Recombinant Human CCBL1 protein is a Human Full Length protein, in the 1 to 442 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others (PubMed:19338303, PubMed:28097769). Also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites (PubMed:7883047). 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 (PubMed:7883047).
CCBL1, KYAT1, Kynurenine--oxoglutarate transaminase 1, Cysteine-S-conjugate beta-lyase, Glutamine transaminase K, Glutamine--phenylpyruvate transaminase, Kynurenine aminotransferase 1, Kynurenine aminotransferase I, Kynurenine--oxoglutarate transaminase I, GTK, KATI
Recombinant Human CCBL1 protein is a Human Full Length protein, in the 1 to 442 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 7.4
Constituents: 89% PBS, 10% Glycerol (glycerin, glycerine), 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab202192 was purified using conventional chromatography techniques.
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others (PubMed:19338303, PubMed:28097769). Also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites (PubMed:7883047). 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 (PubMed:7883047).
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
CCBL1 also known as kynurenine aminotransferase I is an enzyme with a mass of approximately 47 kDa. This enzyme catalyzes the conversion of kynurenine to kynurenic acid participating in the metabolism of tryptophan. It is primarily expressed in the liver kidney and brain reflecting its involvement in various metabolic processes. CCBL1 features key residues in its active site important for substrate binding and enzyme function.
CCBL1 plays a significant role in the immune system and central nervous system. It converts kynurenine into kynurenic acid a notable neuroprotective agent. CCBL1 is part of the larger kynurenine pathway acting as a biochemical hub that regulates the levels of neuroactive metabolites. Its activity affects the concentration of molecules influencing neurotransmission and neuroinflammation.
Enzymes like CCBL1 help regulate the kynurenine pathway which intersects with other metabolic routes. This enzyme also influences the tryptophan catabolism pathway impacting serotonin synthesis and broader neurological functions. CCBL1 interacts with proteins like indoleamine 23-dioxygenase (IDO) which initiates the kynurenine pathway highlighting an interconnected network of enzymes and metabolites.
Enzyme dysregulation often relates to neurological disorders and immune dysfunction. Altered CCBL1 activity has been linked to neurodegenerative diseases such as Alzheimer's disease potentially due to shifts in neuroactive metabolite levels. Through its interaction with IDO CCBL1 affects immune response which may have implications in diseases like multiple sclerosis where neuroinflammation plays a role.
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15% SDS-PAGE analysis of ab202192 (3 μg).
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