Kynurenine--oxoglutarate transaminase 1 (KYAT1) Recombinant Protein | KYAT1 recombinant protein

Recombinant Human Kynurenine--oxoglutarate transaminase 1 (KYAT1)

Cat. Num. AAA117594

• Gene Names: CCBL1; GTK; KAT1; KATI
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Kynurenine--oxoglutarate transaminase 1 (KYAT1); N/A; Recombinant Human Kynurenine--oxoglutarate transaminase 1 (KYAT1); Cysteine-S-conjugate beta-lyase (EC:4.4.1.13); Glutamine transaminase K; GTK; Glutamine-phenylpyruvate transaminase (EC:2.6.1.64); Kynurenine aminotransferase I; KATI; Kynurenine-oxoglutarate transaminase I; KYAT1 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-372. Full Length of Isoform 2
• Sequence: MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFMLNQYTKTFVIIIEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVLNTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTLTIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFRQPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDEPYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKVEL

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for KYAT1 recombinant protein

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.

Product Categories/Family for KYAT1 recombinant protein

Metabolism

References

Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase.Perry S., Harries H., Scholfield C., Lock E., King L., Gibson G., Goldfarb P.FEBS Lett. 360:277-280(1995) DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004) Crystal structure of human kynurenine aminotransferase I.Rossi F., Han Q., Li J., Li J., Rizzi M.J. Biol. Chem. 279:50214-50220(2004) Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K.Han Q., Robinson H., Cai T., Tagle D.A., Li J.J. Med. Chem. 52:2786-2793(2009)

NCBI and Uniprot Product Information

• NCBI GI #: 169881279
• NCBI GeneID: 883
• NCBI Accession #: NP_001116143.1
• NCBI GenBank Nucleotide #: NM_001122671.1
• UniProt Accession #: Q16773; Q5T275; Q8N191
• Molecular Weight: 58.6 kDa
• NCBI Official Full Name: kynurenine--oxoglutarate transaminase 1 isoform a
• NCBI Official Synonym Full Names: cysteine conjugate-beta lyase, cytoplasmic
• NCBI Official Symbol: CCBL1
• NCBI Official Synonym Symbols: GTK; KAT1; KATI
• NCBI Protein Information: kynurenine--oxoglutarate transaminase 1
• UniProt Protein Name: Kynurenine--oxoglutarate transaminase 1
• UniProt Gene Name: CCBL1
• UniProt Synonym Gene Names: GTK; KATI
• UniProt Entry Name: KAT1_HUMAN