ACES (buffer)

ACES
Names
	IUPAC name 2-(carbamoylmethylamino)ethanesulfonic acid
	Other names N-(2-Acetamido)-2-aminoethanesulfonic acid
Identifiers
CAS Number	7365-82-4 ;
3D model (JSmol)	Interactive image; Interactive image;
ChEBI	CHEBI:39062 ;
ChemSpider	73843 ;
ECHA InfoCard	100.028.099
PubChem CID	81832;
UNII	I5SPL5YVBY ;
CompTox Dashboard (EPA)	DTXSID8064644 ;
	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

Good, N.E., "Hydrogen ion buffers for biological research." "Biochemistry", 5(2), 467-477.
Liu, Q., et al., "pK-matched running buffers for gel electrophoresis." "Anal. Biochemistry.", 270(1):112-122.
Alonso, A., "Human α-1-antitrypsin subtyping by hybrid isoelectric focusing in miniaturized polyacrylamide gel." "Electrophoresis", 9(2):65-73.
Strating, H., and Clarke, A.J., "Differentiation of bacterial autolysins by zymogram analysis." "Anal. Biochem.", 291(1):149-154.
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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[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.