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The protein encoded by PTPN12 is a member of the protein tyrosine phosphatase (PTP) family. Zusätzlich bieten wir Ihnen PTPN12 Antikörper (57) und viele weitere Produktgruppen zu diesem Protein an.
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PTPN12 plasmid transfection increased PTPN12 mRNA and protein expressions, suppressed cell proliferation and migration, reduced EGFR (zeige EGFR Proteine) level, and enhanced caspase 3 (zeige CASP3 Proteine) activity compared with control and empty plasmid groups.
PTPN12, PTPRN and PTPN18 were independent prognostic factors in Hepatocellular Carcinoma.
Here, solved is a crystal structure of the native PTPN12 catalytic domain with the catalytic cysteine (residue 231) in dual conformation (phosphorylated and unphosphorylated).
this study, with a relative large population, showed that PTPN12 eQTL (zeige EQTN Proteine) SNP may interact with HBV mutation on HCC (zeige FAM126A Proteine) risk.
MyoVa (zeige MYO5A Proteine)-Ca(2 (zeige CA2 Proteine)+) channel interactions are required for proper long-range axon growth in developing spinal cord in vivo.
PTP-PEST regulates EphA3 (zeige EPHA3 Proteine) activation both by affecting cytoskeletal remodelling and through its direct action as a PTP (zeige SLC25A3 Proteine) controlling EphA3 (zeige EPHA3 Proteine) 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 (zeige MOK Proteine)
The decrease expression of PTPN12 might be important in conferring a more aggressive behavior in NPC (zeige NPC1 Proteine). Thus, PTPN12 expression may be used as a novel independent prognostic biomarker for patients with NPC (zeige NPC1 Proteine).
PTPN12 is potentially a methylation-silenced TSG (zeige TWSG1 Proteine) 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.
PTPN12-deficient, ErbB2 (zeige ERBB2 Proteine)-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 (zeige CDC42 Proteine) signaling by controlling the subcellular localization and phosphorylation status of Rho GDP dissociation inhibitor 1 (zeige ARHGDIA Proteine).
Pyk2 (zeige PTK2B Proteine) deregulation played a pivotal role in the migration defect caused by PTPN12 deficiency.
Regulation of the Src kinase-associated phosphoprotein (zeige SKAP2 Proteine) 55 homologue by the protein tyrosine phosphatase (zeige ACP1 Proteine) PTP-PEST in the control of cell motility.
macrophage fusion is critically dependent on PTP-PEST.
Overexpression of PTP-PEST substantially inhibits lipopolysaccharide (LPS (zeige TLR4 Proteine))-induced tyrosine phosphorylation of IkappaB kinase (zeige CHUK Proteine) (IKKbeta (zeige IKBKB Proteine)) at Tyr188/199 in RAW264.7 cells.
PTP-PEST is a key regulator of integrin-mediated functions in endothelial cells.
the dephosphorylation of Pyk2 (zeige PTK2B Proteine) requires dynamin's GTPase (zeige RACGAP1 Proteine) activity and is mediated by the tyrosine phosphatase PTP-PEST.
PTP-PEST controls Pyk2 (zeige PTK2B Proteine) activity and is a positive regulator of secondary T cell activation.
the paxillin (zeige PXN Proteine)-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