Analytical Data
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Gene name
BPI
- Application
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Alternative Names
BPI；Bactericidal permeability-increasing Protein
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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
P17213
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Expression Region
32-487aa
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AA Sequence
VNPGVVVRISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSISNANIKISGKWKAQKRFLKMSGNFDLSIEGMSISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGWLIQLFHKKIESALRNKMNSQVCEKVTNSVSSELQPYFQTLPVMTKIDSVAGINYGLVAPPATTAETLDVQMKGEFYSENHHNPPPFAPPVMEFPAAHDRMVYLGLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIHVSASTPPHLSVQPTGLTFYPAVDVQAFAVLPNSSLASLFLIGMHTTGSMEVSAESNRLVGELKLDRLLLELKHSNIGPFPVELLQDIMNYIVPILVLPRVNEKLQKGFPLPTPARVQLYNVVLQPHQNFLLFGADVVYK
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Molecular Weight
57.6 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 BPI (Bactericidal/Permeability-Increasing) proteins has garnered significant attention due to their crucial role in the immune response, particularly in the context of bacterial infections. BPI proteins, initially identified in humans and some other mammals, are primarily secreted by neutrophils and exhibit potent bactericidal properties against a wide range of Gram-negative bacteria. Their mechanism of action involves binding to the lipopolysaccharides (LPS) on the bacterial surface, leading to the disruption of membrane integrity and eventual bacterial death. This unique capability makes BPI proteins potential candidates for therapeutic applications in treating infections that are resistant to conventional antibiotics. Furthermore, understanding the structure-function relationship of BPI proteins through recombinant protein technology can pave the way for the development of engineered variants with enhanced antibacterial activity, stability, or specificity. Advances in molecular biology techniques, including genetic engineering, have made it feasible to produce recombinant BPI proteins in various expression systems, allowing for detailed biophysical and biochemical characterization. The research on BPI proteins not only aims to elucidate their fundamental biological functions but also explores their potential in pharmaceutical development, thereby addressing the pressing global challenge of antibiotic resistance.
