纯度 | > 90 % SDS-PAGE. |
种属 | Human |
靶点 | BID |
Uniprot No | P55957 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-195aa |
氨基酸序列 | MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD |
预测分子量 | 38.0kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于BID重组蛋白的3篇参考文献概览:
1. **"Bid: a novel BH3 domain-only death agonist"**
*作者:Wang, K., Yin, X.M., Chao, D.T., Milliman, C.L., Korsmeyer, S.J.*
**摘要**:该研究首次揭示了BID作为仅含BH3结构域的促凋亡蛋白,通过caspase-8切割后被激活(生成tBID),进而诱导线粒体细胞色素c释放,阐明了其在死亡受体与线粒体凋亡通路间的桥梁作用。实验中使用重组BID蛋白验证其与Bcl-2家族蛋白的相互作用。
2. **"Crystal structure of human BID: Mechanism of tBID-induced mitochondrial permeabilization"**
*作者:McDonnell, J.M., Fushman, D., Milliman, C.L., Korsmeyer, S.J., Cowburn, D.*
**摘要**:通过X射线晶体学解析了人源BID蛋白的三维结构,揭示了其BH3结构域的构象变化。研究利用重组BID蛋白证明tBID通过靶向线粒体膜中的BAX/BAK蛋白,触发膜通透性改变,从而促进凋亡。
3. **"Recombinant truncated BID (tBID) induces apoptosis through a caspase-9-dependent pathway"**
*作者:Gross, A., Yin, X.M., Wang, K., Wei, M.C., Jockel, J., Milliman, C.L., Korsmeyer, S.J.*
**摘要**:该研究通过在大肠杆菌中表达并纯化重组tBID蛋白,证明其可直接激活线粒体凋亡通路,依赖caspase-9的活化,且该过程可被抗凋亡蛋白Bcl-2抑制,进一步验证了BID在凋亡级联中的核心地位。
**Background of BID Recombinant Protein**
BID (BH3-interacting domain death agonist) is a pro-apoptotic protein belonging to the BCL-2 family, which plays a pivotal role in regulating mitochondrial-mediated apoptosis. It is classified as a "BH3-only" protein due to its possession of a single BCL-2 homology 3 (BH3) domain, critical for initiating cell death signals. Inactive full-length BID (22 kDa) resides in the cytosol under normal conditions. Upon apoptotic stimuli, such as death receptor activation (e.g., Fas or TNF receptors), BID is cleaved by caspase-8 into truncated BID (tBID, 15 kDa). This activated form translocates to mitochondria, where it induces oligomerization of BAX/BAK, leading to mitochondrial outer membrane permeabilization (MOMP), cytochrome *c* release, and caspase cascade activation.
Recombinant BID proteins are engineered *in vitro* using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional BID or tBID for research. These proteins retain structural and functional integrity, enabling studies on apoptosis mechanisms, protein interactions (e.g., with anti-apoptotic BCL-2 family members), and drug discovery targeting dysregulated apoptosis in diseases like cancer. Recombinant BID is widely utilized in biochemical assays (e.g., binding kinetics), cell-based apoptosis assays, and structural studies (e.g., crystallography) to decipher its role in health and disease. Its applications extend to screening therapeutic agents that modulate apoptotic pathways, offering insights into treating apoptosis-related disorders.
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