Analytical Data
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Gene name
BCL2L1
- Application
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Alternative Names
BCL2L1；BCL2L；BCLX；Bcl-2-like Protein 1
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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
Q07817
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Expression Region
1-209aa
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AA Sequence
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
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Molecular Weight
39.4kDa
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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
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Protein Description
BCL2L1, also known as Bcl-xL, is a crucial member of the Bcl-2 family of proteins, which play a significant role in the regulation of apoptosis, or programmed cell death. This protein is particularly important in maintaining cell survival by inhibiting pro-apoptotic factors, thus allowing for the prolonged lifespan of cells, which is vital in various physiological processes. However, dysregulation of BCL2L1 has been implicated in numerous cancers and other diseases, where its overexpression can contribute to tumorigenesis by promoting cell survival in the presence of apoptosis-inducing signals. Research involving recombinant BCL2L1 protein has gained traction as it provides insights into the molecular mechanisms governing its function and offers potential therapeutic avenues. Studying BCL2L1 in a recombinant form allows for the detailed analysis of its protein structure and interactions, paving the way for the development of inhibitors that could restore the balance between cell death and survival in cancer treatment. Furthermore, understanding BCL2L1's interactions with other cellular proteins could reveal novel pathways and targets for therapeutic intervention, making it a focal point in cancer research and a key candidate for drug development.
