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The protein encoded by PTPN3 is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPN3 Proteins (6) and many more products for this protein.
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High expression of PTPN3 was significantly associated with unfavorable prognosis of GBM. Moreover, in GBM cell lines, PTPN3 promoted cell proliferation and invasion, and the PTP common inhibitor pervanadate suppressed GBM proliferation and invasion.
PTPN3 promotes tumorigenicity, stemness and drug resistance in ovarian cancer.
Results indicate that protein tyrosine phosphatase non-receptor type 3 (PTPN3) may act as a tumor suppressor in lung cancer through its modulation of epidermal growth factor receptor (EGFR) signaling.
analysis of how allosteric regulation of p38gamma and PTPN3 involves a PDZ domain-modulated complex formation
These studies thus identified PTPH1 as a novel ER phosphatase and further demonstrate a therapeutic potential of enhancing breast cancer sensitivity to antiestrogens through dephosphorylating ER by PTPH1.
Activating mutations in and high expression levels of PTPN3 were associated with tumor recurrence in cholangiocarcinoma.
p38gamma Mitogen-activated protein kinase signals through phosphorylating its phosphatase PTPH1 in regulating ras protein oncogenesis and stress response.
The fusion transcript of ALK and PTPN3 identified resulted from translocation of a part of ALK gene into the third intron of PTPN3. Analysis of the transcript sequence indicates that no protein with any enzymatic activity is produced.
PTPH1 stimulated breast cancer growth through regulating vitamin D receptor expression. PTPH1 was overexpressed in primary breast cancer and levels of its protein expression positively correlated with clinical metastasis.
PTPH1 plays a role in Ras-dependent malignant growth by a mechanism depending on its p38gamma-binding activity. Ras increases p38gamma and PTPH1 expression and there is a coupling of increased p38gamma and PTPH1 protein expression in colon cancer.
regulates TACE (tnf-alpha convertase}
first reported demonstration that protein tyrosine phosphatase H1(PTPH1) is capable of interacting with and dephosphorylating T cell receptor zeta subunit
PTPH1 binds to the PDZ-domain binding motif of the cardiac voltage-gated sodium channel Na(v)1 and regulates the activity of Na(v)1.
Degradation of PTPN3 by HPV-16 E6 requires E6AP, the proteasome, and an interaction between the carboxy terminus of E6 and the PDZ domain of PTPN3.
phosphatase activity and FERM domain of PTPN3 are essential for its suppression of HBV gene expression.
PTP-H1 has a role in modulating GHR signaling and systemic growth through insulin-like growth factor 1 secretion
Data suggest that reducing the level of PTPH1 may contribute to the oncogenic activity of high-risk genital E6 proteins.
PTPN3 and PTPN4 are dispensable for TCR signal transduction.
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 protein contains a C-terminal PTP domain and an N-terminal domain homologous to the band 4.1 superfamily of cytoskeletal-associated proteins. P97, a cell cycle regulator involved in a variety of membrane related functions, has been shown to be a substrate of this PTP. This PTP was also found to interact with, and be regulated by adaptor protein 14-3-3 beta. Several alternatively spliced transcript variants encoding different isoforms have been found for this gene.
cytoskeletal-associated protein tyrosine phosphatase
, protein-tyrosine phosphatase H1
, tyrosine-protein phosphatase non-receptor type 3