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The protein encoded by PTPN12 is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPN12 Proteins (9) and many more products for this protein.
Showing 10 out of 47 products:
Human Polyclonal PTPN12 Primary Antibody for ICC, IF - ABIN4348590
Harris, Blaser, Moreno, Treloar, Gorrini, Sasaki, Mason, Knobbe, Rufini, Hallé, Elia, Wakeham, Tremblay, Melino, Done, Mak: PTPN12 promotes resistance to oxidative stress and supports tumorigenesis by regulating FOXO signaling. in Oncogene 2014
Show all 2 Pubmed References
MyoVa (show MYO5A Antibodies)-Ca(2 (show CA2 Antibodies)+) channel interactions are required for proper long-range axon growth in developing spinal cord in vivo.
PTP-PEST regulates EphA3 (show EPHA3 Antibodies) activation both by affecting cytoskeletal remodelling and through its direct action as a PTP (show SLC25A3 Antibodies) controlling EphA3 (show EPHA3 Antibodies) phosphorylation.
Study suggests that PTPN12 expression is a valuable prognostic biomarker for non-small cell lung cancer.
PTPN12 expression decreases in human renal cell carcinoma (show MOK Antibodies)
The decrease expression of PTPN12 might be important in conferring a more aggressive behavior in NPC (show NPC1 Antibodies). Thus, PTPN12 expression may be used as a novel independent prognostic biomarker for patients with NPC (show NPC1 Antibodies).
PTPN12 is potentially a methylation-silenced TSG (show TWSG1 Antibodies) for breast cancer that may play an important role in breast carcinogenesis and could potentially serve as an independent prognostic factor for invasive breast cancer patients.
Decreased expression of PTPN12 correlates with tumor recurrence and poor survival of patients with hepatocellular carcinoma.
these data suggest that PTP-PEST affects epithelial cell motility by controlling the distribution and phosphorylation of p120 (show HNRNPU Antibodies) and its availability to control Rho GTPase (show RACGAP1 Antibodies) activity.
The involvement of PTPN12 in the antioxidant response of breast cancer cells suggests that PTPN12 may represent a novel therapeutic target for this disease
Overexpression of PTPN12 inhibited proliferation and migration in OSCC cells.
PTPN12-deficient, ErbB2 (show ERBB2 Antibodies)-dependent breast cancer cells were more resistant to anoikis and had augmented migratory and invasive properties.
Integrin beta 8 and PTP-PEST form protein complexes at the leading edge of migrating cells and balance patterns of Rac1 and Cdc42 (show CDC42 Antibodies) signaling by controlling the subcellular localization and phosphorylation status of Rho GDP dissociation inhibitor 1 (show ARHGDIA Antibodies).
Pyk2 (show PTK2B Antibodies) deregulation played a pivotal role in the migration defect caused by PTPN12 deficiency.
Regulation of the Src kinase-associated phosphoprotein (show SKAP2 Antibodies) 55 homologue by the protein tyrosine phosphatase (show ACP1 Antibodies) PTP-PEST in the control of cell motility.
macrophage fusion is critically dependent on PTP-PEST.
Overexpression of PTP-PEST substantially inhibits lipopolysaccharide (LPS (show TLR4 Antibodies))-induced tyrosine phosphorylation of IkappaB kinase (show CHUK Antibodies) (IKKbeta (show IKBKB Antibodies)) at Tyr188/199 in RAW264.7 cells.
PTP-PEST is a key regulator of integrin-mediated functions in endothelial cells.
the dephosphorylation of Pyk2 (show PTK2B Antibodies) requires dynamin's GTPase (show RACGAP1 Antibodies) activity and is mediated by the tyrosine phosphatase PTP-PEST.
PTP-PEST controls Pyk2 (show PTK2B Antibodies) activity and is a positive regulator of secondary T cell activation.
the paxillin (show PXN Antibodies)-PTP-PEST interaction contributes to integrin signaling
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains a C-terminal PEST motif, which serves as a protein-protein interaction domain, and may regulate protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of the oncogene c-ABL and thus may play a role in oncogenesis. This PTP was also shown to interact with, and dephosphorylate, various products related to cytoskeletal structure and cell adhesion, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin. This suggests it has a regulatory role in controlling cell shape and mobility. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
protein-tyrosine phosphatase G1
, tyrosine-protein phosphatase non-receptor type 12
, protein-tyrosine phosphatase P19