ACES (buffer)

ACES
Names
Preferred IUPAC name
2-[(2-Amino-2-oxoethyl)amino]ethane-1-sulfonic acid
Other names
N-(2-Acetamido)-2-aminoethanesulfonic acid
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
ECHA InfoCard 100.028.099 Edit this at Wikidata
UNII
  • InChI=1S/C4H10N2O4S/c5-4(7)3-6-1-2-11(8,9)10/h6H,1-3H2,(H2,5,7)(H,8,9,10) checkY
    Key: DBXNUXBLKRLWFA-UHFFFAOYSA-N checkY
  • InChI=1/C4H10N2O4S/c5-4(7)3-6-1-2-11(8,9)10/h6H,1-3H2,(H2,5,7)(H,8,9,10)
    Key: DBXNUXBLKRLWFA-UHFFFAOYAH
  • C(CS(=O)(=O)O)NCC(=O)N
  • O=S(=O)(O)CCNCC(=O)N
Properties
C4H10N2O4S
Molar mass 182.199
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
☒N verify (what is checkY☒N ?)

ACES (N-(2-acetamido)-2-aminoethanesulfonic acid) is a chemical compound that is one of Good's buffers. It was developed in the 1960s to provide buffer solutions with pH ranging from 6.15-8.35 for use in various applications. With a pKa of 6.9, it is often used as a buffering agent in biological and biochemical research. It is a zwitterionic buffer with a useful buffering range of 6.1-7.5. The pioneering publication by Good and his co-workers described the synthesis and physical properties of ACES buffer.[1]

Applications

ACES had been used to develop buffers for both agarose and polyacrylamide gel electrophoresis.[2] ACES use in isoelectric focusing of proteins has also been documented.[3] Use of ACES has been published in a protocol for the analysis of bacterial autolysins in a discontinuous SDS-PAGE system.[4] Potential inhibition of ACES and other Good buffers has been investigated in γ-aminobutyric acid receptor binding to rat brain synaptic membranes.[5]

References

  1. ^ Good, N.E., "Hydrogen ion buffers for biological research." "Biochemistry", 5(2), 467–477.
  2. ^ Liu, Q., et al., "pK-matched running buffers for gel electrophoresis." "Anal. Biochemistry.", 270(1):112-122.
  3. ^ Alonso, A., "Human α-1-antitrypsin subtyping by hybrid isoelectric focusing in miniaturized polyacrylamide gel." "Electrophoresis", 9(2):65-73.
  4. ^ Strating, H., and Clarke, A.J., "Differentiation of bacterial autolysins by zymogram analysis." "Anal. Biochem.", 291(1):149-154.
  5. ^ Tunnicliff, G., and Smith, J.A., "Competitive inhibition of γ-aminobutyric acid receptor binding by N-2-hydroxyethylpiperazine-N'-2-ε-ethanesulfonic acid and related buffer." "J. Neurochem.", 36(3):1122-1126.

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