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 -70C. 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.
Molekulargewicht:
4243
Reinheit:
Purified ~90%
Formulierung:
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 th
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