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The protein encoded by PTP4A1 belongs to a small class of prenylated protein tyrosine phosphatases (PTPs), which contains a PTP domain and a characteristic C-terminal prenylation motif. Additionally we are shipping PTP4A1 Antibodies (88) and PTP4A1 Kits (1) and many more products for this protein.
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data shed new light on the structural basis underlying the interaction between PRL (show PRL Proteins) phosphatases and CNNM transporters and provides a hypothesis about the molecular mechanism by which PRL-1, upon binding to CNNM2 (show CNNM2 Proteins), might increase the intracellular concentration of Mg(2 (show MCOLN1 Proteins)+) thereby contributing to tumor progression and metastasis.
Prl-1 is required for proper timing of liver regeneration after partial hepatectomy
PRL-1 binding to p115 RhoGAP (show ARHGAP1 Proteins) provides a coordinated mechanism underlying ERK1/2 and RhoA (show RHOA Proteins) activation
In cones and cone-derived cultured cells both Prl-1 activity and Prl-1 gene expression are modulated under oxidative stress.
Results showed that SIAH1 and PTP4A1 expression was regulated by mir-944 in breast cancer cells. miR-944 binds directly the 3 UTR of their promotor region.
miR (show MLXIP Proteins)-601 inhibits growth and invasion of breast cancer cells by targeting PTP4A1.
Data indicate that protein-tyrosine-phosphatase of regenerating liver 1 (PRL1) gene was expressed much more highly in prostate cancer (PCa (show FLVCR1 Proteins)) than in nonneoplastic prostate samples.
Upregulation of PRL-1 (show PLRG1 Proteins) expression is inversely correlated with miR (show MLXIP Proteins)-26a in primary cervical cancer tissues.
Data highlight the oncogenic function of PRL-1 (show PLRG1 Proteins) in HCC (show FAM126A Proteins) invasion and metastasis.
We confirmed with our previous findings that PTP4A1-PHF3-EYS variants were significantly associated with alcohol dependence.
PTP4A1-PHF3-EYS variants were associated with alcohol dependence.
Results suggest that TRP32 maintains the reduced state of PRL (show PRL Proteins) and thus regulates the biological function of PRL (show PRL Proteins).
Studies indicate that PRL-1 (show PLRG1 Proteins) and PRL-2 (show PTP4A2 Proteins) and PRL-3 are oncogenes and belong to the few phosphatases that lead to the development of cancer.
upregulation of PRL-1 (show PLRG1 Proteins) protein correlates with shortened patient survival in human hepatocellular carcinoma
The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs), which contains a PTP domain and a characteristic C-terminal prenylation motif. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This tyrosine phosphatase is a nuclear protein, but may primarily associate with plasma membrane. The surface membrane association of this protein depends on its C-terminal prenylation. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which implicated its role in the tumorigenesis. Studies in rat suggested that this gene may be an immediate-early gene in mitogen-stimulated cells.
protein tyrosine phosphatase type IVA 1
, protein tyrosine phosphatase type IVA, member 1
, Protein tyrosine phosphatase type IVA 1
, protein-tyrosine phosphatase 4a1
, protein-tyrosine phosphatase of regenerating liver 1
, protein tyrosine phosphatase type IVA protein 1
, protein tyrosine phosphatase 4a1