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PRL-2/PTP4A2  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: E. coli  
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PRL-2/PTP4A2 Related Pathways

    PRL-2/PTP4A2 Related Protein, Antibody, cDNA Gene, and ELISA Kits

    PRL-2/PTP4A2 Summary & Protein Information

    PRL-2/PTP4A2 Background

    Gene Summary: The protein encoded by PTP4A2 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. [provided by RefSeq, Aug 2010]
    General information above from NCBI
    Catalytic activity: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
    Enzyme regulation: Inhibited by sodium orthovanadate and pentamidine.
    Subunit structure: In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB.
    Subcellular location: Cell membrane. Early endosome. Cytoplasm.
    Tissue specificity: Ubiquitously expressed, with highest levels in skeletal muscle, heart and thymus. Overexpressed in prostate tumor tissue.
    Post-translational: Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB. Unfarnesylated forms are redirected to the nucleus and cytosol.
    Sequence similarity: Belongs to the protein-tyrosine phosphatase family.
    Contains 1 tyrosine-protein phosphatase domain.C
    General information above from UniProt

    PRL-2 (Protein-tyrosine phosphatase of regenerating liver 2), also known as PTP4A2 (Protein tyrosine phosphatase type IVA, member 2), is a member of PTP family and has an important function in controlling cell growth. PRL-2 phosphatases may be multifunctional enzymes with diverse roles in a variety of tissue and cell types. The phosphatase of regenerating liver (PRL) family, comprising PRL-1, PRL-2 and PRL-3, is a group of prenylated phosphatases that are candidate cancer biomarkers and therapeutic targets. PRL-1, PRL-2, and PRL-3 represent a novel class of protein-tyrosine phosphatase with a C-terminal prenylation motif. They are three closely related intracellular enzymes that possess the PTP active site signature sequence CX 5R. The PRL-2 mRNA is elevated in primary breast tumors relative to matched normal tissue, and also dramatically elevated in metastatic lymph nodes compared with primary tumors. PRL-2 plays a role in breast cancer progression. PRL-2 is a pathogenic molecule in hematopoietic malignancies and suggest its potential as a novel therapeutic target.

    PRL-2/PTP4A2 Alternative Name

    HH13,PRL2,PRL-2,PTP4A,PTP4A2,PTPCAAX2,ptp-IV1a,ptp-IV1b,BM-008,HH7-2,HU-PP-1,OV-1, [human]
    MGC102154,Prl-2,Ptp4a2,MGC103400,RP23-114O4.2, [mouse]

    PRL-2/PTP4A2 Related Studies

  • Akiyama S, et al. (2010) PRL-2 increases Epo and IL-3 responses in hematopoietic cells. Blood Cells Mol Dis. 44(4): 209-14.
  • Hardy S, et al. (2010) Overexpression of the protein tyrosine phosphatase PRL-2 correlates with breast tumor formation and progression. Cancer Res. 70(21): 8959-67.
  • Yuan L, et al. (2007) Differential expression and functional constraint of PRL-2 in hibernating bat. Comp Biochem Physiol B Biochem Mol Biol. 148(4): 375-81.
  • Dumaual CM, et al. (2006) Cellular localization of PRL-1 and PRL-2 gene expression in normal adult human tissues. J Histochem Cytochem. 54(12): 1401-12.
  • Zeng Q, et al. (2000) Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. J Biol Chem. 275(28): 21444-52.