GOT1, human recombinant protein
Glutamic-oxaloacetic transaminase 1, Aspartate aminotransferase 1, Transaminase A, GIG18
|Calculated MW||48.4 kDa (433 aa, 1-413 aa + His Tag)|
|Other Names||Glutamic-oxaloacetic transaminase 1, Aspartate aminotransferase 1, Transaminase A, GIG18|
|Results||Specific activity is > 13 unit/mg|
|Sequence||MGSSHHHHHH SSGLVPRGSH MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ|
|Storage||-20°C; 0.5 mg/ml solution 20 mM Tris-HCl buffer (pH 8.0), 20% glycerol, 100 mM NaCl and 1 mM DTT.|
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Provided below are standard protocols that you may find useful for product applications.
Glutamic-oxaloacetic transaminase (GOT) is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology. Recombinant human GOT1, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Bousquet-Lemercier B.,et al.Biochemistry 29:5293-5299(1990).
Wang C.Y.,et al.Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
Yu W.,et al.Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Deloukas P.,et al.Nature 429:375-381(2004).
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