Analytical Data
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Gene name
dltA
- Application
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Alternative Names
D-alanine--poly(phosphoribitol) ligase subunit 1 D-alanine-activating enzyme dae
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Species
Bacillus subtilis
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P39581
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Expression Region
1-503aa
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Molecular Weight
59.8 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
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.
