PRL-2 / PTP4A2 Protein

Phosphatase of regenerating liver 2 / Protein tyrosine phosphatase type IVA, member 2

PRL-2 / PTP4A2 Products

PRL-2 / PTP4A2 Protein, Recombinant

Molecule	Species	Description //For Detailed Info. and Price------CLICK!	Cat. No
PRL-2/PTP4A2	Human	PRL-2/PTP4A2 Protein, Recombinant, with GST Tag	13097-H09E

PRL-2 / PTP4A2 cDNA Clone

Molecule	Species	Description //For Detailed Info. and Price------CLICK!	Cat. No
PRL-2/PTP4A2	Human	Human PTP4A2 Gene cDNA Clone / ORF Clone	HG13097-G

PRL-2 / PTP4A2 Related Areas

Cancer>>Cell Cycle>>PRL-2/PTP4A2

PRL-2 / PTP4A2 Alternative Names

PTP4A2, BM-008, HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, PTP4A, PTPCAAX2, ptp-IV1a, ptp-IV1b [Homo sapiens]

Ptp4a2, RP23-114O4.2, MGC102154, MGC103400, Prl-2 [Mus musculus]

PRL-2 / PTP4A2 Background

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 Related Studies

1. Akiyama S, et al. (2010) PRL-2 increases Epo and IL-3 responses in hematopoietic cells. Blood Cells Mol Dis. 44(4): 209-14.
2. 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.
3. 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.
4. 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.
5. 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.