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The protein encoded by PTPN13 is a member of the protein tyrosine phosphatase (PTP) family. Zusätzlich bieten wir Ihnen PTPN13 Antikörper (54) und PTPN13 Proteine (6) und viele weitere Produktgruppen zu diesem Protein an.
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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 (zeige FAM126A ELISA Kits) cells.
Mutation in PTPN13 gene is associated with gastric cancer peritoneal carcinomatosis.
This work studied heat diffusion in the well-known PDZ (zeige INADL ELISA Kits)-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.
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 (zeige CISH ELISA Kits) and trans states of the photoswitch
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 (zeige CTNNB1 ELISA Kits) 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 (zeige INADL ELISA Kits) binding motif of APC (zeige APC ELISA Kits).
SDCCAG3 (zeige SDCCAG3 ELISA Kits) forms a complex with PTPN13. Interaction of SDCCAG3 (zeige SDCCAG3 ELISA Kits) with PTPN13 is mediated via the FERM domain of PTPN13 and via the N-terminus of SDCCAG3 (zeige SDCCAG3 ELISA Kits).
Data indicate that Bcr-abl (zeige ABL1 ELISA Kits) increases PTPN13 promoter activity in an Icsbp (zeige IRF8 ELISA Kits)-dependent manner.
Since PTPL1 catalytic activity is important for cell transformation, VCP (zeige vcp ELISA Kits) 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 (zeige USH1C ELISA Kits) tyrosine phosphatase PTP-BL and are dephosphorylated.
FAP-1 has a role in binding to, and consequently inhibition of, Fas (zeige FAS ELISA Kits) export to the cell surface
RSK2 (zeige RPS6KA3 ELISA Kits) phosphorylates three sites in Cdc25C (zeige CDC25C ELISA Kits) and also partially activates Cdc25C (zeige CDC25C ELISA Kits).
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