Analytical Data
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Gene name
BID
- Application
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Alternative Names
BH3-interacting domain death agonist; BID; p15 BID
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P70444
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Expression Region
Met1~Asp195
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Molecular Weight
26kDa
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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
Related Products
Protein Description
The research on BID (BH3-interacting domain death agonist) recombinant protein stems from its critical role in apoptosis regulation and cellular stress response. BID is a pro-apoptotic member of the Bcl-2 family of proteins, which plays a pivotal role in the intrinsic pathway of apoptosis. Upon activation, BID is cleaved to form a truncated form known as tBID, which translocates to the mitochondria and facilitates the release of cytochrome c, ultimately leading to cell death. Understanding the mechanisms by which BID and its derivatives operate is essential for elucidating how cells balance survival and death in physiological and pathological conditions, including cancer, neurodegeneration, and ischemic injury. Researchers have increasingly focused on the recombinant expression of BID and tBID to study their structure-function relationships, binding affinities with other apoptotic regulators, and potential therapeutic applications. By generating and characterizing BID recombinant proteins, scientists aim to develop novel strategies for manipulating apoptosis in cancer therapies, promoting cell survival in neurodegenerative diseases, and enhancing protective mechanisms against cellular damage. The intricate interplay between BID and other apoptotic mediators highlights its significance as a target in drug design and provides valuable insights into the development of more effective treatment regimens aimed at diseases characterized by dysregulated apoptosis.
