Analytical Data
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Gene name
Bcl-2-like 蛋白 1
- Application
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Alternative Names
Apoptosis regulator Bcl-X
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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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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Molecular Weight
39.4 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
Bcl-2-like protein 1 (BCL2L1), also known as Bcl-XL, is a member of the Bcl-2 family of proteins that play a crucial role in regulating apoptosis, the process of programmed cell death. Dysregulation of this protein has been implicated in various forms of cancer, where it often contributes to tumor survival by inhibiting apoptosis, thereby allowing cancer cells to evade death. Research on recombinant BCL2L1 protein has been driven by the need to understand its structure-function relationship and its role in cellular mechanisms. Studying this protein is essential not only for elucidating its function in the apoptotic pathway but also for evaluating its potential as a therapeutic target. The development of BCL2L1 inhibitors or modulators has garnered significant interest in cancer therapy, as these could restore the apoptotic process in cancer cells. Furthermore, BCL2L1 has been shown to interact with other proteins within apoptosis and survival signaling pathways, making it a pivotal molecule in the cross-talk between survival and death signals. Therefore, producing recombinant BCL2L1 allows researchers to perform biochemical assays, structural studies, and high-throughput screening of small molecules, leading to novel insights into potential treatment strategies for cancer and other diseases associated with apoptosis dysfunction.
