Analytical Data
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Gene name
pbpA
- Application
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Alternative Names
Peptidoglycan TGase DD-transpeptidase
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Species
Clostridium botulinum
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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
A5I6G4
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Expression Region
663-830aa
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Molecular Weight
35.2 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
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Protein Description
The study of the pbpA recombinant protein is rooted in its significance within bacterial physiology and antibiotic resistance mechanisms. PbpA, or Penicillin-binding protein A, is an essential enzyme in the peptidoglycan biosynthesis pathway, critical for maintaining the structural integrity of bacterial cell walls. Understanding its function is particularly important as it is a target for beta-lactam antibiotics, which are widely used to combat bacterial infections. However, the emergence of antibiotic-resistant strains has heightened the urgency for detailed investigations into the mechanisms by which bacteria regulate pbpA expression and activity. Research has shown that mutations in the pbpA gene can lead to alterations in antibiotic susceptibility and virulence, making it a focal point for developing new therapeutic strategies. Moreover, recombinant techniques allow for the production of purified PbpA, facilitating biochemical assays to evaluate its functional properties and interactions with antibiotics. Insights gained from these studies can contribute to a deeper understanding of bacterial resistance patterns and inform the design of novel inhibitors or adjuvant therapies to enhance the efficacy of existing antibiotics. Thus, the investigation of pbpA recombinant protein not only sheds light on fundamental biological processes but also holds promise for addressing pressing public health challenges posed by antibiotic resistance.
