Analytical Data
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Gene name
NlpD
- Application
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Alternative Names
nlpD; b2742; JW2712Murein hydrolase activator NlpD
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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
P0ADA3
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Expression Region
26-379aa
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Molecular Weight
53.5 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
NlpD is a crucial protein in bacterial physiology and has garnered significant interest due to its role in bacterial cell envelope integrity and pathogenicity. It belongs to the group of non-classical proteins that are known to play essential roles in stress responses and virulence. Research has highlighted NlpD's involvement in the maintenance of the peptidoglycan layer, which is vital for bacterial shape and protection against environmental stresses. Understanding the structure and function of NlpD is important for elucidating the mechanisms of bacterial infection, as well as for potential therapeutic applications. Recent studies have focused on the recombinant expression of NlpD to facilitate functional assays and structural characterization. The production of recombinant NlpD allows for detailed studies of its biochemical properties, interactions with other cellular components, and its potential as a target for novel antimicrobial agents. As antibiotic resistance continues to rise, research into essential bacterial proteins like NlpD is critical for developing innovative strategies to combat infectious diseases. Overall, the study of NlpD and its recombinant forms represents a promising avenue for advancing our understanding of bacterial physiology and improving public health outcomes.
