Analytical Data
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Gene name
BAD
- Application
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Alternative Names
BAD；BBC6；BCL2L8；Bcl2-associated agonist of cell death
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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
Q92934
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Expression Region
1-168aa
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AA Sequence
MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH QQEQPTSSSH HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA PPNLWAAQRY GRELRRMSDE FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV FQSWWDRNLG RGSSAPSQ
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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
BAD (Bcl-2-associated agonist of cell death) protein is a critical regulator of apoptosis, functioning as a pro-apoptotic member of the Bcl-2 protein family. Its expression and activity are pivotal in maintaining cellular homeostasis, particularly in response to stress signals. Research into the BAD protein has gained momentum due to its implications in various pathological conditions, including cancer, neurodegenerative diseases, and heart diseases, where dysregulation of apoptosis contributes to disease progression. The understanding of BAD's role in intrinsic apoptotic pathways has opened avenues for targeted therapies aimed at modulating its function, either to promote cell death in cancer cells or to inhibit apoptosis in degenerative diseases. Furthermore, BAD interacts with other key molecules in the apoptosis cascade, influencing cellular responses to growth factors and environmental stresses. Advances in recombinant technology have enabled the production of purified BAD protein, facilitating studies on its structural and functional properties. Elucidating the precise mechanisms by which BAD modulates apoptosis, and its interactions with other apoptotic regulators, is essential for developing strategies to manipulate its activity in therapeutic contexts. Overall, the ongoing exploration of BAD and its potential for therapeutic intervention underscores its significance in cellular biology and disease treatment strategies.
