| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ABCB7 |
| Uniprot No | O75027 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-752aa |
| 氨基酸序列 | MALLAMHSWRWAAAAAAFEKRRHSAILIRPLVSVSGSGPQWRPHQLGALGTARAYQIPESLKSITWQRLGKGNSGQFLDAAKALQVWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKEEERKKLQEEIVNSVKGCGNCSC |
| 预测分子量 | 82,6 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3篇关于ABCB7重组蛋白的研究文献摘要(基于公开信息整理，部分为虚构示例)：
---
1. **文献名称**: "Functional characterization of human ABCB7 in mitochondrial iron metabolism"
**作者**: Bekri S, et al.
**摘要**: 本研究通过重组表达人源ABCB7蛋白，证实其参与线粒体内铁硫簇的转运。实验显示ABCB7缺陷导致细胞线粒体铁蓄积，并伴随细胞色素C氧化酶活性下降，提示其与X连锁铁粒幼细胞性贫血的病理机制相关。
---
2. **文献名称**: "Cloning and expression analysis of ABCB7 in mammalian cells"
**作者**: Lill R, et al.
**摘要**: 作者利用哺乳动物表达系统重组表达了ABCB7蛋白，发现其定位于线粒体内膜。通过敲低实验表明，ABCB7通过调控谷胱甘肽代谢影响胞质铁硫蛋白的成熟，揭示了其在跨膜转运中的双重功能。
---
3. **文献名称**: "Structural insights into ABCB7 through cryo-EM analysis"
**作者**: Kim H, et al.
**摘要**: 本研究首次通过冷冻电镜解析了重组ABCB7蛋白的三维结构，揭示了其ATP结合域和跨膜区的构象变化，为理解其转运底物的分子机制及药物开发提供了结构基础。
---
注：以上文献为模拟示例，实际引用请通过PubMed或Google Scholar核实具体文献信息。
ABCB7. a member of the ATP-binding cassette (ABC) transporter superfamily, is a transmembrane protein involved in cellular transport processes. Predominantly localized to the inner mitochondrial membrane, it plays a critical role in iron homeostasis and iron-sulfur (Fe-S) cluster biogenesis. Fe-S clusters are essential cofactors for enzymes participating in electron transport, DNA repair, and metabolic pathways. ABCB7 facilitates the export of Fe-S clusters or a sulfur-containing component from mitochondria to the cytosol, ensuring their availability for cytosolic and nuclear enzymes.
Mutations in the ABCB7 gene are linked to X-linked sideroblastic anemia with ataxia (XLSA/A), a rare genetic disorder characterized by defective hemoglobin synthesis in red blood cells and neurological impairment. This connection underscores ABCB7’s importance in both hematological and neurological systems. Studies suggest ABCB7 interacts with components of the mitochondrial iron-sulfur machinery, such as glutaredoxin 5 (GLRX5), to maintain cellular iron balance and prevent toxic iron accumulation.
Recombinant ABCB7 protein, produced via heterologous expression systems (e.g., Escherichia coli, mammalian cells, or yeast), enables functional and structural studies. Its purification often involves affinity chromatography tags (e.g., His-tag) followed by biochemical characterization. Recombinant ABCB7 is used to investigate substrate specificity, ATPase activity, and molecular mechanisms underlying XLSA/A. Additionally, it serves as a tool for drug screening to identify compounds modulating Fe-S cluster transport or iron metabolism, with potential therapeutic applications for iron-related disorders.
Research on recombinant ABCB7 also contributes to understanding mitochondrial dysfunction in neurodegenerative diseases and cancer, where altered Fe-S cluster dynamics may play a role. Despite progress, unresolved questions remain about its exact transport substrates and regulatory networks, highlighting the need for further structural and functional analyses.
×
