Integrin α3/ITGA3/CD49c Antibody (F35 177-1): sc-53354

Integrin α3 Antibody (F35 177-1) is a mouse monoclonal IgG1 kappa light chain antibody that detects Integrin α3 protein of human origin by immunofluorescence (IF). Integrin α3, also known as very late activation antigen 3 (VLA-3), plays a crucial role in cell adhesion and signaling, which are essential for various biological processes such as cell growth, differentiation, migration, and apoptosis. Integrin α3 is primarily located on the cell surface, where anti-Integrin α3 antibody (F35 177-1) can detect heterodimers with β1 subunits, allowing interaction with components of the extracellular matrix, including fibronectin, collagen, and vitronectin. The proper localization of Integrin α3 is vital for function, as Integrin α3 facilitates communication between cells and their environment, enabling responses to external signals and maintaining tissue integrity. Additionally, Integrin α3 undergoes post-translational modifications, including cleavage in the extracellular domain, which results in disulfide-linked light and heavy chains that are essential for structural integrity and functional interactions. Integrin α3 monoclonal antibody (F35 177-1) is an invaluable tool for researchers studying the dynamics of cell adhesion and signaling pathways in human tissues.

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Integrin α3/ITGA3/CD49c Antibody (F35 177-1) References:

1. CD9 is expressed in extravillous trophoblasts in association with integrin alpha3 and integrin alpha5.  |  Hirano, T., et al. 1999. Mol Hum Reprod. 5: 162-7. PMID: 10065872
2. Differential regulation of cellular adhesion and migration by recombinant laminin-5 forms with partial deletion or mutation within the G3 domain of alpha3 chain.  |  Kariya, Y., et al. 2003. J Cell Biochem. 88: 506-20. PMID: 12532327
3. Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin.  |  Hamano, Y., et al. 2003. Cancer Cell. 3: 589-601. PMID: 12842087
4. Gain of glycosylation in integrin α3 causes lung disease and nephrotic syndrome.  |  Nicolaou, N., et al. 2012. J Clin Invest. 122: 4375-87. PMID: 23114595
5. Loss of integrin α3 prevents skin tumor formation by promoting epidermal turnover and depletion of slow-cycling cells.  |  Sachs, N., et al. 2012. Proc Natl Acad Sci U S A. 109: 21468-73. PMID: 23236172
6. Identification of integrin α3 as a molecular marker of cells undergoing epithelial-mesenchymal transition and of cancer cells with aggressive phenotypes.  |  Shirakihara, T., et al. 2013. Cancer Sci. 104: 1189-97. PMID: 23786209
7. Disease-associated single amino acid mutation in the calf-1 domain of integrin α3 leads to defects in its processing and cell surface expression.  |  Yamada, M. and Sekiguchi, K. 2013. Biochem Biophys Res Commun. 441: 988-93. PMID: 24220332
8. Combined mTOR inhibitor rapamycin and doxorubicin-loaded cyclic octapeptide modified liposomes for targeting integrin α3 in triple-negative breast cancer.  |  Dai, W., et al. 2014. Biomaterials. 35: 5347-5358. PMID: 24726747
9. High integrin α3 expression is associated with poor prognosis in patients with non-small cell lung cancer.  |  Li, Q., et al. 2020. Transl Lung Cancer Res. 9: 1361-1378. PMID: 32953510
10. Monoclonal antibody ONS-M21 recognizes integrin alpha3 in gliomas and medulloblastomas.  |  Kishima, H., et al. 1999. Br J Cancer. 79: 333-9. PMID: 9888477

The preferred Integrin α3/ITGA3/CD49c antibody is Integrin α3/ITGA3/CD49c Antibody (A-3): sc-374242.