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The protein encoded by PTP4A3 belongs to a small class of prenylated protein tyrosine phosphatases (PTPs). Additionally we are shipping PTP4A3 Antibodies (75) and PTP4A3 Proteins (11) and many more products for this protein.
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our results suggest that the Prl3b1-cre mice line provides a unique resource to understand testicular germ-cell development
Results demonstrate that Ptp4a3 contributes to the malignant phenotype of tumor-initiating cells.
PRL-3 protein was significantly reduced in mouse STAT3 (show STAT3 ELISA Kits)-knockout liver cells compared with STAT3 (show STAT3 ELISA Kits)-wild type counterparts, and ectopic expression of STAT3 (show STAT3 ELISA Kits) in these cells led to a pronounced increase in PRL-3 protein.
Data indicate that Mycobacterium tuberculosis T cell stimulatory epitope (MT) is a potentially effective molecular adjuvant in preparation of monoclonal antibody (mAb) specific for phosphatase of regenerating liver-3 (PRL-3).
These findings strongly support a role for PTP4A3 as an important contributor to endothelial cell function and as a multimodal target for cancer therapy and mitigating VEGF-regulated angiogenesis.
the first definitive evidence implicating Ptp4a3 in colon tumorigenesis
role of PTP4A3 in acute myeloid leukemia (show BCL11A ELISA Kits)
PTP4A3 was identified as a novel negative regulator of LPS (show TLR4 ELISA Kits)-induced LITAF/TNF-alpha production.
PRL-3 was highly expressed in metastatic melanoma B16-BL6 cells but not in its lowly metastatic parental cell line, B16 cells
PRL-3-expressing cells rapidly induce metastatic tumor formation in lung
Data show that phosphatase of regenerating liver-3 (PRL (show PRL ELISA Kits)-3a) is an important mediator of growth factor signaling in MM cells and hence possibly a good target for treatment of MM.
Data suggest that phosphatase of regenerating liver-3 (PRL-3)might play a tumor suppressor role in lung cancer, distinct from other cancers, by inhibiting epithelial-mesenchymal transition (EMT (show ITK ELISA Kits))-related pathways.
A novel role of PRL-3 in tumor development through its adverse impact on telomere homeostasis.
our result indicated that PRL-3 promotes protein phosphorylation by acting as an 'activator kinase' and consequently regulates cytokine secretion.
The disruption of epithelial architecture by PRL-3 revealed here is a newly recognized mechanism for PRL-3-promoted cancer progression.
This study suggests PRL-3 and SFKs are key mediators of the IL6 (show IL6 ELISA Kits)-driven signaling events.
Regulation of PTP4A3 expression is altered in specific subgroups of acute leukemias and this is likely brought about by expression of the aberrant ETV6 (show ETV6 ELISA Kits)-RUNX1 (show RUNX1 ELISA Kits) and BCR (show BCR ELISA Kits)-ABL1 (show ABL1 ELISA Kits) fusion genes.
PRL-3 engages the focal adhesion pathway in trip0le-negative breast cancer cells as a key mechanism for promoting TNBC cell migration and invasion.
PTP4A3 regulated glioblastoma multiforme via miR (show MLXIP ELISA Kits)-137-mediated Akt (show AKT1 ELISA Kits)/mTOR (show FRAP1 ELISA Kits) signaling pathway.
Studies suggest that transcriptional, translational, or posttranslational regulation might be involved in the aberrant expression of phosphatase of regenerating liver (PRL)-3.
Results uncovered that aberrant overexpression of PRL-3 could initiate chordoma in early development.
Data show that protein-tyrosine phosphatase (show ACP1 ELISA Kits) PRP4A3 (prl3) and van gogh like1 (vangl1 (show Vangl1 ELISA Kits)) are Necessary Components in prohibitin1 (phb1 (show PHB ELISA Kits)) dependent neural crest specification.
PTP4A3 is required for cephalic neural crest migration in vivo during embryonic development.
The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs). PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This class of PTPs contain a PTP domain and a characteristic C-terminal prenylation motif. Studies of this class of PTPs in mice demonstrated that they were prenylated proteins in vivo, which suggested their association with cell plasma membrane. Overexpression of this gene in mammalian cells was reported to inhibit angiotensin-II induced cell calcium mobilization and promote cell growth. Two alternatively spliced variants exist.
protein tyrosine phosphatase type IVA, member 3
, protein tyrosine phosphatase type IVA 3
, protein-tyrosine phosphatase 4a3
, protein-tyrosine phosphatase of regenerating liver 3
, potentially prenylated protein tyrosine phosphatase
, protein tyrosine phosphatase 4a3