Kynurenine--oxoglutarate transaminase 1 (KYAT1), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 1-372aa. Protein Length: Full Length of Isoform 2. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: MAKQLQARRL DGIDYNPWVE FVKLASEHDV VNLGQGFPDF PPPDFAVEAF QHAVSGDFML NQYTKTFVII IEPFFDCYEP MTMMAGGRPV FVSLKPGPIQ NGELGSSSNW QLDPMELAGK FTSRTKALVL NTPNNPLGKV FSREELELVA SLCQQHDVVC ITDEVYQWMV YDGHQHISIA SLPGMWERTL TIGSAGKTFS ATGWKVGWVL GPDHIMKHLR TVHQNSVFHC PTQSQAAVAE SFEREQLLFR QPSSYFVQFP QAMQRCRDHM IRSLQSVGLK PIIPQGSYFL ITDISDFKRK MPDLPGAVDE PYDRRFVKWM IKNKGLVAIP VSIFYSVPHQ KHFDHYIRFC FVKDEATLQA MDEKLRKWKV EL. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: 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. Reference: 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). Function: 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.