Analytical Data
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Gene name
pbpD
- Application
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Alternative Names
pbpD；Penicillin-binding Protein 4
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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
P40750
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Expression Region
213-450aa
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AA Sequence
PNNPTLYDPLKHFDYTKSRQERLLKGLKDAGVITDKELKKAVKQKIKLDVEKREDKYPDYVSYVNDEFTQLVSESEGFDKRLQKASGKQKEKIENELSARVSTLMKDGVKIYTALDPYMQNQVVAQMNSKLPYADVQGGAAVINHQTHQIIALSGGKNYQKYDFNRAYQAYRQPGSSIKPLLDYGPYIEQTGATTSSTIDASKFCSKDYCPQNYNNRTYGTVTLDTAFKNSYNTPAIR
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Molecular Weight
43.0 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
PBP-D, or Penicillin-Binding Protein D, is an essential component in the cell wall biosynthesis of bacteria, particularly in Gram-negative organisms. Its primary role is to facilitate the cross-linking of peptidoglycan, which provides structural integrity and shape to bacterial cells. Research on PBP-D has gained significance due to the rising prevalence of antibiotic-resistant strains of bacteria, making it a vital target for novel antimicrobial drug development. By investigating the structure and function of PBP-D, scientists aim to understand its mechanism of action and interactions with beta-lactam antibiotics, which inhibit cell wall synthesis. Additionally, the recombinant expression of PBP-D offers a platform for studying its enzymatic properties and protein-protein interactions in detail. This research not only contributes to the fundamental understanding of bacterial cell biology but also lays the groundwork for innovative therapeutic strategies against multidrug-resistant infections. Overall, the study of PBP-D represents a critical avenue in microbiology and drug discovery, with the potential to address significant public health challenges posed by resistant bacterial pathogens.
