PRL-1/2/3 Antibody (G-10): sc-365659

PRL-1/2/3 Antibody (G-10) is a mouse monoclonal IgG1 antibody that detects PRL-1/2/3 in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). PRL-1/2/3 proteins, part of the protein tyrosine phosphatase family, play crucial roles in regulating cellular processes, particularly in cell growth and division. PRL-3, also known as Protein Tyrosine Phosphatase Type IVA, member 3, is predominantly expressed in heart and skeletal muscle, as well as in epithelial cells of the small intestine, where PRL-3 associates with the cell plasma membrane. PRL-3′s localization is significant as PRL-3 is involved in critical signaling pathways that regulate cell proliferation and migration. Overexpression of PRL-3 has been linked to the inhibition of angiotensin-II induced calcium mobilization, which in turn promotes cell growth and is associated with colorectal cancer metastasis. PRL-3 serves as both a vital player in normal cellular functions and a potential therapeutic target for cancer treatment. PRL-1/2/3 (G-10) antibody is an essential tool for researchers studying these important proteins and their roles in various biological processes and diseases.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

PRL-1/2/3 Antibody (G-10) References:

1. Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome.  |  Zeng, Q., et al. 2000. J Biol Chem. 275: 21444-52. PMID: 10747914
2. PRL-3 and PRL-1 promote cell migration, invasion, and metastasis.  |  Zeng, Q., et al. 2003. Cancer Res. 63: 2716-22. PMID: 12782572
3. Generation of PRL-3- and PRL-1-specific monoclonal antibodies as potential diagnostic markers for cancer metastases.  |  Li, J., et al. 2005. Clin Cancer Res. 11: 2195-204. PMID: 15788667
4. Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer.  |  Radke, I., et al. 2006. Br J Cancer. 95: 347-54. PMID: 16832410
5. PRL-1 protein promotes ERK1/2 and RhoA protein activation through a non-canonical interaction with the Src homology 3 domain of p115 Rho GTPase-activating protein.  |  Bai, Y., et al. 2011. J Biol Chem. 286: 42316-42324. PMID: 22009749
6. RNAi‑mediated knockdown of PRL‑3 inhibits cell invasion and downregulates ERK 1/2 expression in the human gastric cancer cell line, SGC‑7901.  |  Cao, Y., et al. 2013. Mol Med Rep. 7: 1805-11. PMID: 23589069
7. Localizing PRL-2 expression and determining the effects of dietary Mg(2+) on expression levels.  |  Gungabeesoon, J., et al. 2016. Histochem Cell Biol. 146: 99-111. PMID: 27015884
8. The phosphatase PRL-3 affects intestinal homeostasis by altering the crypt cell composition.  |  Rubio, T., et al. 2021. J Mol Med (Berl). 99: 1413-1426. PMID: 34129057
9. Increased PRL-1 in BM-derived MSCs triggers anaerobic metabolism via mitochondria in a cholestatic rat model.  |  Kim, JY., et al. 2023. Mol Ther Nucleic Acids. 31: 512-524. PMID: 36865088
10. Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1.  |  Zeng, Q., et al. 1998. Biochem Biophys Res Commun. 244: 421-7. PMID: 9514946

The preferred PRL-3 antibody is PRL-3 Antibody (318): sc-130355.