Synthetic peptide directed towards the N terminal region of human ATIC
Application
Anti-ATIC (AB2) antibody produced in rabbit is suitable for western blotting at a concentration of 1.25μg/ml.
Biochem/physiol Actions
ATIC gene encodes a bifunctional enzyme 5-Amino-4-imidazolecarboxamide ribonucleotide transformylase/IMP cyclohydrolase. The enzyme is responsible for catalysis of the last two steps in the de novo synthesis of inosine 5′-monophosphate. The N-terminal domain comprise of phosphoribosylaminoimidazolecarboxamide formyltransferase activity whereas the C-terminal domain has IMP cyclohydrolase activity. Mutation in ATIC gene results in destabilization of various degrees of purinosome assembly which leads to AICA-ribosiduria.
Sequence
Synthetic peptide located within the following region: YVVVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKG
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.
The Journal of biological chemistry, 277(25), 22168-22174 (2002-04-12)
5-Amino-4-imidazolecarboxamide ribonucleotide transformylase/IMP cyclohydrolase (ATIC) is a bifunctional protein possessing two enzymatic activities that sequentially catalyze the last two steps in the pathway for de novo synthesis of inosine 5'-monophosphate. This bifunctional enzyme is of particular interest because of its
Human molecular genetics, 21(7), 1534-1543 (2011-12-20)
The purinosome is a multienzyme complex composed by the enzymes active in de novo purine synthesis (DNPS) that cells transiently assemble in their cytosol upon depletion or increased demand of purines. The process of purinosome formation has thus far been
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