Analytical Data
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Gene name
bLg
- Application
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Alternative Names
LGB; B-LG
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Species
Pig
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04119
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Expression Region
Val19~Val178
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Molecular Weight
24kDa
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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 bLg (bacteriophage lambda) recombinant proteins has emerged as a significant area of research in molecular biology and biotechnology due to their potential applications in various fields, including therapeutics, diagnostics, and agriculture. Bacteriophage lambda is a well-characterized virus that infects bacteria and has been instrumental in understanding genetic mechanisms and protein interactions. Researchers have harnessed the unique properties of bLg proteins to develop recombinant forms that can enhance biological functions or serve as tools for specific assays. The ability to manipulate bLg proteins allows for the exploration of protein folding, stability, and functionality, which can contribute to the design of novel biomolecules. Moreover, bLg-based vaccines and diagnostic kits are being investigated for their efficacy in combating infectious diseases, highlighting the relevance of bLg recombinant proteins in public health. Additionally, the incorporation of bLg proteins in plant systems has shown promise in improving crop resistance to pathogens, suggesting their potential in sustainable agriculture. Overall, the study of bLg recombinant proteins is not only pivotal for expanding our understanding of protein biology but also for addressing real-world challenges in health and food security.
