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The protein encoded by PTPN13 is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPN13 Proteins (3) and PTPN13 Kits (2) and many more products for this protein.
Showing 10 out of 51 products:
Human Polyclonal PTPN13 Primary Antibody for ICC, IF - ABIN4348593
Meinhold-Heerlein, Stenner-Liewen, Liewen, Kitada, Krajewska, Krajewski, Zapata, Monks, Scudiero, Bauknecht, Reed: Expression and potential role of Fas-associated phosphatase-1 in ovarian cancer. in The American journal of pathology 2001
Show all 2 references for ABIN4348593
Human Polyclonal PTPN13 Primary Antibody for IF (p), IHC (p) - ABIN714341
Evrard, Lecce, Michelis, Nomura-Kitabayashi, Pandey, Purushothaman, dEscamard, Li, Hadri, Fujitani, Moreno, Benard, Rimmele, Cohain, Mecham, Randolph, Nabel, Hajjar, Fuster, Boehm, Kovacic: Endothelial to mesenchymal transition is common in atherosclerotic lesions and is associated with plaque instability. in Nature communications 2016
The data show that the levels of PTPN13 and beta-catenin (show CTNNB1 Antibodies) 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 (show INADL Antibodies) binding motif of APC (show APC Antibodies).
SDCCAG3 (show SDCCAG3 Antibodies) forms a complex with PTPN13. Interaction of SDCCAG3 (show SDCCAG3 Antibodies) with PTPN13 is mediated via the FERM domain of PTPN13 and via the N-terminus of SDCCAG3 (show SDCCAG3 Antibodies).
Data indicate that Bcr-abl (show ABL1 Antibodies) increases PTPN13 promoter activity in an Icsbp (show IRF8 Antibodies)-dependent manner.
Since PTPL1 catalytic activity is important for cell transformation, VCP (show vcp Antibodies) 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 Antibodies) tyrosine phosphatase PTP-BL and are dephosphorylated.
FAP-1 has a role in binding to, and consequently inhibition of, Fas (show FAS Antibodies) export to the cell surface
examination of potential role of PTP-BL in the dynamics of the cortical actin cytoskeleton
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 Antibodies) cells.
Mutation in PTPN13 gene is associated with gastric cancer peritoneal carcinomatosis.
This work studied heat diffusion in the well-known PDZ (show INADL Antibodies)-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 (show INADL Antibodies)-mediated interaction of PTPN13 and PTEN (show PTEN Antibodies) is described with possible relevance for tumor suppression.
The effect of the viscogens sucrose, and glycerol on the kinetic response of a photoperturbed PTPN13 is investigated.
A comprehensive molecular dynamics simulation study of the PDZ2 domain of human tyrosine phosphatase 1E in the ligand-bound and -free state, as well as the photoswitchable protein in the cis (show CISH Antibodies) and trans states of the photoswitch
Thus, our results suggest a previously unknown Stat3-PTPN13 molecular network controlling squamous cell lung carcinoma development
Association of rs7014346 in POU5F1P1, rs989902 in PTPN13, and rs7003146 in TCF7L2 with variations in the risk of breast cancer in a Chinese Han population.
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.
protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)
, protein tyrosine phosphatase, non-receptor type 13
, protein-tyrosine phosphatase BAS
, tyrosine-protein phosphatase non-receptor type 13-like
, protein tyrosine phosphatase DPZPTP
, protein tyrosine phosphatase PTP-BL
, protein-tyrosine phosphatase RIP
, tyrosine phosphatase
, tyrosine-protein phosphatase non-receptor type 13
, fas-associated protein-tyrosine phosphatase 1
, protein-tyrosine phosphatase 1E
, protein-tyrosine phosphatase PTPL1