partners of this protein implicate the roles of this PTP in cell adhesion, neurite growth, and neuronal differentiation. Alternate transcript variants encoding different isoforms have been found for this gene.
protein tyrosine phosphatase, receptor type, B
, Receptor-type tyrosine-protein phosphatase beta
, receptor-type tyrosine-protein phosphatase beta-like
, receptor-type tyrosine-protein phosphatase beta
, protein tyrosine phosphatase, receptor type, beta polypeptide
, vascular endothelial protein tyrosine phosphatase
, protein-tyrosine phosphatase beta