Analytical Data
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Gene name
pbp
- Application
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Alternative Names
pbp；PBP；PEBP；Phosphatidylethanolamine-binding Protein 1
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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
P07944
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Expression Region
344-670aa
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AA Sequence
NDYGSGTAIHPQTGELLALVSTPSYDVYPFMYGMSNEEYNKLTEDKKEPLLNKFQITTSPGSTQKILTAMIGLNNKTLDDKTSYKIDGKGWQKDKSWGGYNVTRYEVVNGNIDLKQAIESSDNIFFARVALELGSKKFEKGMKKLGVGEDIPSDYPFYNAQISNKNLDNEILLADSGYGQGEILINPVQILSIYSALENNGNINAPHLLKDTKNKVWKKNIISKENINLLNDGMQQVVNKTHKEDIYRSYANLIGKSGTAELKMKQGETGRQIGWFISYDKDNPNMMMAINVKDVQDKGMASYNAKISGKVYDELYENGNKKYDIDE
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Molecular Weight
44.2 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
PBP (Penicillin-binding proteins) are a family of proteins that play a critical role in bacterial cell wall synthesis and maintenance. They are classified into different classes based on their function and structural characteristics. The analysis of PBP has garnered significant attention due to its importance in understanding bacterial physiology and its implications in antibiotic resistance. Many bacteria, particularly clinically relevant pathogens such as Staphylococcus aureus and Streptococcus pneumoniae, possess PBPs that contribute to their survival and virulence. The emergence of antibiotic-resistant strains has necessitated the development of novel therapeutics targeting PBPs, making their study more urgent. Recent advances in recombinant protein technology have enabled researchers to produce and purify PBP variants, allowing for in-depth biochemical and structural studies. By elucidating the mechanisms by which PBPs interact with beta-lactam antibiotics and understanding their conformational dynamics, scientists aim to design more effective inhibitors that can circumvent resistance mechanisms. Additionally, recombinant PBPs can serve as valuable tools in vaccine development and diagnostics. Overall, the study of PBP recombination not only deepens our understanding of bacterial resistance and pathogenesis but also provides a promising avenue for combating infections caused by resistant bacteria.
