Recombinant Human PRL-1 protein is a Human Full Length protein, in the 2 to 173 aa range, expressed in Escherichia coli, with >95% purity and suitable for Inhib.
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Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.
PRL1, PTPCAAX1, PTP4A1, Protein tyrosine phosphatase type IVA 1, PTP(CAAXI), Protein-tyrosine phosphatase 4a1, Protein-tyrosine phosphatase of regenerating liver 1, PRL-1
Recombinant Human PRL-1 protein is a Human Full Length protein, in the 2 to 173 aa range, expressed in Escherichia coli, with >95% purity and suitable for Inhib.
pH: 8
Constituents: 50% Glycerol (glycerin, glycerine), 0.435% Sodium chloride, 0.395% Tris HCl, 0.307% Glutathione, 0.0584% EDTA, 0.05% Sorbitan monolaurate, ethoxylated, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.
Belongs to the protein-tyrosine phosphatase family.
Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.
0.45 U/ug. One unit will hydrolyze 1 pmol 6, 8-difluoro-4-methyl umbelliferyl phosphate (DiFMUP) per minute at pH 6.3 and 30ºC. Assay buffer: 50 mM Bis-Tris, pH 6.3, 2 mM EDTA, 2 mM DTT, 100 mM DiFMUP.
PRL-1 also known as phosphatase of regenerating liver-1 or DIFMU-P is an enzyme that functions as a phosphatase. It has a molecular mass of approximately 20 kDa. PRL-1 is actively expressed in various tissues including the liver and skeletal muscle where it plays significant roles in cellular processes. Mechanically it exhibits a dual specificity for both tyrosine and serine/threonine residues enabling it to dephosphorylate target proteins which can regulate diverse signaling pathways.
PRL-1 plays an important role in cell proliferation differentiation and migration. Its activity impacts cellular motility making it important for physiological and pathological processes. While PRL-1 primarily acts as a monomer it can also form complexes with other proteins amplifying its biological effects. Elevation in PRL-1 expression levels correlates with enhanced migratory capacity of tumor cells suggesting a role in cancer progression.
Various cellular functions involve PRL-1 which participates in the MAPK and PI3K/Akt pathways. These pathways are critical in regulating cell cycle and survival. PRL-1's relation to proteins like AKT1 and ERK1/2 highlights its contribution to intracellular signaling cascades that drive growth and survival responses in cells. PRL-1's phosphatase activity influences these pathways by modulating the phosphorylation status of various substrate proteins impacting downstream signaling.
Increased expression of PRL-1 relates to cancer particularly colorectal and breast cancers. Its role in promoting cell proliferation and migration makes it a target of interest for cancer research. PRL-1 is connected with proteins such as p53 and E-cadherin within these contexts correlating with the loss of cell-cell adhesion and increased invasive characteristics in tumor cells. Targeting PRL-1 could provide therapeutic benefits in managing cancer-associated pathologies.
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