Analytical Data
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Gene name
HIST3H2A
- Application
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7L7L0
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Expression Region
Met1~Lys130
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Molecular Weight
44kDa
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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
BPI (Bactericidal/Permeability-Increasing protein) is a crucial component of the innate immune system, primarily found in neutrophils and epithelial cells. It plays a significant role in host defense against bacterial infections by exerting antimicrobial activity and enhancing bacterial phagocytosis. The structure of BPI reveals a unique cationic protein with the ability to bind to lipopolysaccharides found on the surface of Gram-negative bacteria, leading to disruption of their membranes. This interaction not only neutralizes the bacterial threats but also promotes inflammatory responses essential for clearing infections. Research on BPI and its recombinant forms has gained momentum due to its therapeutic potential in treating sepsis, pneumonia, and other infectious diseases, where conventional antibiotics may fail. Advances in molecular biology techniques have enabled the production of recombinant BPI, allowing scientists to study its structure-function relationships and optimize its antimicrobial properties. Additionally, modifications of the BPI protein may enhance its stability and efficacy, paving the way for novel antimicrobial agents that can combat multidrug-resistant pathogens. The ongoing exploration of BPI's mechanisms and its engineered variants aims to harness its full potential for clinical applications, contributing to innovative strategies in infectious disease management.
