Analytical Data
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Gene name
bla
- Application
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Alternative Names
bla；BCM1；BLAST1；CD48 antigen
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Species
E.coli
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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
P09326
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Expression Region
27-220aa
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AA Sequence
QGHLVHMTVVSGSNVTLNISESLPENYKQLTWFYTFDQKIVEWDSRKSKYFESKFKGRVRLDPQSGALYISKVQKEDNSTYIMRVLKKTGNEQEWKIKLQVLDPVPKPVIKIEKIEDMDDNCYLKLSCVIPGESVNYTWYGDKRPFPKELQNSVLETTLMPHNYSRCYTCQVSNSVSSKNGTVCLSPPCTLARS
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Molecular Weight
51.3 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
BLA (Bacterial Lytic Agent) recombinant protein research has garnered significant attention due to its potential applications in industrial biotechnology and medicine. As antibiotic resistance emerges as a major global health threat, innovative alternatives such as bacteriocins and lytic enzymes are being explored for their antibacterial properties. BLA proteins, derived from bacteriophages, specifically target and lyse bacterial cells, offering a promising solution for combating pathogenic bacteria. The ability to engineer these proteins recombinantly allows researchers to optimize their activity and specificity, enhancing their efficacy as therapeutic agents. Moreover, BLA proteins can be utilized in food preservation, wastewater treatment, and as bio-sanitizers, thus broadening their utility beyond clinical applications. Understanding the structure-function relationship of BLA proteins through biochemical and structural studies provides insights into their mechanism of action and aids in the design of more effective antimicrobial agents. Overall, the research on BLA recombinant proteins is at the forefront of addressing the challenges posed by antibiotic resistance while providing sustainable solutions in various fields.
