PTPµ Antibody (SK15): sc-56959

PTPµ Antibody (SK15) is a mouse monoclonal IgG1 antibody that detects PTPµ in mouse, rat, and human samples through western blotting (WB) and immunoprecipitation (IP) applications. PTPµ, a member of the protein tyrosine phosphatase family, is primarily localized to the cell membrane and plays a crucial role in cell adhesion and signaling processes. PTPµ′s unique structure includes a conserved amino-terminal MAM domain, which is essential for homophilic binding, allowing PTPµ to interact with itself and potentially regulate the assembly and disassembly of cadherin/catenin complexes at cell junctions. This function is vital for maintaining tissue integrity and facilitating communication between cells, which is particularly important during development and in the context of tumor progression. Dysregulation of PTPµ has been implicated in various diseases, making PTPµ a significant target for research into therapeutic interventions. Anti-PTPµ antibody (SK15) is an invaluable tool for researchers studying the intricate roles of protein tyrosine phosphatases in cellular processes and disease mechanisms.

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

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

PTPµ Antibody (SK15) References:

1. Receptor-type protein-tyrosine phosphatase mu is expressed in specific vascular endothelial beds in vivo.  |  Bianchi, C., et al. 1999. Exp Cell Res. 248: 329-38. PMID: 10094839
2. Protein tyrosine phosphatase-mu differentially regulates neurite outgrowth of nasal and temporal neurons in the retina.  |  Burden-Gulley, SM., et al. 2002. J Neurosci. 22: 3615-27. PMID: 11978837
3. The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu.  |  Cismasiu, VB., et al. 2004. J Biol Chem. 279: 26922-31. PMID: 15084579
4. The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase mu.  |  Del Vecchio, RL. and Tonks, NK. 2005. J Biol Chem. 280: 1603-12. PMID: 15491993
5. Impaired flow-induced dilation in mesenteric resistance arteries from receptor protein tyrosine phosphatase-mu-deficient mice.  |  Koop, EA., et al. 2005. Am J Physiol Heart Circ Physiol. 288: H1218-23. PMID: 15706045
6. Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion.  |  Aricescu, AR., et al. 2006. EMBO J. 25: 701-12. PMID: 16456543
7. E-cadherin promotes retinal ganglion cell neurite outgrowth in a protein tyrosine phosphatase-mu-dependent manner.  |  Oblander, SA., et al. 2007. Mol Cell Neurosci. 34: 481-92. PMID: 17276081
8. Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration.  |  Burgoyne, AM., et al. 2009. Cancer Res. 69: 6960-8. PMID: 19690139
9. Protein tyrosine phosphatase mu regulates glioblastoma cell growth and survival in vivo.  |  Kaur, H., et al. 2012. Neuro Oncol. 14: 561-73. PMID: 22505657
10. The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu.  |  Hoffmann, KM., et al. 1997. J Biol Chem. 272: 27505-8. PMID: 9346878