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

Recombinant Human Kynurenine--oxoglutarate transaminase 1 (KYAT1)

Cat. Num. AAA1459467

• Gene Names: CCBL1; GTK; KAT1; KATI
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Kynurenine--oxoglutarate transaminase 1 (KYAT1); 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
• Protein Family: Kynurenine--oxoglutarate transaminase
• UniProt Gene Name: CCBL1
• UniProt Synonym Gene Names: GTK; KATI
• UniProt Entry Name: KAT1_HUMAN

NCBI Description

This gene encodes a cytosolic enzyme that is responsible for the metabolism of cysteine conjugates of certain halogenated alkenes and alkanes. This metabolism can form reactive metabolites leading to nephrotoxicity and neurotoxicity. Increased levels of this enzyme have been linked to schizophrenia. Multiple transcript variants that encode different isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

CCBL1: 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. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 2.6.1.64; Lyase; Transferase; EC 2.6.1.7; EC 4.4.1.13

Chromosomal Location of Human Ortholog: 9q34.11

Cellular Component: cytoplasm; cytosol; nucleoplasm

Molecular Function: cysteine-S-conjugate beta-lyase activity; glutamine-phenylpyruvate transaminase activity; glutamine-pyruvate transaminase activity; kynurenine-oxoglutarate transaminase activity; phenylalanine(histidine) transaminase activity; protein binding; protein homodimerization activity; pyridoxal phosphate binding; transaminase activity

Biological Process: amino acid biosynthetic process; amino acid derivative metabolic process; L-phenylalanine catabolic process; tryptophan catabolic process