Analytical Data
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基因名
dltA
- Application
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别名
D-alanine--poly(phosphoribitol) ligase subunit 1 D-alanine-activating enzyme dae
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种属
Bacillus subtilis
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P39581
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表达区间
1-503aa
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分子量
59.8 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
The study of DltA recombinant protein is rooted in its crucial role in the process of d-alanylation of lipoteichoic acid (LTA) in Gram-positive bacteria. DltA serves as a membrane-associated enzyme that catalyzes the addition of d-alanine to the LTA molecule, a modification that is essential for bacterial cell wall integrity and biofilm formation. This d-alanylation not only enhances the positive charge of the bacterial surface, contributing to increased resistance against host immune responses but also plays a significant role in the adhesion of bacteria to host tissues. Due to its importance in bacterial virulence and pathogenesis, including in pathogens like Staphylococcus aureus, DltA has gained significant attention as a potential target for antibiotic development. Investigating the structure and function of the DltA recombinant protein aids in understanding the enzymatic mechanisms involved in d-alanylation and provides insights into the biochemical pathways of bacterial cell wall biosynthesis. Furthermore, the purification and characterization of the DltA recombinant protein can reveal critical information regarding its enzymatic activity and regulatory mechanisms, paving the way for novel antibacterial strategies aimed at combating resistant bacterial infections. As antibiotic resistance remains a global health concern, research on DltA and its associated pathways is increasingly relevant, presenting opportunities for the development of new therapeutic interventions that can effectively disrupt bacterial growth without compromising host cells.
