Synthetic peptide directed towards the C terminal region of human HAL
Application
Anti-HAL antibody produced in rabbit is suitable for western blotting at a concentration of 1.25μg/ml and for immunohistochemistry of paraffin-embedded tissue sections at a concentration of 4-8μg/ml.
Biochem/physiol Actions
Histidine ammonia-lyase (HAL) is a cytosolic enzyme important in histidine catabolism. It catalyzes the nonoxidative deamination of L-histidine to trans-urocanic acid. Defective HAL activity results in accumulation of histidine and histamine in body fluids, a condition termed as hisdinemia.
Sequence
Synthetic peptide located within the following region: EAAHRLLLEQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLQFLHKKSTK
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
European journal of biochemistry, 269(6), 1790-1797 (2002-03-16)
Histidine ammonia-lyase (EC 4.3.1.3) catalyzes the nonoxidative elimination of the alpha-amino group of histidine using a 4-methylidene-imidazole-5-one (MIO), which is formed autocatalytically from the internal peptide segment 142Ala-Ser-Gly. The structure of the enzyme inhibited by a reaction with l-cysteine was
Histidinemia (MIM235800) is characterized by elevated histidine in body fluids and decreased urocanic acid in blood and skin and results from histidase (histidine ammonia lyase, EC 4.3.1.3) deficiency. It is the most frequent inborn metabolic error in Japan. Although the
Histidase (EC 4.3.1.3) is a cytosolic enzyme that catalyzes the nonoxidative deamination of histidine to urocanic acid. Histidinemia, resulting from reduced histidase activity as reported in Cambridge stock his/his mice and in humans, is the most frequent inborn metabolic error
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