Analytical Data
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Gene name
BCL2L11
- Application
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Alternative Names
BCL2L11；BIM；Bcl-2-like Protein 11
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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
O43521
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Expression Region
1-112aa
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AA Sequence
MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQDRSPAPMSC DKSTQTPSPPCQAFNHYLSAMVVILEDIGDLSLCFGFIFTGLDLYGHHHS QDTEQLNHKDFS
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Molecular Weight
39 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
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Protein Description
BCL2L11, also known as Bok, is a member of the Bcl-2 family of proteins, which play critical roles in regulating apoptosis, the programmed cell death essential for maintaining cellular homeostasis and tissue development. Unlike its anti-apoptotic counterparts, BCL2L11 functions primarily as a pro-apoptotic factor, promoting cell death in various biological contexts, including development, immune responses, and cancer. Research has shown that BCL2L11 is involved in the response to cellular stressors, such as DNA damage and oxidative stress, suggesting its potential role as a tumor suppressor. Given the importance of apoptosis in cancer therapy, studying the mechanisms underlying BCL2L11's function could unveil valuable insights for targeted treatments. Furthermore, the generation of recombinant BCL2L11 proteins enables detailed investigations of its structural and functional properties, providing a better understanding of how it interacts with other Bcl-2 family members and cellular pathways. Overall, BCL2L11 represents an important focus of research aimed at elucidating the complex regulatory networks of apoptosis, with implications for developing innovative therapeutic strategies in cancer and other diseases where apoptosis is dysregulated.
