Actin and myosin are the two major cytoskeletal proteins implicated in cellular movements, secretion, phagocytosis, cytokinesis, exocytosis and chromosome movement. At least 6 actin isoforms have been identified by protein sequence analyses. Four actin isoforms represents the differentiation markers of muscle tissues. Actin isoforms are >90% conserved, except the N-terminal 18aa (50-60% homology).
In absence of salts, actin exists as a globular monomeric protein (G-actin). In presence of ATP, a divalent cation (Ca 2+ or Mg 2+) and high salts ( KCl, NaCl or MgCl2), the G-actin polymerizes to form a fibrous or filamentous actin (F-actin) which incorporates the cation and ATP. Dialysis of the F-actin solution against water reverses the polymerization.
Source:Prepared from the acetone powder of bovine skeletal muscle by the method of Spudich and Watt. A mol. wt of approximately 42-43kD based on sequence information of the rabbit muscle protein general similarity of actins across species and SDS electrophoresis.
Form: Protein estimated by Biuret is approximately 90%.
Storage and Stability:For long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 12 months.
仕様
Size：100ug
Source Antigen：Bovine skeletal muscle
Grade：Purified
Purity：Purified ~90%
Form：Supplied as a liquid in buffer A (2mM Tris buffer, pH 8.0, 0.02mM ATP, 0.5mM, Beta-mercaptanol and 0.2mM CaCl2). The filtrate is clarified by centrifugation, then the action is polymerized by addition of 50mM KCl and 2mM MgCl2. The KCl concentration is then increase to 0.6M and the solution is stirred for 90 minutes. The F-actin is then collected by centrifugation, resuspended in Buffer A and extensively dialyzed to convert to G-actin. Protein estimated by Biuret is approximately 90%.
