Anti-Actin/ACTA1 Antibody Picoband® (monoclonal, 3H5) Fluoro488 Conjugated

Actin, a highly conserved protein, is a major component of both the cytoskeletal and contractile structures in the cell types. It varies in amount, being related to the type of differentiation and to the functional state of cells and tissues. The actins exhibit over 90% sequence homology, but each isoform has a unique NH2-terminal sequence. The isoforms are comprised of three alpha-actin, one beta-actin, two gamma-actin. Because the amino acid sequence of the C-terminal is the same for almost all actins, this antibody has been raised using a synthetic peptide corresponding to the C-terminal 11 residues.

Cancer, Cell Biology, Cell Cycle, Cell Division,2339, Chromosome Structure, DNA/RNA, DNA Damage & Repair, DNA Damage Response, Epigenetics and Nuclear Signaling

Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin.

1. Gunning, P., Ponte, P., Okayama, H., Engel, J., Blau, H. and Kedes, L.Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed.Mol. Cell. Biol.1983; 3 (5), 787-795. 2. Goebel, H.H., Brockmann, K., Bonnemann, C.G., Warlo, I.A., Hanefeld, F., Labeit, S., Durling, H.J. and Laing, N.G. Actin- related myopathy without any missense mutation in the ACTA1 Gene.J. Child Neurol.2004; 19 (2), 149-153. 3. Laing, N.G., Clarke, N.F., Dye, D.E., Liyanage, K., Walker, K.R., Kobayashi, Y., Shimakawa, S., Hagiwara, T., Ouvrier, R., Sparrow, J.C., Nishino, I., North, K.N. and Nonaka, I.Actin mutations are one cause of congenital fibre type disproportion.Ann. Neurol.2004; 56 (5), 689-694.