Analytical Data
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Gene name
Bcl-2-like protein 2
- Application
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Alternative Names
Apoptosis regulator Bcl-W
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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
Q92843
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Expression Region
2-193aa
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Molecular Weight
36.6 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 2 (Bcl2L2), a member of the Bcl-2 family, plays a crucial role in the regulation of apoptosis and cell survival. Its primary function is to promote cell survival by inhibiting programmed cell death, making it a significant factor in various physiological and pathological processes, including cancer, neurodegenerative diseases, and immune responses. Research has shown that overexpression of Bcl2L2 is associated with tumorigenesis and resistance to chemotherapy, positioning it as a potential therapeutic target. Given its importance, the study of recombinant Bcl2L2 proteins has garnered attention for understanding the protein's structure, function, and interaction with other apoptotic regulators. Recombinant expression systems, such as bacterial or yeast systems, are often employed to produce functional Bcl2L2 proteins, allowing for the investigation of its biochemical properties and the development of Bcl2L2 inhibitors. Exploring these recombinant proteins can lead to insights into apoptotic pathways and the design of novel drugs aimed at reversing the anti-apoptotic effects of Bcl2L2 in cancer cells. The ongoing research highlights the potential of targeting Bcl2L2 as a therapeutic strategy to enhance the efficacy of existing treatments and improve clinical outcomes in malignancies characterized by elevated Bcl2L2 levels.
