Analytical Data
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Gene name
menI
- Application
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Alternative Names
(DHNA-CoA hydrolase)(DHNA-CoA thioesterase)
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Species
Escherichia coli
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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
P77781
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Expression Region
1-136aa
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Molecular Weight
27.9 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
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Protein Description
MenI is a key protein involved in the biosynthesis of menaquinone (vitamin K2), which plays a critical role in various biological processes, including electron transport and redox reactions in bacteria. Understanding MenI's structure and function is essential because menaquinone is vital for bacterial survival and pathogenicity, making it an attractive target for antibiotic development. Given the rise of antibiotic resistance, researchers are increasingly focused on exploring novel targets within bacterial metabolic pathways. The study of MenI not only provides insights into the fundamental biochemical processes of bacteria but also opens up potential avenues for therapeutic intervention. By elucidating the enzymatic mechanisms and regulatory networks associated with MenI, scientists aim to develop innovative strategies to combat bacterial infections, ultimately contributing to the field of antimicrobial drug design. Additionally, research on MenI can shed light on its evolutionary significance and variations among different bacterial species, enhancing our understanding of microbial diversity and ecology.
