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The protein encoded by PTPN9 is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPN9 Antibodies (28) and many more products for this protein.
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PTPN9 inhibited cell proliferation in HepG2 cells.
PTPMeg2 is an important phosphatase for the dephosphorylation of STAT3 (show STAT3 Proteins) and plays a critical role in breast cancer development.
This study indentified VEGFR2 (show KDR Proteins) as a PTPN9 substrate, and indicated that PTPN9 is a negative regulator of VEGFR2 (show KDR Proteins) signaling and function in endothelial cells.
data suggest PTPN9 as a negative regulator of breast cancer cells by targeting ErbB2 (show ERBB2 Proteins) and EGFR (show EGFR Proteins) and inhibiting STAT (show STAT1 Proteins) activation
Purification and characterization of protein tyrosine phosphatase (show ACP1 Proteins) PTP (show SLC25A3 Proteins)-MEG2
PTP (show SLC25A3 Proteins)-MEG2 has an important role in the development of erythroid cells.
PTPase-MEG2 through its Sec14p homology domain couples inositide phosphorylation to tyrosine dephosphorylation and the regulation of intracellular traffic of the secretory pathway in T cells.
PTP (show SLC25A3 Proteins)-MEG2 reduced the phosphotyrosine content of NSF (show NSF Proteins) and co-localized with NSF (show NSF Proteins) and syntaxin 6 (show STX6 Proteins) in intact cells, the first demonstrated role for a protein tyrosine phosphatase (show ACP1 Proteins) in the regulated secretory pathway
role in the negative regulation of hepatic insulin (show INS Proteins) signaling
the N terminus of PTPMEG2 is necessary for the targeting of this phosphatase to the secretory vesicle compartment by association with other proteins involved in intracellular transport.
As a result, overexpression of PTP (show SLC25A3 Proteins)-MEG2 down-regulates NGF (show NGFB Proteins)/TrkA (show NTRK1 Proteins) signaling and blocks neurite outgrowth and differentiation
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 N-terminal domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the Golgi complex in yeast. This PTP was found to be activated by polyphosphoinositide, and is thought to be involved in signaling events regulating phagocytosis.
protein tyrosine phosphatase, non-receptor type 9
, PTPase MEG2
, protein-tyrosine phosphatase MEG2
, tyrosine-protein phosphatase non-receptor type 9
, Protein-tyrosine phosphatase, non-receptor type 9 (Protein-tyrosine phosphatase MEG2) (PTPase-MEG2)