纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | VDAC1 |
Uniprot No | P21796 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-283aa |
氨基酸序列 | MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTE TTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFD SSFSPNTGKKNAKIKTGYKREHINLGCDMDFDIAGPSIRGALVLGYEGWL AGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNK KLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQT LKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA |
预测分子量 | 57 kDa |
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VDAC1重组蛋白的3篇参考文献及其摘要概括:
1. **《Recombinant human VDAC1: overexpression in E. coli, purification, and functional characterization》**
*作者:Shoshan-Barmatz V, et al.*
**摘要**:研究报道了在大肠杆菌中高效表达重组人源VDAC1蛋白的方法,通过亲和层析纯化获得高纯度蛋白,并验证其形成功能性通道的能力,证实其在线粒体膜上的阴离子选择性及电压依赖性。
2. **《Structural and functional analysis of the recombinant voltage-dependent anion channel 1 (VDAC1)》**
*作者:Ujwal R, et al.*
**摘要**:利用X射线晶体学解析了重组VDAC1的原子结构,揭示了其β-桶状构象及潜在的调控位点,为理解VDAC1在代谢物转运和细胞凋亡中的作用提供了结构基础。
3. **《VDAC1 recombinant protein interaction with tubulin modulates mitochondrial membrane permeability》**
*作者:Maldonado EN, et al.*
**摘要**:通过体外实验证明重组VDAC1蛋白与微管蛋白的相互作用可调控线粒体膜通透性,影响细胞能量代谢和凋亡信号通路,提示其在癌症治疗中的潜在靶点价值。
4. **《Reconstitution of recombinant VDAC1 into lipid bilayers for electrophysiological characterization》**
*作者:Rostovtseva TK, et al.*
**摘要**:研究将重组VDAC1蛋白成功重构至人工脂质双层中,通过电生理记录分析其通道特性,发现其通透性受膜电位和ATP浓度调节,为研究线粒体代谢调控机制提供了模型系统。
(注:以上文献信息为示例,实际引用时建议通过学术数据库核对准确信息。)
Voltage-Dependent Anion Channel 1 (VDAC1), a major pore-forming protein in the mitochondrial outer membrane, regulates the cross-membrane transport of metabolites, ions, and nucleotides, serving as a critical gateway for mitochondrial-nuclear communication. As the most abundant isoform of the VDAC family, it governs cellular energy metabolism by facilitating ATP/ADP exchange and modulating calcium signaling. Structurally, VDAC1 adopts a β-barrel conformation with 19 transmembrane β-strands and an N-terminal α-helix that dynamically regulates channel permeability. Its activity is modulated by post-translational modifications, including phosphorylation and acetylation, as well as interactions with apoptosis-related proteins like Bcl-2 family members.
Recombinant VDAC1 protein, typically expressed in bacterial (E. coli) or eukaryotic systems, enables structural and functional studies of this channel protein. Purification strategies often incorporate affinity tags (e.g., His-tag) followed by ion-exchange chromatography. The recombinant form has been instrumental in resolving VDAC1's 3D structure through NMR and X-ray crystallography, revealing voltage-gating mechanisms and interaction sites for metabolic enzymes like hexokinase.
Research highlights VDAC1's dual role in cell survival and death: it maintains metabolic homeostasis under normal conditions but participates in apoptotic signaling through cytochrome c release during stress. Dysregulation of VDAC1 is implicated in cancer (metabolic reprogramming), neurodegenerative diseases (mitochondrial dysfunction), and cardiovascular disorders. Recent studies explore its potential as a therapeutic target, with recombinant VDAC1 serving as a platform for screening channel modulators and investigating pathological protein interactions (e.g., amyloid-β in Alzheimer's). Current challenges in recombinant applications include maintaining native conformation and resolving oligomerization effects on channel properties.
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