Recombinant Mouse Ornithine Transcarbamylase, Mitochondrial (OTC) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02904P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Ornithine Transcarbamylase, Mitochondrial (OTC) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02904P
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Product Overview

Description Recombinant Mouse Ornithine Transcarbamylase, Mitochondrial (OTC) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P11725
Target Symbol OTC
Synonyms Otc; Ornithine carbamoyltransferase; mitochondrial; EC 2.1.3.3; Ornithine transcarbamylase; OTCase
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence SQVQLKGRDLLTLKNFTGEEIQYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPSFLTTQDIHLGVNESLTDTARVLSSMTDAVLARVYKQSDLDTLAKEASIPIVNGLSDLYHPIQILADYLTLQEHYGSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDPNIVKLAEQYAKENGTKLSMTNDPLEAARGGNVLITDTWISMGQEDEKKKRLQAFQGYQVTMKTAKVAASDWTFLHCLPRKPEEVDDEVFYSPRSLVFPEAENRKWTIMAVMVSLLTDYSPVLQKPKF
Expression Range 33-354aa
Protein Length Full Length of Mature Protein
Mol. Weight 52.1kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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

KEGG: mmu:18416

STRING: 10090.ENSMUSP00000056152

UniGene: PMID: 26829317

  • 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
  • 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
  • in vivo regulation by HNF4alpha PMID: 11994307
  • 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
  • Phenotypic correction of OTC deficiency using low-dose helper-dependent adenoviral vectors is reported. PMID: 18563850
  • Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. PMID: 19318352
  • FAQs

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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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