Analytical Data
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Gene name
pbpA
- Application
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Alternative Names
pbpA；Peptidoglycan D.D-transpeptidase PbpA
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Species
E.coli
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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
A5I6G4
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Expression Region
663-830aa
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AA Sequence
VDRISGKLPTQLSYRDPRGSTVYNEFFINGTIPTEYDDIHVEAQINKLTGKLASKFTPSFLVESRVFLRRDYSPGVELLDQQWLLPYSIDEGGSLPPTEEKNNSNTRDKNKDKNKNKNKDKNPSQDKPNNNNNDNNSNNNNNNNDNNNNTKPPENDSNQNHEDNKNKQ
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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
Related Products
Protein Description
The study of the pbpA gene and its encoded protein, PbpA, has garnered significant interest due to its crucial role in bacterial physiology and pathogenesis. PbpA, a penicillin-binding protein (PBP), is primarily involved in the synthesis of peptidoglycan, a vital component of the bacterial cell wall that provides structural integrity and protection against environmental stresses. Understanding the function and regulation of PbpA is essential for elucidating bacterial growth and division mechanisms. Furthermore, since penicillin and other beta-lactam antibiotics target PBPs to disrupt cell wall synthesis, PbpA is also a key player in antibiotic resistance. Many pathogenic bacteria exhibit altered expression or mutations in pbpA, which can contribute to their survival in the presence of antibiotic treatment. Therefore, recombinant PbpA is often studied to gain insights into its enzymatic activity, interaction with antibiotics, and role in resistance mechanisms. Additionally, exploring the structure-function relationship of PbpA through recombinant protein techniques can facilitate the design of novel inhibitors that could serve as potential therapeutics against antibiotic-resistant bacterial strains. Such research not only enhances our understanding of microbial resistance but also aids in the development of innovative strategies to combat bacterial infections, making PbpA a significant target in microbiology and pharmaceutical research.
