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The protein encoded by PTP4A2 belongs to a small class of the protein tyrosine phosphatase (PTP) family. Zusätzlich bieten wir Ihnen Protein tyrosine Phosphatase Type IVA, Member 2 Proteine (16) und viele weitere Produktgruppen zu diesem Protein an.
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Human Monoclonal PTP4A2 Primary Antibody für ELISA, WB - ABIN1724901
Hardy, Wong, Muller, Park, Tremblay: Overexpression of the protein tyrosine phosphatase PRL-2 correlates with breast tumor formation and progression. in Cancer research 2010
Show all 2 Pubmed References
a critical role for PRL2 phosphatase in mediating Notch and c-Kit signals in early T cell progenitors, is reported.
Oncogenic PRL-2 controls tumor growth by modulating intracellular magnesium levels through binding with the CNNM3 magnesium transporter.
PTP4A2 plays critical roles in regulating hematopoietic stem cell self-renewal and mediating SCF/KIT signaling.
PRL2 promotes Kit-mediated PI3K/Akt signaling by reducing the level of PTEN that normally antagonizes the pathway.
Phosphatase of regenerating liver 2 (PRL2) is essential for placental development by down-regulating PTEN (Phosphatase and Tensin Homologue Deleted on Chromosome 10) and activating Akt protein
identified a critical role for PRL2 phosphatase in the proliferation and survival of human AML cells. Further, we demonstrated that PRL2 is essential for the leukemogenic potential of AML1-ETO9a in vivo
In the Title.
Our findings highlight the important role of miR-29c in regulating CRC EMT via GSK-3b/b-catenin signaling by targeting GNA13 and PTP4A and provide new insights into the metastatic basis of colorectal cancer
PTP4A2 expression is correlated with overall survival in progestin receptor-positive breast carcinomas.
Results suggest that TRP32 maintains the reduced state of PRL and thus regulates the biological function of PRL.
Studies indicate that PRL-1 and PRL-2 and PRL-3 are oncogenes and belong to the few phosphatases that lead to the development of cancer.
Results suggest a model in which PRL-2 promotes cell migration and invasion through an ERK1/2-dependent signaling pathway.
PRL-2 plays an important role in lung cancer and can be a biomarker of lung cancer, substituting for the function of other PRLs.
Overexpression of the protein tyrosine phosphatase PRL-2 correlates with breast tumor formation and progression.
Mouse pre-B-cells transfected with human PRL-2 had higher growth responses to Epo or IL-3, shorter cell cycle, less Epo requirement for survival, more cell migration, less cell adhesion, change to an immature cell morphology, & more Bmi-1 expression.
PRL-2 can promote cell adhesion and invasion activity of human hepatocellular carcinoma cells.
PRL phosphatases increase cell proliferation by stimulating progression from G1 into S phase
PRL-2 mRNA expression was not significantly higher in malignant compared to benign breast tissue.
PRL-2 was expressed heavily in almost every tissue and cell type examined. Widespread expression of PRL-2 in multiple organ systems suggests an important functional role for these enzymes in normal tissue homeostasis.
Colonic adenocarcinoma cells have the ability to produce PTP4A1, PTP4a2, and PTP4A3, which may relate to the lymph node metastasis of colonic adenocarcinoma.
The protein encoded by this gene belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif. This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis. Alternatively spliced transcript variants have been described. Related pseudogenes exist on chromosomes 11, 12 and 17.
, protein tyrosine phosphatase type IVA 2
, protein tyrosine phosphatase 4a2
, protein tyrosine phosphatase type IVA, member 2
, protein-tyrosine phosphatase 4a2
, protein-tyrosine phosphatase of regenerating liver 2
, phosphatase of regenerating liver 2
, protein tyrosine phosphatase IVA
, protein tyrosine phosphatase IVA2