Product Uses Include
• Resuspension of actin protein
• Dilution and storage of G-actin protein
This buffer contains 5 mM Tris-HCl pH 8.0 and 0.2 mM CaCl2. Used as a general G-actin (monomer) buffer with the addition of 0.2 mM ATP (see Cat. # BSA04) and 0.5 mM DTT (A-buffer). The buffer can be changed to a general F-actin (filament supporting) buffer by the addition of 1/10th volume of actin polymerization buffer (see Cat. # BSA02).
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.
|Park, Jin Suk et al.||Mechanical regulation of glycolysis via cytoskeleton architecture||Nature||2020||ISSN 1476-4687|
|Limatola, Nunzia et al.||Nicotine Induces Polyspermy in Sea Urchin Eggs through a Non-Cholinergic Pathway Modulating Actin Dynamics||Cells||2019||ISSN 2073-4409|
|Laitila, Jenni et al.||A nebulin super-repeat panel reveals stronger actin binding toward the ends of the super-repeat region||Muscle and Nerve||2019||ISSN 1097-4598|
|Da’as, Sahar I. et al.||Hypertrophic cardiomyopathy-linked variants of cardiac myosin-binding protein C3 display altered molecular properties and actin interaction||Biochemical Journal||2018||ISSN 1470-8728|
|Patel, Vaibhav B. et al.||PI3Kα-regulated gelsolin activity is a critical determinant of cardiac cytoskeletal remodeling and heart disease||Nature Communications||2018||ISSN 2041-1723|
|Goryunov, D et al.||Microtubule-actin cross-linking factor 1: domains, interaction partners, and tissue-specific functions||Methods in Enzymology||2016||Article Link|
|Reeg, Sandra et al.||The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome||Free Radical Biology and Medicine||2016||ISSN 1873-4596|
|Wang, Y et al.||Fluorescence imaging with one-nanometer accuracy (FIONA)||JoVE (Journal of …||2014||Article Link|
|Metcalf, Daniel J. et al.||Test samples for optimizing storm super-resolution microscopy||Journal of Visualized Experiments||2013||ISSN 1940-087X|
|Xiao, Xiang et al.||c-Yes regulates cell adhesion at the apical ectoplasmic specialization-blood-testis barrier axis via its effects on protein recruitment and distribution||American Journal of Physiology - Endocrinology and Metabolism||2013||ISSN 1522-1555|
|Butler, Suzanne C. et al.||Inhibitory effects of pectenotoxins from marine algae on the polymerization of various actin isoforms||Toxicology in vitro : an international journal published in association with BIBRA||2012||ISSN 1879--3177|
|Fan, Jianguo et al.||A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lens||The FEBS journal||2012||ISSN 1742-464X|
|Jiwani, Shahanawaz et al.||Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerization||Biochemical and biophysical research communications||2012||ISSN 1090--2104|
|Trigili, Chiara et al.||Mechanism of Action of the Cytotoxic Macrolides Amphidinolide X and J||ChemBioChem||2011||ISSN 1439--7633|
|Tsai, Chih Chien et al.||7-Chloro-6-piperidin-1-yl-quinoline-5,8-dione (PT-262), a novel ROCK inhibitor blocks cytoskeleton function and cell migration||Biochemical pharmacology||2011||ISSN 1873--2968|
|Cheng, Chao Min et al.||Creating cellular and molecular patterns via gravitational force with liquid droplets||Applied Physics Letters||2008||ISSN 0003-6951|
|Takamiya, Rina et al.||Overexpression of mutated Cu,Zn-SOD in neuroblastoma cells results in cytoskeletal change||American journal of physiology. Cell physiology||2005||ISSN 0363--6143|
|Kumar, Narendra et al.||Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin||The Journal of biological chemistry||2004||ISSN 0021--9258|
|Goryunov, Dmitry et al.||Studying cytolinker proteins||Methods in Cell Biology||2004||ISSN 0091-679X|
|Fontao, Lionel et al.||The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin||Journal of cell science||2001||ISSN 0021--9533|
|Zhai, Liwei et al.||Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton||The Journal of biological chemistry||2001||ISSN 0021--9258|
|Blader, Ira J. et al.||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||Molecular Biology of the Cell||1999||ISSN 1059-1524|
Question 1: Can the general actin buffer be stored with ATP added or should it be added fresh?
Answer 1: On the day of the experiment, the general actin buffer (Cat. # BSA01) should be supplemented with 0.2 mM ATP (Cat. # BSA04) to create an optimal actin monomer buffer. We do not recommend storing the actin buffer with ATP in it. Prepare the actin buffer + ATP in a volume that is needed for the experiment. Calcium ions and ATP are required for actin conformation. In addition, ATP is hydrolysed during actin polymerization and is required for the polymerization process.
Question 2: What is the composition of Cytoskeleton’s general actin buffer?
Answer 2: Upon resuspension in 100 ml of sterile de-ionized water, the buffer (Cat. # BSA01) will be at 1X strength buffer and contain: 0.2 mM calcium chloride and 5 mM Tris-HCl, pH 8.0.
If you have any questions concerning this product, please contact our Technical Service department at email@example.com