ACES (buffer)

ACES (buffer)

Names
IUPAC name 2-(carbamoylmethylamino)ethanesulfonic acid
Other names N-(2-Acetamido)-2-aminoethanesulfonic acid
Identifiers
CAS Number	7365-82-4
ChEBI	CHEBI:39062
ChemSpider	73843
Jmol interactive 3D	Image Image
PubChem	81832
InChI InChI=1S/C4H10N2O4S/c5-4(7)3-6-1-2-11(8,9)10/h6H,1-3H2,(H2,5,7)(H,8,9,10) Key: DBXNUXBLKRLWFA-UHFFFAOYSA-N 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
SMILES C(CS(=O)(=O)O)NCC(=O)N O=S(=O)(O)CCNCC(=O)N
Properties
Chemical formula	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).
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Infobox references

ACES is the common abbreviation for the compound N-(2-Acetamido)-2-aminoethanesulfonic acid.

ACES is one of Good's buffers developed in the 1960s to provide buffers with pH ranging from 6.15-8.35 for use in various applications. With a pK_a 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.