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ATIC Antibody (C-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession P31939
Additional Information
Gene ID 471
Other Names Bifunctional purine biosynthesis protein PURH, Phosphoribosylaminoimidazolecarboxamide formyltransferase, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, AICAR transformylase, IMP cyclohydrolase, ATIC, IMP synthase, Inosinicase, ATIC, PURH
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name ATIC (HGNC:794)
Function Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis (PubMed:11948179, PubMed:14756554). Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) (PubMed:9378707, PubMed:11948179, PubMed:10985775). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction (PubMed:10985775). Also catalyzes the cyclization of FAICAR to IMP (PubMed:11948179, PubMed:14756554). Is able to convert thio-AICAR to 6- mercaptopurine ribonucleotide, an inhibitor of purine biosynthesis used in the treatment of human leukemias (PubMed:10985775). Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (PubMed:25687571).
Cellular Location Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54113}
Tissue Location Present in the heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas.
Research Areas
Citations (0)
citation

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Background

ATIC is a bifunctional protein that catalyzes the last two steps of the de novo purine biosynthetic pathway. The N-terminal domain has phosphoribosylaminoimidazolecarboxamide formyltransferase activity, and the C-terminal domain has IMP cyclohydrolase activity.

References

Sharma,S. Pharmacogenet. Genomics 19 (10), 823-828 (2009)Vergis,J.M. J. Biol. Chem. 276 (11), 7727-7733 (2001)

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$ 277.78
Cat# BP6979d
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