|Application ||WB, E|
|Calculated MW||19535 Da|
|Other Names||Protein tyrosine phosphatase type IVA 3, PRL-R, Protein-tyrosine phosphatase 4a3, Protein-tyrosine phosphatase of regenerating liver 3, PRL-3, PTP4A3, PRL3|
|Target/Specificity||This PRL3 antibody is generated from rabbits immunized with a recombinant protein encoding full length of human PRL3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PRL3 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.|
|Cellular Location||Cell membrane. Early endosome|
|Tissue Location||Mainly expressed in cardiomyocytes and skeletal muscle; also found in pancreas. Consistently overexpressed in colon cancer metastasis|
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Provided below are standard protocols that you may find useful for product applications.
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. PRL-3 expression was found to be up-regulated in human liver carcinoma compared with normal liver. Its expression in colorectal cancers may contribute to the establishment of liver metastasis. In a different study, PRL-3 is found to be expressed in tumor metastasis and vasculature, regardless of the tumor source.
Kato,H., et al. Clin. Cancer Res. 10 (21), 7318-7328 (2004)
Wu,X., et al. Am. J. Pathol. 164 (6), 2039-2054 (2004)
Kim,K.A., et al. FEBS Lett. 565 (1-3), 181-187 (2004)
Kozlov,G., et al. J. Biol. Chem. 279 (12), 11882-11889 (2004)
Bardelli,A., eta l. Clin. Cancer Res. 9 (15), 5607-5615 (2003)
Saha,S., et al. Science 294 (5545), 1343-1346 (2001)
Matter,W.F., et al. Biochem. Biophys. Res. Commun. 283 (5), 1061-1068 (2001)
Zeng,Q., et al. J. Biol. Chem. 275 (28), 21444-21452 (2000)
Zeng,Q., et al. Biochem. Biophys. Res. Commun. 244 (2), 421-427 (1998)
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