General actin buffer: 1x stock

General actin buffer: 1x stock
$0.00

Product Uses Include

•  Resuspension of actin protein
•  Dilution and storage of G-actin protein

Material
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).

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 tservice@cytoskeleton.com

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.

AuthorTitleJournalYearArticle Link
Park, Jin Suk et al.Mechanical regulation of glycolysis via cytoskeleton architectureNature2020ISSN 1476-4687
Limatola, Nunzia et al.Nicotine Induces Polyspermy in Sea Urchin Eggs through a Non-Cholinergic Pathway Modulating Actin DynamicsCells2019ISSN 2073-4409
Laitila, Jenni et al.A nebulin super-repeat panel reveals stronger actin binding toward the ends of the super-repeat regionMuscle and Nerve2019ISSN 1097-4598
Da’as, Sahar I. et al.Hypertrophic cardiomyopathy-linked variants of cardiac myosin-binding protein C3 display altered molecular properties and actin interactionBiochemical Journal2018ISSN 1470-8728
Patel, Vaibhav B. et al.PI3Kα-regulated gelsolin activity is a critical determinant of cardiac cytoskeletal remodeling and heart diseaseNature Communications2018ISSN 2041-1723
Goryunov, D et al.Microtubule-actin cross-linking factor 1: domains, interaction partners, and tissue-specific functionsMethods in Enzymology2016Article Link
Reeg, Sandra et al.The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasomeFree Radical Biology and Medicine2016ISSN 1873-4596
Wang, Y et al.Fluorescence imaging with one-nanometer accuracy (FIONA)JoVE (Journal of …2014Article Link
Metcalf, Daniel J. et al.Test samples for optimizing storm super-resolution microscopyJournal of Visualized Experiments2013ISSN 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 distributionAmerican Journal of Physiology - Endocrinology and Metabolism2013ISSN 1522-1555
Butler, Suzanne C. et al.Inhibitory effects of pectenotoxins from marine algae on the polymerization of various actin isoformsToxicology in vitro : an international journal published in association with BIBRA2012ISSN 1879--3177
Fan, Jianguo et al.A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lensThe FEBS journal2012ISSN 1742-464X
Jiwani, Shahanawaz et al.Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerizationBiochemical and biophysical research communications2012ISSN 1090--2104
Trigili, Chiara et al.Mechanism of Action of the Cytotoxic Macrolides Amphidinolide X and JChemBioChem2011ISSN 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 migrationBiochemical pharmacology2011ISSN 1873--2968
Cheng, Chao Min et al.Creating cellular and molecular patterns via gravitational force with liquid dropletsApplied Physics Letters2008ISSN 0003-6951
Takamiya, Rina et al.Overexpression of mutated Cu,Zn-SOD in neuroblastoma cells results in cytoskeletal changeAmerican journal of physiology. Cell physiology2005ISSN 0363--6143
Kumar, Narendra et al.Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villinThe Journal of biological chemistry2004ISSN 0021--9258
Goryunov, Dmitry et al.Studying cytolinker proteinsMethods in Cell Biology2004ISSN 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 plectinJournal of cell science2001ISSN 0021--9533
Zhai, Liwei et al.Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeletonThe Journal of biological chemistry2001ISSN 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 vitroMolecular Biology of the Cell1999ISSN 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 tservice@cytoskeleton.com