AICAR transformylase Antibody (F38 P7 H9): sc-53612

AICAR transformylase Antibody (F38 P7 H9) is a mouse monoclonal IgG1 kappa light chain antibody that detects AICAR transformylase protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and immunohistochemistry. Anti-AICAR transformylase antibody (F38 P7 H9) is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. AICAR transformylase plays a crucial role in purine biosynthesis, specifically catalyzing the conversion of AICAR (5-aminoimidazole-4-carboxamide ribonucleotide) to formyl-AICAR, which is essential for the production of nucleotides and inositol monophosphate (IMP). This enzymatic activity is vital for cellular functions, as nucleotides are the building blocks of DNA and RNA, and are involved in energy transfer and signaling pathways. Defects in the ATIC gene, which encodes AICAR transformylase, can lead to AICA-ribosuria, a severe inborn error of metabolism characterized by the accumulation of AICA-riboside and its derivatives, resulting in significant neurological impairments such as mental retardation, epilepsy, and congenital blindness. AICAR transformylase monoclonal antibody (F38 P7 H9) accurately detects this protein across multiple species, making this reagent invaluable for researchers studying purine metabolism and related disorders.

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AICAR transformylase Antibody (F38 P7 H9) References:

1. Human AICAR transformylase: role of the 4-carboxamide of AICAR in binding and catalysis.  |  Wall, M., et al. 2000. Biochemistry. 39: 11303-11. PMID: 10985775
2. AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC.  |  Marie, S., et al. 2004. Am J Hum Genet. 74: 1276-81. PMID: 15114530
3. Different foreign genes incidentally integrated into the same locus of the Streptococcus suis genome.  |  Sekizaki, T., et al. 2005. J Bacteriol. 187: 872-83. PMID: 15659665
4. 5-Aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside renders glucose output by the liver of the dog insensitive to a pharmacological increment in insulin.  |  Camacho, RC., et al. 2005. Am J Physiol Endocrinol Metab. 289: E1039-43. PMID: 16046457
5. 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranoside (AICAR) attenuates the expression of LPS- and Abeta peptide-induced inflammatory mediators in astroglia.  |  Ayasolla, KR., et al. 2005. J Neuroinflammation. 2: 21. PMID: 16174294
6. AMP-activated protein kinase alpha2 activity is not essential for contraction- and hyperosmolarity-induced glucose transport in skeletal muscle.  |  Fujii, N., et al. 2005. J Biol Chem. 280: 39033-41. PMID: 16186119
7. A role for hypothalamic malonyl-CoA in the control of food intake.  |  Hu, Z., et al. 2005. J Biol Chem. 280: 39681-3. PMID: 16219771
8. AMP-activated protein kinase protects cardiomyocytes against hypoxic injury through attenuation of endoplasmic reticulum stress.  |  Terai, K., et al. 2005. Mol Cell Biol. 25: 9554-75. PMID: 16227605
9. AICAR stimulates IL-6 production via p38 MAPK in cardiac fibroblasts in adult mice: a possible role for AMPK.  |  Du, JH., et al. 2005. Biochem Biophys Res Commun. 337: 1139-44. PMID: 16229818
10. Ring opening reactions: synthesis of AICAR analogs as potential antimetabolite agents.  |  Costanzi, S., et al. 2005. Nucleosides Nucleotides Nucleic Acids. 24: 415-8. PMID: 16247961
11. Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis.  |  Verma, P., et al. 2017. FEBS J. 284: 4233-4261. PMID: 29063699
12. AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine biosynthesis and infection by Cryptococcus neoformans.  |  Wizrah, MSI., et al. 2022. J Biol Chem. 298: 102453. PMID: 36063996

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-AICAR transformylase Antibody (F38 P7 H9) has 3 citations in a variety of scientific publications.

Primary antibodies like Anti-AICAR transformylase Antibody (F38 P7 H9) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

AICAR transformylase Antibody (F38 P7 H9) Specifications

Alternate Product Name: AICAR transformylase

Product Clone Name: F38 P7 H9

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG₁ kappa light chain

Amino Acids: 582-592

Epitope Target: AICAR transformylase

Epitope Species: human

Product Reactivity/Detection: AICAR transformylase

Species Reactivity/Detection: mouse, rat, human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: Drosophila, Xenopus

Applications: WB, IP, IF, IHC(P)

Vialing Information: Each vial contains 200 µg IgG₁ kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 3 citations in various scientific publications

Available Conjugates/Forms for AICAR transformylase Antibody (F38 P7 H9): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin