Recombinant Mouse Ornithine Carbamoyltransferase/OTC Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9990P

Recombinant Mouse Ornithine Carbamoyltransferase/OTC Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9990P
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Product Overview

Host Species Mouse
Accession P11725
Synonym EC MGC129967 MGC129968 MGC138856 OCTD Ornithine Carbamoyltransferase Ornithine carbamoyltransferase mitochondrial Ornithine carbamoyltransferase, mitochondrial Ornithine transcarbamylase Otc OTC_HUMAN OTCase
Description Recombinant Mouse Ornithine Carbamoyltransferase/OTC Protein (Tagged) was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 52 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion.
Subcellular Location Mitochondrion matrix.
Protein Families ATCase/OTCase family
Database References
Associated Diseases Defects in Otc are the cause of the Sparse fur (spf) phenotype. Spf mouse have an OTCase with an overall decrease in activity, and altered substrate affinity.

Gene Functions References

  1. Gene correction in adult OTC-deficient mice was lower and accompanied by larger deletions that ablated residual expression from the endogenous OTC gene, leading to diminished protein tolerance and lethal hyperammonemia on a chow diet PMID: 26829317
  2. The corresponding OTC tissue enzyme activities were between 3-6% of normal control in mouse and human liver. The use of the cryptic splice sites was reproduced in minigenes carrying murine or human mutant sequences PMID: 25853564
  3. Serum OCT seemed to reflect tumor necrosis factor-alpha-mediated hepatic damage in diabetic obese mice and could be useful in the application for non-alcoholic fatty liver disease with features of metabolic syndrome, such as obesity and diabetes. PMID: 19793175
  4. in vivo regulation by HNF4alpha PMID: 11994307
  5. Results highlight the importance of the interaction between the OTC spf-ash mutation (ornithine transcarbamylase deficiency) and genetic backgrounds on metabolic phenotypes (ureagenesis, arginine metabolism, and nitric oxide production). PMID: 17925451
  6. Phenotypic correction of OTC deficiency using low-dose helper-dependent adenoviral vectors is reported. PMID: 18563850
  7. Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. PMID: 19318352


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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