Analytical Data
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Gene name
BCL2L2
- Application
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Alternative Names
BCL2L2；BCLW；KIAA0271；Bcl-2-like Protein 2
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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
Q92843
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Expression Region
2-172aa
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AA Sequence
MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG DEFETRFRRT FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF VFGAALCAES VNKEMEPLVG QVQEWMVAYL ETQLADWIHS SGGWAEFTAL YGDGALEEAR RLREGNWASV RT
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Molecular Weight
19 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
BCL2L2, also known as BCL-W, is a member of the BCL-2 family of proteins, which play a crucial role in the regulation of apoptosis, or programmed cell death. This protein is primarily expressed in various tissues, including the testis and brain, and is known for its anti-apoptotic properties, helping to promote cell survival by inhibiting apoptotic pathways. The study of BCL2L2 has gained significant interest due to its potential implications in cancer biology, where its overexpression can contribute to tumorigenesis by preventing the normal cell death that occurs in response to cellular stress and damage. Moreover, BCL2L2 has been implicated in various hematological malignancies, solid tumors, and neurodegenerative diseases, making it a critical target for therapeutic interventions. Recombinant expression of BCL2L2 allows for detailed functional analysis and structure-function studies, thereby aiding in the development of BCL2L2 inhibitors as potential cancer treatments. Furthermore, the investigation of its interactions with other proteins within the apoptotic signaling pathways continues to provide insight into the complex mechanisms of cell survival and death, which are essential for maintaining cellular homeostasis and responding to stressors. Understanding the molecular characteristics and biological significance of BCL2L2 will not only enhance our knowledge of cancer progression and resistance mechanisms but also pave the way for innovative therapeutic strategies aimed at modulating apoptosis in disease contexts. Thus, the research surrounding BCL2L2 recombinant proteins holds promise for advancing both basic science and clinical applications in oncology and beyond.
