Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
The protein encoded by PTPRB is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPRB Antibodies (22) and PTPRB Proteins (17) and many more products for this protein.
Showing 10 out of 17 products:
PTPRB was down-regulated in non-small-cell lung cancer patients and was associated with patient overall survival.
STIM1 (show STIM1 ELISA Kits)-induced Ca(2 (show CA2 ELISA Kits)+) signaling activates Pyk2 (show PTK2B ELISA Kits) to inhibit the interaction of VE-PTP and VE-cadherin (show CDH5 ELISA Kits) and hence increase endothelial permeability.
Results provide evidence that PTPRB and PLCG1 (show PLCG1 ELISA Kits) mutations are driving events in a subset of secondary angiosarcomas.
VE-PTP activates TIE2 (show TEK ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) has been observed over expressed in human breast cancer patients, suggesting its role in cell proliferation.
In the absence of Tie-2 (show TEK ELISA Kits), VE-PTP inhibition destabilizes endothelial barrier integrity in agreement with the VE-cadherin (show CDH5 ELISA Kits)-supportive effect of VE-PTP.
The Lewis X (show FUT4 ELISA Kits) epitope is mainly expressed on phosphacan (show PTPRZ1 ELISA Kits)/receptor protein tyrosine phosphatase (show PTPRT ELISA Kits) beta (RPTPbeta) in the developing mouse brain.
We suggest that lymphocyte binding to vascular cell adhesion molecule 1 (show VCAM1 ELISA Kits) triggers a signaling process that enables a VE-PTP substrate to dissociate VE-PTP from VE-cadherin (show CDH5 ELISA Kits), thereby facilitating efficient transmigration.
We conclude that the role of Tie2 (show TEK ELISA Kits) 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 ELISA Kits) tyrosine phosphorylation, endothelial cell polarity
IGFBP-2 (show IGFBP2 ELISA Kits) bound receptor protein tyrosine phosphatase (show PTPRT ELISA Kits) beta, which led to its dimerization and inactivation. Analysis of aortas obtained from IGFBP-2 (show IGFBP2 ELISA Kits)(-/-) mice showed that receptor protein tyrosine phosphatase (show PTPRT ELISA Kits) beta was activated.
Data show that vascular endothelial protein tyrosine phosphatase (VE-PTP) is a transmembrane binding partner of VE-cadherin (show CDH5 ELISA Kits) that reduces the tyrosine phosphorylation of VE-cadherin (show CDH5 ELISA Kits) and cell layer permeability.
the activity of VE-PTP is not required for the initial formation of blood vessels, yet it is essential for their maintenance and remodeling.
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