Analytical Data
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Gene name
ompT
- Application
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Alternative Names
ompT；Protease 7
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09169
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Expression Region
21-317aa
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AA Sequence
STETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKVSQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRGGNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIKGWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGFRDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELGGTFKYSGWVESSDNDEHYDPGKRITYRSKVKDQNYYSVAVNAGYYVTPNAKVYVEGAWNRVTNKKGNTSLYDHNNNTSDYSKNGAGIENYNFITTAGLKYTF
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Molecular Weight
37.5 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
The ompT protein, a member of the outer membrane protease family found in Gram-negative bacteria, plays a crucial role in various biological processes, including protein quality control and the maintenance of outer membrane integrity. Its significance has gained attention due to its involvement in the degradation of misfolded or damaged proteins, which helps bacteria adapt to environmental stresses. Researchers have increasingly focused on the recombinant expression of ompT for several reasons. Firstly, it has potential applications in biotechnology and medicine, such as in the development of biosensors or therapeutic proteins. Additionally, understanding the structure and function of ompT can provide insights into bacterial pathogenicity and resistance mechanisms. The challenges associated with successfully obtaining and characterizing recombinant ompT, such as ensuring proper folding and activity in a heterologous expression system, have spurred advancements in protein engineering and expression techniques. Studies have shown that optimizing expression conditions and employing suitable tags can enhance yield and functionality of ompT. Consequently, research on ompT recombinant protein not only furthers our understanding of bacterial physiology but also opens avenues for innovations in antimicrobial strategies and biotechnological applications. This research area continues to evolve, driven by the need for efficient protein production systems and the rising importance of outer membrane proteins in microbial ecology and pathogenicity.
