Analytical Data
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基因名
pbp
- Application
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别名
pbp；PBP；PEBP；Phosphatidylethanolamine-binding Protein 1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P07944
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表达区间
344-670aa
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氨基酸序列
NDYGSGTAIHPQTGELLALVSTPSYDVYPFMYGMSNEEYNKLTEDKKEPLLNKFQITTSPGSTQKILTAMIGLNNKTLDDKTSYKIDGKGWQKDKSWGGYNVTRYEVVNGNIDLKQAIESSDNIFFARVALELGSKKFEKGMKKLGVGEDIPSDYPFYNAQISNKNLDNEILLADSGYGQGEILINPVQILSIYSALENNGNINAPHLLKDTKNKVWKKNIISKENINLLNDGMQQVVNKTHKEDIYRSYANLIGKSGTAELKMKQGETGRQIGWFISYDKDNPNMMMAINVKDVQDKGMASYNAKISGKVYDELYENGNKKYDIDE
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分子量
44.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
