ATP: 100mM stock

ATP: 100mM stock

Product Uses Include

  • Addition to general actin buffer
  •  Substrate for ATPases
  • Energy source for kinesin motor activity
  • Energy source for kinases


Adenosine triphosphate (ATP). 100 mM solution of ATP at pH 7.0 (to reduce hydrolysis) provided as a lyophilized powder. Required for G-actin stability and F-actin assembly and dynamics.

For product Datasheets and MSDSs please click on the PDF links below.   For additional information, click on the FAQs tab above or contact our Technical Support department at

Xiao et al., 2013. c-Yes regulates cell adhesion at the apical ectoplasmic specialization-blood-testis barrier axis via its effects on protein recruitment and distribution. Am. J. Physiol. Endocrinol. Metab. 304, E145-E159. 

Butler et al., 2012. Inhibitory effects of pectenotoxins from marine algae on the polymerization of various actin isoforms. Toxicol. In Vitro. 26, 493-499.

Jiwani et al., 2012. Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerization. Biochem. Biophys. Res. Commun. 420, 816-821.

Fan et al., 2012. A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lens. FEBS. J. 279, 2892-2904.

Tsai et al., 2011. 7-Chloro-6-piperidin-1-yl-quinoline-5,8-dione (PT-262), a novel ROCK inhibitor blocks cytoskeleton function and cell migration. Biochem. Pharmacol. 81, 856-865.

Trigili et al., 2011. Mechanism of Action of the Cytotoxic Macrolides Amphidinolide X and J. ChemBioChem. 12, 1027-1030.

Takamiya et al., 2005. Overexpression of mutated Cu,Zn-SOD in neuroblastoma cells results in cytoskeletal change. Am. J. Physiol. 288, C253-C259.

Kumar et al., 2004. Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin. J. Biol. Chem. 279, 45036-45046.

Fontao et al., 2001. The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. Cell Sci. 114, 2065-2076.

Zhai et al., 2001. Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton. J. Biol. Chem . 276, 36163-36167.

Blader et al., 1999. GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Mol. Biol. Cell. 10, 581-596.


Question 1: Can the reconstituted ATP be stored at 4°C for any length of time or does it need to be immediately snap-frozen?

Answer 1:  The ATP (Cat. # BSA04) should be reconstituted to 100 mM with 1 ml of cold 100 mM Tris, pH 7.5.  Set aside the volume that is needed for the day’s experiment (stable for 4 h on ice) and the remaining ATP should then be aliquoted into experiment-sized amounts, snap frozen in liquid nitrogen, and stored at or below -20°C. These stocks are stable for 6 months at -20°C.


Question 2: How long are solutions with ATP in them stable at 4°C if performing actin polymerization experiments?

Answer 2: Buffers containing ATP (Cat. # BSA04) will be stable for 4 h on ice.  Keep on ice until ready to use.  After 4 h discard the tube, do not re-freeze to use later.  Prepare fresh buffers (or freshly frozen aliquot) for the next experiment.



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