|Calculated MW||28.3 kDa (246 aa, 1-222 aa + His Tag)|
|Other Names||Glutathione S-transferase alpha 4, GSTA4-4, GTA4|
|Results||Specific activity > 0.9 units/mg|
|Sequence||MGSSHHHHHH SSGLVPRGSH MGSHMAARPK LHYPNGRGRM ESVRWVLAAA GVEFDEEFLE TKEQLYKLQD GNHLLFQQVP MVEIDGMKLV QTRSILHYIA DKHNLFGKNL KERTLIDMYV EGTLDLLELL IMHPFLKPDD QQKEVVNMAQ KAIIRYFPVF EKILRGHGQS FLVGNQLSLA DVILLQTILA LEEKIPNILS AFPFLQEYTV KLSNIPTIKR FLEPGSKKKP PPDEIYVRTV YNIFRP|
|Storage||-20°C; 1 mg/ml solution 20 mM Tris-HCl buffer, pH 8.0, 20% glycerol, 2 mM DTT and 100 mM NaCl.|
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Provided below are standard protocols that you may find useful for product applications.
GSTA4, also known as glutathione S-transferase A4, belongs to the GST superfamily. This enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows very high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is highly effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, an important product of peroxidative degradation of arachidonic acid and a commonly used biomarker for oxidative damage in tissue. This enzyme is expressed at a high level in brain, placenta, and skeletal muscle and much lower in lung and liver. Recombinant human GSTA4 protein, fused to His-tag at N-terminus, was expressed in E.Coli and purified by using conventional chromatography techniques.
Hubatsch I.,et al.Biochem. J. 330:175-179(1998).
Board P.G.,et al.Biochem. J. 330:827-831(1998).
Liu S.,et al.Arch. Biochem. Biophys. 352:306-313(1998).
Piper J.T.,et al.Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
Desmots F.,et al.Biochem. J. 336:437-442(1998).
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