Analytical Data
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Gene name
pbpD
- Application
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Alternative Names
pbpD; BSU31490; Penicillin-binding protein 4; PBP 4) [Includes: Penicillin-insensitive transglycosylase; EC 2.4.1.129; Peptidoglycan TGase); Penicillin-sensitive transpeptidase; EC 3.4.16.4; DD-transpeptidase)]
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Species
Bacillus subtilis
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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
P40750
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Expression Region
213-450aa
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Molecular Weight
43 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
PbpD, or penicillin-binding protein D, is a crucial enzyme involved in bacterial cell wall synthesis, primarily in Gram-negative bacteria. As an important member of the PBP family, PbpD plays a significant role in maintaining cell integrity and shape, facilitating the synthesis and remodeling of peptidoglycan, which is the primary component of bacterial cell walls. The study of PbpD and its related proteins has garnered increasing attention due to its potential as a target for antibiotic development, especially in the face of rising antibiotic resistance in pathogenic bacteria. With the emergence of multi-drug resistant strains, there is an urgent need for new therapeutic strategies to combat bacterial infections. Researchers aim to elucidate the structure-function relationship of PbpD, investigate its enzymatic mechanisms, and assess its interactions with antibiotics and inhibitors. By developing PbpD-targeted inhibitors, the goal is to create innovative antibiotics that can effectively disrupt cell wall synthesis, leading to bacterial cell death. Furthermore, understanding the regulatory pathways involving PbpD could provide insights into bacterial growth and division, paving the way for new drug discovery approaches. This research not only has significant implications for treating resistant bacterial infections but also contributes to the broader field of microbiology and antibiotic development.
