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The protein encoded by PTPN13 is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPN13 Antibodies (54) and PTPN13 Kits (1) and many more products for this protein.
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The single nucleotide polymorphism genotype of PTPN13 exon 39 was determined in DNA extracted from blood samples from 174 sporadic colorectal cancer patients and 176 healthy individuals. The risk of colorectal cancer was 2.087 times greater for patients with the GG genotype than for those with the TT genotype. PTPN13 rs989902 is significantly associated with the risk of colorectal cancer in the Polish population.
suggest that CAFs, irrespective of identity, have low influence on the degree of tumor infiltration by inflammatory- and/or immune-cells. However, CAFFAP may exert immuno-adjuvant roles in NSCLC, and targeting CAFs should be cautiously considered
we found that miR-26a confers epidermal growth factor receptor-targeted tyrosine kinase inhibitors resistance of non-small cell lung cancer cells by targeting and silencing PTPN13
Fap1 inhibition increased Fas sensitivity and decreased beta-catenin activity in human CD34+ CML cells
the crystal structure of the PTP-Bas PDZ1 domain at 1.6 A resolution, is reported.
PTPN13 overexpression significantly inhibited the progression of HCC (show FAM126A Proteins) cells.
Mutation in PTPN13 gene is associated with gastric cancer peritoneal carcinomatosis.
This work studied heat diffusion in the well-known PDZ-2 protein, and confirmed that this protein has two cognate allosteric pathways and that heat flows preferentially through these.
Necl-4 serves as a novel regulator for contact inhibition of cell movement and proliferation cooperatively with the VEGF receptor and PTPN13
A PDZ-mediated interaction of PTPN13 and PTEN is described with possible relevance for tumor suppression.
contributions of Fap1 to tyrosine kinase inhibitors (TKI)resistance, CML blast crisis, and relapse after TKI discontinuation
The data show that the levels of PTPN13 and beta-catenin (show CTNNB1 Proteins) must be strictly regulated by extracellular signaling to regulate hematopoietic stem cells attachment to the bone marrow niche and the balance between proliferation and quiescence.
The study presents a detailed kinetics analysis of the interaction between PTP-BL PDZ2 domain and a peptide mimicking the PDZ binding motif of APC (show APC Proteins).
SDCCAG3 (show SDCCAG3 Proteins) forms a complex with PTPN13. Interaction of SDCCAG3 (show SDCCAG3 Proteins) with PTPN13 is mediated via the FERM domain of PTPN13 and via the N-terminus of SDCCAG3 (show SDCCAG3 Proteins).
Data indicate that Bcr-abl (show ABL1 Proteins) increases PTPN13 promoter activity in an Icsbp (show IRF8 Proteins)-dependent manner.
Since PTPL1 catalytic activity is important for cell transformation, VCP (show vcp Proteins) regulation by PTPL1 might be important for tumorigenesis.
These findings demonstrate a key role for PTP-BL in 3T3-L1 and mouse embryo fibroblasts-derived adipocyte differentiation that is independent of its enzymatic activity.
Structure, dynamics and binding characteristics of the second PDZ domain of PTP-BL
With delayed kinetics, ephrinB ligands recruit the cytoplasmic PDZ domain containing protein (show USH1C Proteins) tyrosine phosphatase PTP-BL and are dephosphorylated.
FAP-1 has a role in binding to, and consequently inhibition of, Fas (show FAS Proteins) export to the cell surface
RSK2 (show RPS6KA3 Proteins) phosphorylates three sites in Cdc25C (show CDC25C Proteins) and also partially activates Cdc25C (show CDC25C Proteins).
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 is a large intracellular protein. It has a catalytic PTP domain at its C-terminus and two major structural domains: a region with five PDZ domains and a FERM domain that binds to plasma membrane and cytoskeletal elements. This PTP was found to interact with, and dephosphorylate, Fas receptor and IkappaBalpha through the PDZ domains. This suggests it has a role in Fas mediated programmed cell death. This PTP was also shown to interact with GTPase-activating protein, and thus may function as a regulator of Rho signaling pathways. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.
fas-associated protein-tyrosine phosphatase 1
, protein-tyrosine phosphatase 1E
, protein-tyrosine phosphatase PTPL1
, tyrosine-protein phosphatase non-receptor type 13
, protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)
, protein tyrosine phosphatase, non-receptor type 13
, tyrosine-protein phosphatase non-receptor type 13-like
, protein tyrosine phosphatase DPZPTP
, protein tyrosine phosphatase PTP-BL
, protein-tyrosine phosphatase RIP
, tyrosine phosphatase
, protein Tyr phosphatase
, M-phase inducer phosphatase 1-B
, cell division cycle 25 homolog C
, cell division cycle 25C S homeolog
, protein-tyrosine phosphatase BAS