Analytical Data
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Gene name
BID
- Application
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Alternative Names
BID；BH3-interacting domain death agonist
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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
P55957
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Expression Region
1-195aa
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AA Sequence
MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD
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Molecular Weight
38.0kDa
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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
BID (BH3-interacting domain death agonist) is a pro-apoptotic Bcl-2 family protein that plays a critical role in mediating apoptosis, particularly in response to cellular stress and various death signals. It functions as a molecular switch that helps to relay signals from other apoptotic stimuli to the mitochondrial pathway of programmed cell death. Upon activation, BID undergoes proteolytic cleavage, leading to the formation of tBID, which translocates to the mitochondria and triggers cytochrome c release, thereby activating downstream apoptotic cascades. Research into BID has gained traction due to its implications in cancer therapy, where its overexpression or loss can influence the efficacy of chemotherapeutic agents. Understanding the mechanisms of BID action can also illuminate its role in various diseases beyond cancer, including neurodegenerative disorders and immune responses. Recent studies have focused on elucidating the structural properties of BID as well as its interactions with other mitochondrial proteins, which could pave the way for novel therapeutic strategies that target apoptotic pathways for disease intervention. Understanding BID's dynamics, regulation, and interactions is essential for developing potential treatments aimed at controlling cell death in pathological conditions.
