1,N6-Etheno-adenosine-5'-triphosphate, Sodium salt
For research use only!
Shipping: shipped on blue ice
Storage Conditions: store at -20 °C
Short term exposure (up to 1 week cumulative) to ambient temperature possible.
Shelf Life: 12 months after date of delivery
Molecular Formula: C12H16N5O13P3 (free acid)
Molecular Weight: 531.20 g/mol (free acid)
Purity: ≥ 95 % (HPLC)
Form: clear aqueous solution
Concentration: 10 mM - 11 mM
pH: 7.5 ±0.5
Spectroscopic Properties: λmax 275 nm, ε 6.0 L mmol-1 cm-1 (Tris-HCl pH 7.5), λexc 300 nm, λem 415 nm
Exchange rate from G-actin and wild type
FRET-studies on conformational changes
Formation in erythrocytes andendothelial cells
Fluorescence anisotropy changes during protein binding
Influence on centromeric binding protein E associated activity
Yeast and muscle actins
Coflin and profilin
P2Y receptor in cardiac endothelial cells
Please click the black arrow on the right to expand the citation list. Click publication title for the full text.
 Saratovskikh et al. (2010) Kinetic of transport of technogenic oxicants through model membranes. J. Environmental Protection 1:410.
 McKane et al. (2006) Effect of the substitution of muscle actin-specific subdomain 1 and 2 residues in yeast actin and actin function. J. Biol. Chem. 281:29916.
 Dedova et al. (2006) Thymosin β4 induces a conformational change in actin monomers. Biophysical J. 90:985.
 Mattig et al. (2003) Modulation of adenine nucleotide concentrations in human plasma by erythrocytes and endothelial cells. Thrombosis Res. 110:195.
 Suarez et al. (202) Biochemical defects in retina-specific human ATP binding cassette transporter nucleotide binding domain 1 mutants associated with macular degeneration. J. Biol. Chem. 277:21759.
 Thrower et al. (1995) Mitotic HeLa cells contain a CENP-E associated minus end-directed microtubule motor. EMBO Journal 14:918.
 Wen et al. (2008) Control of the ability of profilin to bind and facilitate nucleotide exchange from G-actin. J. Biol. Chem. 283:9444.
 Kardos et al. (2009) The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin. Biophysical J. 96:2335.
 Yang et al. (1994) Purinergic axis in cardiac blood vessels: Agonist mediated release of ATP from cardiac endothelial cells. Circ. Res. 74 (3):401.
Singh et al. (2011) Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite. J. Biol. Chem. 286 (32): 28256.
Aguilar et al. (2001) Ectoenzymatic breakdown of diadenosine polyphosphates by Xenopus laevis oocytes. Eur. J. Biochem. 268 (5):1289.
Churchich et al. (2000) A catalytic site of protein disulfide isomerase probed with adenosine-5 '-triphosphate analogs. BBA-Protein Struct. M. 1479 (1):293.
Gualix et al. (1999) Studies of chromaffin granule functioning by flow cytometry: Transport of fluorescent epsilon-ATP and granular size increase induced by ATP. Receptor Channel 6 (6):449.
Franksskiba et al. (1994) Quenching of fluorescent nucleotides bound to myosin - a probe of the active-site conformation. Biochemistry-US 33 (42):12720.
Miki et al. (1994) Domain motion in actin observed by fluorescence resonance energy-transfer. Biochemistry-US 33 (33):10171.
Root et al. (1992) The accessibility of ethenonucleotides to collisional quenchers and the nucleotide cleft in G-Actin and F-Actin. Protein Sci. 1 (8):1014.
Conner et al. (1989) Sister chromatid exchange induced by etheno-ATP derivatives invitro. Cancer Res. 49 (14):3839.
Wang et al. (1981) Exchange of 1, N (6)-etheno-ATP with Actin-bound nucleotides as a tool for studying the steady-state exchange of subunits in F-Actin solutions. P. Natl. Acad. Sci.-Biol. 78 (9):5503.
Yanagida (1981) Angles of nucleotides bound to cross-bridges in glycerinated muscle-fiber at various concentrations of epsilon-ATP, epsilon-ADP and epsilon-AMPPNP detected by polarized fluorescence. J. Mol. Biol. 146 (4):539.
Burtnick et al. (1979) Circular-polarization of the fluorescence of Actin-bound epsilon-ATP - effects of binding DNAse-I. FEBS Lett. 97 (1):166.
Kaplan et al. (1976) Mitochondrial ATPase activity and adenine-nucleotide transport with epsilon-ATP. J. Cell Biol. 70 (2):a414.
Hohne et al. (1975) New principle for activity measurement of ADP or ATP dependent enzymes - fluorescence quenching of epsilon-ADP and epsilon-ATP by divalent metal-ions. Anal. Biochem. 69 (2):607.