|Calculated MW||29.1 kDa (249 aa, 1-225 aa)|
|Other Names||Glutathione S-transferase mu 3, GST5, GSTB, GSTM3-3, GTM3|
|Results||Specific activity > 4.7 units/mg|
|Sequence||MGSSHHHHHH SSGLVPRGSH MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC|
|Storage||-20°C; 1 mg/ml solution 20 mM Tris-HCl buffer, pH 8.0, 10% glycerol, 1 mM DTT and 100 mM NaCl.|
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Provided below are standard protocols that you may find useful for product applications.
Glutathione S-transferase mu 3, also known as GSTM3, is member of the glutathione s-transferase (GST) family of proteins. There are eight families of GST proteins, namely alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have a variety of functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. Recombinant human GSTM3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Campbell E.,et al.J. Biol. Chem. 265:9188-9193(1990).
Patskovsky Y.V.,et al.Arch. Biochem. Biophys. 361:85-93(1999).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Ross V.L.,et al.Biochem. J. 294:373-380(1993).
Hussey A.J.,et al.Biochim. Biophys. Acta 1203:131-141(1993).
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