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The protein encoded by PTPRB is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPRB Kits (22) and PTPRB Proteins (11) and many more products for this protein.
Showing 10 out of 26 products:
Cow (Bovine) Polyclonal PTPRB Primary Antibody for ELISA - ABIN4348614
Winderlich, Keller, Cagna, Broermann, Kamenyeva, Kiefer, Deutsch, Nottebaum, Vestweber: VE-PTP controls blood vessel development by balancing Tie-2 activity. in The Journal of cell biology 2009
PTPRB was down-regulated in non-small-cell lung cancer patients and was associated with patient overall survival.
STIM1 (show STIM1 Antibodies)-induced Ca(2 (show CA2 Antibodies)+) signaling activates Pyk2 (show PTK2B Antibodies) to inhibit the interaction of VE-PTP and VE-cadherin (show CDH5 Antibodies) and hence increase endothelial permeability.
Results provide evidence that PTPRB and PLCG1 (show PLCG1 Antibodies) mutations are driving events in a subset of secondary angiosarcomas.
VE-PTP activates TIE2 (show TEK Antibodies) 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 Antibodies) 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 Antibodies) 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 Antibodies) response to ANGPT2 (show ANGPT2 Antibodies). VEPTP is absent from lymphatic endothelium in mouse in vivo, permitting ANGPT2 (show ANGPT2 Antibodies)/TIE2 (show TEK Antibodies)-mediated lymphangiogenesis.
PTPRB regulates branching morphogenesis in the mammary epithelium by modulating the response of the FGFR (show FGFR2 Antibodies) signalling pathway to FGF stimulation
In the absence of Tie-2 (show TEK Antibodies), VE-PTP inhibition destabilizes endothelial barrier integrity in agreement with the VE-cadherin (show CDH5 Antibodies)-supportive effect of VE-PTP.
The Lewis X (show FUT4 Antibodies) epitope is mainly expressed on phosphacan (show PTPRZ1 Antibodies)/receptor protein tyrosine phosphatase (show PTPRT Antibodies) beta (RPTPbeta) in the developing mouse brain.
We suggest that lymphocyte binding to vascular cell adhesion molecule 1 (show VCAM1 Antibodies) triggers a signaling process that enables a VE-PTP substrate to dissociate VE-PTP from VE-cadherin (show CDH5 Antibodies), thereby facilitating efficient transmigration.
We conclude that the role of Tie2 (show TEK Antibodies) 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 Antibodies) tyrosine phosphorylation, endothelial cell polarity
IGFBP-2 (show IGFBP2 Antibodies) bound receptor protein tyrosine phosphatase (show PTPRT Antibodies) beta, which led to its dimerization and inactivation. Analysis of aortas obtained from IGFBP-2 (show IGFBP2 Antibodies)(-/-) mice showed that receptor protein tyrosine phosphatase (show PTPRT Antibodies) 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