Analytical Data
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Gene name
Bcl2L
- Application
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Alternative Names
Bcl2L；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
Bcl2L (B-cell lymphoma 2 like) proteins are critical regulators of apoptosis, a process that balances cell survival and death, influencing numerous physiological and pathological conditions. As members of the Bcl-2 family, which includes both pro-apoptotic and anti-apoptotic proteins, Bcl2L plays a pivotal role in determining cell fate in response to various stress signals, such as DNA damage and oxidative stress. Research into Bcl2L has garnered increasing interest due to its implications in cancer biology; dysregulation of its expression or function can lead to tumorigenesis and resistance to chemotherapy. Investigating the structure and function of Bcl2L proteins through techniques such as recombinant protein production, crystallography, and functional assays allows for a better understanding of their role in cellular mechanisms. These studies not only enhance our knowledge of cell survival pathways but also pave the way for the development of targeted therapies aimed at modulating apoptosis in cancer treatment. Consequently, Bcl2L serves as a potential biomarker and therapeutic target, highlighting the importance of understanding its biology within the context of cell death and disease progression.
