Analytical Data
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Gene name
BSDL
- Application
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Alternative Names
CEL; FAP; BAL; BSSL; FAPP; LIPA; MODY8; Carboxyl Ester Lipase; Bile salt-stimulated lipase; Bucelipase; Cholesterol esterase; Pancreatic lysophospholipase; Sterol esterase
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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
P19835
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Expression Region
Asp117~Glu361
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Molecular Weight
56kDa
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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
BSDL, or Bacterial Sialidase D-Lactate, is an important enzyme that has gained significant attention in biochemistry and biotechnology due to its potential applications in medicine and industry. Sialidases are enzymes that cleave sialic acid residues from glycoproteins and glycopeptides, playing a crucial role in various biological processes, including cell signaling, pathogen recognition, and immune response modulation. The study of BSDL is particularly relevant because it is derived from a bacterial source, making it a valuable tool for understanding the enzymatic mechanisms of carbohydrate metabolism in prokaryotes. Additionally, BSDL has shown promise in therapeutic applications, such as in drug development for diseases linked to sialic acid metabolism, including certain cancers and viral infections. Its ability to modify glycan structures can lead to enhanced efficacy of glycoprotein-based therapeutics. Research into the expression, purification, and structural characterization of BSDL has paved the way for its potential application in glyco-engineering and vaccine development. The ongoing exploration of BSDL's properties aims to unlock new avenues for harnessing this enzyme in both diagnostic and treatment strategies, emphasizing the importance of understanding bacterial enzymes in the broader context of human health and disease.
