Analytical Data
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Gene name
BCL2L14
- Application
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Alternative Names
BCL2L14；BCLG；Apoptosis facilitator Bcl-2-like Protein 14
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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
Q9BZR8
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Expression Region
1-327aa
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AA Sequence
MCSTSGCDLEEIPLDDDDLNTIEFKILAYYTRHHVFKSTPALFSPKLLRTRSLSQRGLGNCSANESWTEVSWPCRNSQSSEKAINLGKKKSSWKAFFGVVEKEDSQSTPAKVSAQGQRTLEYQDSHSQQWSRCLSNVEQCLEHEAVDPKVISIANRVAEIVYSWPPPQATQAGGFKSKEIFVTEGLSFQLQGHVPVASSSKKDEEEQILAKIVELLKYSGDQLERKLKKDKALMGHFQDGLSYSVFKTITDQVLMGVDPRGESEVKAQGFKAALVIDVTAKLTAIDNHPMNRVLGFGTKYLKENFSPWIQQHGGWEKILGISHEEVD
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Molecular Weight
63.6 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
BCL2L14, also known as BNIP3L (Bcl-2-like 14), is a member of the Bcl-2 family of proteins, which play crucial roles in the regulation of apoptosis and cellular stress responses. It is particularly significant in the context of cancer and neurodegenerative diseases, as its expression is influenced by hypoxic conditions and various stress stimuli. Research has shown that BCL2L14 is involved in the regulation of mitochondrial autophagy, a process vital for cellular homeostasis and survival under stress conditions. Given its pro-apoptotic function, BCL2L14 has garnered attention as a potential therapeutic target. Studies have indicated that manipulating its expression may enhance the efficacy of cancer treatments by promoting cancer cell death. Furthermore, exploring its interactions with other proteins in the Bcl-2 family could provide insights into the complex cell survival pathways and lead to the development of novel strategies for managing diseases characterized by dysregulated apoptosis. Recent advances in recombinant protein technologies have enabled the production and purification of BCL2L14, facilitating detailed biochemical and structural studies that could elucidate its functional mechanisms. Understanding the role of BCL2L14 in cellular pathways not only enhances our knowledge of tumor biology but also opens new avenues for targeted therapies in cancer and other conditions where apoptosis is a key factor.
