O2501
Ornithine Transcarbamylase from Streptococcus faecalis
lyophilized powder, ≥300 units/mg protein
Synonym(s):
Carbamoylphosphate:L-Ornithine Carbamoyltransferase, OTCase, Ornithine Carbamoyl Transferase
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About This Item
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form
lyophilized powder
Quality Level
specific activity
≥300 units/mg protein
composition
Protein, ≥65% Lowry
storage temp.
−20°C
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Biochem/physiol Actions
Mutations in ornithine transcarbamylase cause Ornithine transcarbamylase deficiency which prevents the clearance of the byproduct ammonia leading to hyperammonemia.
Unit Definition
One unit will form 1.0 μmole of citrulline from ornithine and carbamyl phosphate per min at pH 8.5 at 37 °C.
Physical form
Lyophilized powder contains Tris buffer salts
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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James M Wilson et al.
Molecular genetics and metabolism, 105(2), 263-265 (2011-12-02)
A 66 year old woman who is a manifesting heterozygote for ornithine transcarbamylase deficiency (OTCD) presented with hepatocellular carcinoma (HCC). Fourteen years prior to this presentation she participated in a phase I gene therapy study which used an adenoviral vector
Gabriela Jenikova et al.
Vaccine, 29(51), 9529-9537 (2011-10-18)
Giardia lamblia is a leading protozoan cause of diarrheal disease worldwide, yet preventive medical strategies are not available. A crude veterinary vaccine has been licensed for cats and dogs, but no defined human vaccine is available. We tested the vaccine
Tatjana Skrbić et al.
PLoS computational biology, 8(6), e1002504-e1002504 (2012-06-22)
Stochastic simulations of coarse-grained protein models are used to investigate the propensity to form knots in early stages of protein folding. The study is carried out comparatively for two homologous carbamoyltransferases, a natively-knotted N-acetylornithine carbamoyltransferase (AOTCase) and an unknotted ornithine
Ian E Alexander et al.
Journal of inherited metabolic disease, 35(4), 641-645 (2012-03-10)
Many metabolic diseases are compelling candidates for gene therapy, and are the subject of vigorous pre-clinical research. Successful phenotype correction in mouse models is now commonplace and research effort is increasingly being directed towards addressing the translational challenges inherent in
Eddy C Hsueh et al.
Journal of hematology & oncology, 5, 17-17 (2012-05-02)
Recombinant human arginase (rhArg) has been developed for arginine deprivation therapy in cancer, and is currently under clinical investigation. During pre-clinical evaluation, rhArg has exhibited significant anti-proliferative activity in cancer cells deficient in the expression of ornithine carbamoyl transferase (OCT).
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