PTPµ Antibody (SBK10): sc-65228

PTPµ Antibody (SBK10) is a mouse monoclonal IgG1 kappa light chain antibody that detects PTPμ protein of mouse, rat, and human origin by western blotting (WB) and immunoprecipitation (IP). Anti-PTPμ antibody (SBK10) is available as the non-conjugated format. PTPμ protein is a member of the protein tyrosine phosphatase family, which plays a crucial role in cellular signaling by dephosphorylating tyrosine residues on proteins, thereby regulating various cellular processes such as growth, differentiation, and metabolism. PTPμ is a type I transmembrane protein primarily localized at cell-cell contact points, where PTPμ is involved in the assembly and disassembly of cadherin/catenin complexes, essential for maintaining cell adhesion and tissue integrity. Such localization is particularly important in development and tissue homeostasis, helping regulate interactions between neighboring cells. Dysregulation of PTPμ has been implicated in various pathological conditions, including cancer, making PTPμ a significant target for research in understanding tumor biology and potential therapeutic interventions.

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PTPµ Antibody (SBK10) References:

1. Protein kinase C delta (PKCdelta) is required for protein tyrosine phosphatase mu (PTPmu)-dependent neurite outgrowth.  |  Rosdahl, JA., et al. 2002. Mol Cell Neurosci. 19: 292-306. PMID: 11860281
2. Receptor protein tyrosine phosphatase mu expression as a marker for endothelial cell heterogeneity; analysis of RPTPmu gene expression using LacZ knock-in mice.  |  Koop, EA., et al. 2003. Int J Dev Biol. 47: 345-54. PMID: 12895029
3. Caveolin-1 is transiently dephosphorylated by shear stress-activated protein tyrosine phosphatase mu.  |  Shin, J., et al. 2006. Biochem Biophys Res Commun. 339: 737-41. PMID: 16325778
4. Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration.  |  Phillips-Mason, PJ., et al. 2011. J Cell Biochem. 112: 39-48. PMID: 20506511
5. Diverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia.  |  Hyun, SW., et al. 2011. Exp Lung Res. 37: 327-43. PMID: 21649524
6. Complex-type asparagine-linked oligosaccharides on phosphacan and protein-tyrosine phosphatase-zeta/beta mediate their binding to neural cell adhesion molecules and tenascin.  |  Milev, P., et al. 1995. J Biol Chem. 270: 24650-3. PMID: 7559574
7. Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras OR neu.  |  Elson, A. and Leder, P. 1995. J Biol Chem. 270: 26116-22. PMID: 7592814
8. Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo.  |  Brady-Kalnay, SM., et al. 1995. J Cell Biol. 130: 977-86. PMID: 7642713
9. Increased abundance of the receptor-type protein-tyrosine phosphatase LAR accounts for the elevated insulin receptor dephosphorylating activity in adipose tissue of obese human subjects.  |  Ahmad, F., et al. 1995. J Clin Invest. 95: 2806-12. PMID: 7769120
10. Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain.  |  Zondag, GC., et al. 1995. J Biol Chem. 270: 14247-50. PMID: 7782276
11. Stimulation of receptor protein-tyrosine phosphatase alpha activity and phosphorylation by phorbol ester.  |  den Hertog, J., et al. 1995. Cell Growth Differ. 6: 303-7. PMID: 7794797
12. Increased proteolytic processing of protein tyrosine phosphatase mu in confluent vascular endothelial cells: the role of PC5, a member of the subtilisin family.  |  Campan, M., et al. 1996. Biochemistry. 35: 3797-802. PMID: 8620001