AV41766
Anti-OTC antibody produced in rabbit
IgG fraction of antiserum
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All Photos(3)
Synonym(s):
Anti-OCTD, Anti-Ornithine carbamoyltransferase
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
39 kDa
species reactivity
pig, bovine, horse, sheep, mouse, rat, goat, human, dog
concentration
0.5 mg - 1 mg/mL
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... OTC(5009)
General description
Ornithine carbamoyltransferase/ornithine transcarbamylase is a mitochondrial enzyme that maintains the urea cycle by regenerating citrulline (Cit) from carbamoyl phosphate and ornithine; wherein ornithine is generated during the catabolism of arginine to release urea for excretion.
Specificity
Anti-OTC polyclonal antibody reacts with canine, human, mouse, rat, bovine, and pig ornithine carbamoyltransferase/ornithine transcarbamylase(s).
Immunogen
Synthetic peptide directed towards the N terminal region of human OTC
Application
Anti-OTC polyclonal antibody is used to tag ornithine transcarbamylase for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of ornithine transcarbamylase in the urea cycle.
Biochem/physiol Actions
OTC is a mitochondrial matrix enzyme. Missense, nonsense, and frameshift mutations in this enzyme lead to ornithine transcarbamylase deficiency, which causes hyperammonemia. Since the gene for this enzyme maps close to that for Duchenne muscular dystrophy, it may play a role in that disease also.This nuclear gene encodes a mitochondrial matrix enzyme. Missense, nonsense, and frameshift mutations in this enzyme lead to ornithine transcarbamylase deficiency, which causes hyperammonemia. Since the gene for this enzyme maps close to that for Duchenne muscular dystrophy, it may play a role in that disease also.
Sequence
Synthetic peptide located within the following region: AFRNGHNFMVRNFRCGQPLQNKVQLKGRDLLTLKNFTGEEIKYMLWLSAD
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.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Jason L Robinson et al.
American journal of physiology. Gastrointestinal and liver physiology, 315(4), G638-G649 (2018-07-27)
Necrotizing enterocolitis (NEC) is associated with low plasma arginine and vascular dysfunction. It is not clear whether low intestinal citrulline production, the precursor for arginine synthesis, occurs before and thus predisposes to NEC or if it results from tissue damage.
Xiaoying Wang et al.
The Journal of nutrition, 148(9), 1415-1420 (2018-09-06)
The endogenous production of arginine relies on the synthesis of citrulline by enteral ornithine transcarbamylase (OTC). Mutations in the gene coding for this enzyme are the most frequent cause of urea cycle disorders. There is a lack of correlation between
Alejo M Capiglioni et al.
Cells, 12(11) (2023-06-10)
We previously reported that, in cultured hepatocytes, mitochondrial aquaporin-8 (AQP8) channels facilitate the conversion of ammonia to urea and that the expression of human AQP8 (hAQP8) enhances ammonia-derived ureagenesis. In this study, we evaluated whether hepatic gene transfer of hAQP8
Lin He et al.
Oncology letters, 17(6), 5030-5038 (2019-06-13)
Hepatocellular carcinoma (HCC) is one of the leading causes of cancer-associated mortalities worldwide. The role of ornithine transcarbamylase (OTC) in HCC remains unclear. In the present study, the expression of OTC in HCC was analyzed based on datasets from the
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