Sodium Acetate Buffer Solution for Molecular Biology

Product No. S7899

CAS RN 126-96-5

Product Description

This product is designated as Molecular Biology grade. It is suitable for DNA precipitation and has been analyzed for the presence of nucleases. The Certificate of Analysis provides specific information on the concentration and pH of the product.

Sodium acetate is a widely used reagent in molecular biology applications. It is used as a buffer in conjunction with acetic acid, in the buffering range of pH 3.6 - 5.6.

Sodium acetate is used in the purification and precipitation of

• Nucleic acids,^1,2,3
• Protein crystallization,⁴
• Staining of gels in protein gel electrophoresis,⁵
• and, HPLC.⁶

Large scale applications of sodium acetate include its use as a retardant in plastics manufacturing, as a mordant in dyeing, and in the tanning of leather.⁷

Also,

• A DNA microarray study reported that E. coli response to different levels of sodium acetate.⁸
• A protein unfolding investigation. During reversed-phase chromatography in the presence of varying salts. It included sodium acetate, at different ionic strengths.⁹
• Sodium acetate has been used in conjunction with sodium carbonate to enhance the activation of freeze-dried subtilisin Carlsberg in organic solvents.¹⁰
• Sodium acetate may be used as a substrate for acetokinase (acetate kinase).¹¹

Storage

Room Temperature

Components

This product is a 3 M solution. It is prepared with 18 megaohm water, and is 0.2 µM filtered. This product has a pH of 5.2 ± 0.1 at 25 °C.

Precautions and Disclaimer

This product is for R&D use only, not for drug, household, or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices.

References

1. Evans JK, Troilo P, Ledwith BJ. 1998. Simultaneous Purification of RNA and DNA from Liver Using Sodium Acetate Precipitation. BioTechniques. 24(3):416-418. https://doi.org/10.2144/98243bm18

2. Sambrook J. 2001. Molecular Cloning: A Laboratory Manual. 3. Cold Spring Harbor Laboratory Press.

3. Wallace DM. 1987. [4] Large- and small-scale phenol extractions.33-41. https://doi.org/10.1016/0076-6879(87)52007-9

4. Baniecki ML, McGrath WJ, Dauter Z, Mangel WF. 2002. Adenovirus proteinase: crystallization and preliminary X-ray diffraction studies to atomic resolution. Acta Crystallogr D Biol Cryst. 58(9):1462-1464. https://doi.org/10.1107/s0907444902008429

5. Bjellqvist B, Pasquali C, Ravier F, Sanchez J, Hochstrasser D. 1993. A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale. Electrophoresis. 14(1):1357-1365. https://doi.org/10.1002/elps.11501401209

6. Clark T, White CA, Chu CK, Bartlett MG. 2001. Determination of 3?-azido-2?,3?-dideoxyuridine in maternal plasma, amniotic fluid, fetal and placental tissues by high-performance liquid chromatography. Journal of Chromatography B: Biomedical Sciences and Applications. 755(1-2):165-172. https://doi.org/10.1016/s0378-4347(01)00054-8

7. The Merck Index, 12th ed., Entry# 8711..

8. Polen T, Rittmann D, Wendisch VF, Sahm H. 2003. DNA Microarray Analyses of the Long-Term Adaptive Response of Escherichia coli to Acetate and Propionate. AEM. 69(3):1759-1774. https://doi.org/10.1128/aem.69.3.1759-1774.2003

9. McNay JLM, O'Connell JP, Fernandez EJ. 2001. Protein unfolding during reversed-phase chromatography: II. Role of salt type and ionic strength. Biotechnol. Bioeng.. 76(3):233-240. https://doi.org/10.1002/bit.10016

10. Ru MT, Wu KC, Lindsay JP, Dordick JS, Reimer JA, Clark DS. 2001. Towards more active biocatalysts in organic media: Increasing the activity of salt-activated enzymes. Biotechnol. Bioeng.. 75(2):187-196. https://doi.org/10.1002/bit.1178

11. Rose IA. 1955. [97] Acetate kinase of bacteria (acetokinase).591-595. https://doi.org/10.1016/0076-6879(55)01102-6