Clone: 2A3
Background: Among the six actin isoforms described in mammals, two are found in virtually all cells (β- and γ-cytoplasmic), two are detected in smooth muscle cells (α- and γ-smooth muscle) and two are present in striated muscles, one predominantly in skeletal (α-skeletal) and one in cardiac (α-cardiac) muscle cells. These actin isoforms differ slightly in their N-terminus, but the sequence of each of these actins is highly conserved in higher vertebRates. β- and γ-cytoplasmic actin play crucial roles during various key cellular processes. Whereas β-actin is preferentially localized in stress fibers, circular bundles and at cell-cell contacts, suggesting a role in cell attachment and contraction, γ-actin displays a more versatile organization, according to cell activities. In moving cells, γ-actin is mainly organized as a meshwork in cortical and lamellipodial structures, suggesting a role in cell motility. β- and γ-actin depleted fibroblasts exhibit distinct changes in motility compared with their controls, suggesting a specific role for each isoform in cell locomotion.
Source: 2A3 is a Mouse monoclonal IgG2b antibody derived by fusion of NS0 Mouse myeloma cells with spleen cells from a BALB/c Mouse immunized with a peptide comprising the N-terminal nonapeptide of γ-cytoplasmic actin with an acetylated N-terminus (Ac-EEEIAALVI-COOH) coupled to keyhole limpet hemocyanin through the cysteine residue. The antibody does not cross react with other actin isoforms.
Specificity: 2A3 is a mouse monoclonal IgG2b antibody highly specific for γ-cytoplasmic actin (γ-actin 1; encoded by ACTG1). It does not cross-react with the γ-actin isoform expressed in the enteric smooth muscle tissues (γ-actin 2; encoded by ACTG2).
Formulation: Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.
References: 1. Vandekerckhove, J. and Weber, K. (1978). At least six different actins are expressed in a higher mammal: an analysis based on the amino acid sequence of the amino-terminal tryptic peptide. J Mol Biol. 126(4), 783-802.2. Bassell, G.J., Zhang, H., Byrd, A.L., Femino, A.M., Singer, R.H., Taneja, K.L., Lifshitz, L.M., Herman, I.M. and Kosik, K.S. (1998). Sorting of beta-actin mRNA and protein to neurites and growth cones in culture. J Neurosci. 1998 18(1), 251-65.3. Dugina, V., Zwaenepoel, I., Gabbiani, G., Clément, S. and Chaponnier, C. (2009). ß- and y-cytoplasmic actins display distinct distribution and functional diversity. J Cell Sci 122, 2980-88.4. Gallant, C., Appel, S., Graceffa, P., Leavis, P., Lin, J.J., Gunning, P.W., Schevzov, G., Chaponnier, C., Degnore, J., Lehman, W. and Morgan, K.G. (2011). Tropomyosin variants describe distinct functional subcellular domains in differentiated vascular smooth muscle cells. Am J Physiol Cell Physiol. 300(6), 1356-65.
UniProt: P63261
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. This product contains sodium azide. To prevent formation of toxic vapors, do not mix with strong acidic solutions. To prevent formation of potentially explosive metallic azides in metal plumbing, always wash into drain with copious quantities of water.This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
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