Analytical Data
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Gene name
menI
- Application
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Alternative Names
menI；ydiI；1.4-dihydroxy-2-naphthoyl-CoA hydrolase
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Species
Human
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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
P77781
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Expression Region
1-136aa
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AA Sequence
MIWKRKITLEALNAMGEGNMVGFLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL
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Molecular Weight
27.9kDa
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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 crucial membrane protein found in various bacteria, particularly known for its role in the biosynthesis of menaquinone (vitamin K2). This protein is part of the menaquinone biosynthetic pathway, which is essential for bacterial survival and is implicated in various cellular processes, including electron transport and redox balance. Research into MenI has gained momentum due to its potential as a target for antibacterial drug development. The increasing prevalence of antibiotic-resistant bacteria has prompted scientists to explore novel approaches to inhibiting bacterial growth, with MenI being a promising candidate due to its specific role in essential metabolic pathways. Furthermore, studying MenI can provide valuable insights into the structural and functional mechanisms of membrane proteins, contributing to the broader understanding of bacterial physiology. By characterizing MenI at the molecular level, researchers aim to elucidate its interactions within the biosynthetic pathway and identify potential inhibitors. This could lead to the development of new therapeutic strategies that specifically disrupt the function of this protein, offering a viable approach to combat bacterial infections. Overall, the study of MenI represents a convergence of microbiology, biochemistry, and medicinal chemistry, highlighting the necessity of innovative solutions to address the global challenge of antibiotic resistance.
