Analytical Data
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Gene name
Protease 7/OmpT
- Application
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Alternative Names
Omptin Outer membrane protein 3B Protease A Protease VII
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Species
Escherichia coli O157:H7
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P58603
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Expression Region
21-317aa(G236K,K237G)
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Molecular Weight
49.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Protease 7, also known as OmpT (Outer Membrane Protein T), is a member of the type 1 serine protease family and is primarily found in the outer membrane of certain Gram-negative bacteria, including Escherichia coli. This protein plays a crucial role in the bacterial life cycle by participating in the degradation of peptide bonds, which is essential for nutrient acquisition and regulation of protein turnover. The ability of OmpT to cleave various substrates has garnered significant interest in the fields of microbiology and biotechnology, as it can be utilized in the development of therapeutic agents and diagnostic tools. Furthermore, recombinant forms of OmpT have been explored for their potential to enhance the delivery and efficacy of various biomolecules and vaccines, owing to their unique properties. Research into the structural and functional aspects of Protease 7/OmpT has provided valuable insights into its enzymatic mechanisms, substrate specificity, and potential applications in biocatalysis. Understanding the regulation and expression of this protease is also critical, as it could offer novel strategies for combating antibiotic resistance, which is a growing global concern. Given the increasing relevance of biotechnological applications, studies investigating the re-engineering of OmpT for improved performance in diverse industrial processes are actively being pursued. Overall, Protease 7/OmpT represents a compelling target for ongoing research, with implications reaching far beyond its native bacterial context, potentially revolutionizing approaches in drug development and molecular biology.
