Analytical Data
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Gene name
LEB6
- Application
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Alternative Names
LEB6；Legumin type B
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Species
Vicia faba
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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
P16079
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Expression Region
1-148aa
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AA Sequence
GIPYWTYNNGDEPLVAISLLDTSNIANQLDSTPRVFYLGGNPEVEFPETQEEQQERHQQKHSLPVGRRGGQHQQEEDGNSVLSGFSSEFLAQTFNTEEDTAKRLRSPRDKRNQIVRVEGGLRIINPEGQQEEEEEEEEEKQRSEQGRN
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Molecular Weight
22.9 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
The research on LEB6 recombinant protein has garnered significant attention due to its potential applications in various fields, particularly in biotechnology and medicine. LEB6, a specific variant of the LE protein family, is known for its unique structural properties and functional roles in cellular processes. Studies have indicated that LEB6 plays a critical part in modulating immune responses and may be involved in signal transduction pathways, making it a candidate for therapeutic interventions in autoimmune diseases and cancer. The ability to produce LEB6 as a recombinant protein enables researchers to investigate its properties in a controlled environment, allowing for a deeper understanding of its mechanisms of action. Furthermore, recombinant LEB6 can be utilized in the development of diagnostic tools, vaccines, and therapeutic agents. The ongoing exploration into the production methods, functional assays, and potential applications of LEB6 is crucial, as it may pave the way for innovative solutions to health challenges and enhance our knowledge of protein functions in biological systems. As such, the LEB6 recombinant protein serves as a promising focus for advancing research in molecular biology and developing new therapeutic strategies.
