Analytical Data
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Gene name
BPHL
- Application
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Alternative Names
BPHL；MCNAA；Valacyclovir hydrolase
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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
Q86WA6
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Expression Region
38-291aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSVTSAKVAVNGVQLHYQQTGEGDHAVLLL PGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFER DAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANA YVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQF KHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHL MPEGKHNLHLRFADEFNKLAEDFLQ
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Molecular Weight
31 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
BPHL (Bile Salt-stimulated Lipase) is a significant enzyme involved in lipid metabolism, particularly in the digestion and absorption of dietary fats. It is primarily produced in the pancreas and plays a crucial role in hydrolyzing triglycerides and monoacylglycerols in the intestinal lumen. Abnormalities in BPHL activity have been associated with various metabolic disorders, highlighting its potential as a biomarker or therapeutic target. Recent studies have focused on the recombinant expression of BPHL to explore its biochemical properties, functionality, and potential applications in biomedicine and food science. The ability to produce BPHL in a recombinant system not only facilitates a deeper understanding of its structure-function relationship but also enables the development of enzyme-based products for enhancing lipid digestion and improving nutrient absorption. As interest in enzyme engineering and functional foods grows, research into BPHL recombinant proteins continues to expand, promising novel insights into metabolic health and therapeutic interventions for lipid-related diseases.
