Analytical Data
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Gene name
pbpX
- Application
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Alternative Names
pbpX;Penicillin-binding Protein 2X
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Species
Human
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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
P59676
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Expression Region
287-611aa
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AA Sequence
KYMTATLVSAKTGEILATTQRPTFDADTKEGITEDFVWRDILYQSNYEPGSTMKVMMLAAAIDNNTFPGGEVFNSSELKIADATIRDWDVNEGLTGGRMMTFSQGFAHSSNVGMTLLEQKMGDATWLDYLNRFKFGVPTRFGLTDEYAGQLPADNIVNIAQSSFGQGISVTQTQMIRAFTAIANDGVMLEPKFISAIYDPNDQTARKSQKEIVGNPVSKDAASLTRTNMVLVGTDPVYGTMYNHSTGKPTVTVPGQNVALKSGTAQIADEKNGGYLVGLTDYIFSAVSMSPAENPDFILYVTVQQPEHYSGIQLGEFANPILERA
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Molecular Weight
83.2 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 pbpX recombinant protein has gained significance in the field of microbiology and molecular biology due to its potential implications in bacterial pathogenesis and antibiotic resistance. PbpX, or penicillin-binding protein X, is a crucial enzyme involved in bacterial cell wall synthesis, specifically in the cross-linking of peptidoglycan layers, which is vital for maintaining cell shape and integrity. Its role is particularly intriguing in gram-positive bacteria, where it contributes to the formation of a robust cell wall structure. Understanding the structure and function of pbpX can reveal mechanisms of beta-lactam resistance, as certain bacterial strains exhibit mutations in genes encoding this protein, rendering conventional antibiotics less effective. Researchers are particularly focused on characterizing the pbpX gene in various pathogenic strains, including Streptococcus pneumoniae and Staphylococcus aureus, as these bacteria are responsible for a range of serious infections. The recombinant expression of pbpX in a host system allows scientists to study its biochemical properties, interactions with other proteins, and potential as a target for novel antimicrobial agents. Furthermore, structural analyses through techniques such as X-ray crystallography or cryo-electron microscopy can provide insight into the protein's active site and inform drug design efforts. Overall, the exploration of the pbpX recombinant protein is critical for the development of innovative strategies to combat antibiotic-resistant infections, highlighting its importance in public health and therapeutic development.











