epitope corresponding to amino acids 255-328 mapping near the C-terminus of KAT I of human origin
Modification Notes
Kynurenine aminotransferases KAT I, KAT II, and KAT III belong to the class-I pyridoxal-phosphate-dependent aminotransferase family. KAT I is a cytoplasmic protein involved in glutamine catabolism. KAT I functions in the catalysis of the transamination of L-kinurenine to form kynurenic acid, a neuroprotective and anticonvulsant metabolite of tryptophan. Kynurenic acid is involved in synaptic transmission and has been implicated in a number of neurological disorders including schizophrenia and Huntington’s disease. KAT I also functions in the metabolism of cysteine conjugates in some halogenated alkenes and alkanes to form reactive metabolites. KAT I has three isoforms. Isoform 1is the full length protein, isoform 2 lacks amino acids 68-117 and isoform 3 lacks amino acids 251-422. Based on sequence similarity, KAT I is thought to function as a homodimer.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of KAT I isoforms 1 and 2 of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA also reactive with additional species, including canine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 255-328 mapping near the C-terminus of KAT I of human origin
Tissue Specificity
epitope corresponding to amino acids 255-328 mapping near the C-terminus of KAT I of human origin
Western blot analysis of KAT I expression in HeLa whole cell lysate.
Application Notes
recommended for detection of KAT I isoforms 1 and 2 of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA also reactive with additional species, including canine:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.