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Recombinant Human OSCP1 protein

  • 中文名: 有机溶质载体伴侣1(OSCP1)重组蛋白
  • 别    名: OSCP1;C1orf102;NOR1;Protein OSCP1
货号: PA1000-8798
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点OSCP1
Uniprot No Q8WVF1
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-389aa
氨基酸序列MSVRTLPLLF LNLGGEMLYI LDQRLRAQNI PGDKARKDEW TEVDRKRVLN DIISTMFNRK FMEELFKPQE LYSKKALRTV YERLAHASIM KLNQASMDKL YDLMTMAFKY QVLLCPRPKD VLLVTFNHLD TIKGFIRDSP TILQQVDETL RQLTEIYGGL SAGEFQLIRQ TLLIFFQDLH IRVSMFLKDK VQNNNGRFVL PVSGPVPWGT EVPGLIRMFN NKGEEVKRIE FKHGGNYVPA PKEGSFELYG DRVLKLGTNM YSVNQPVETH VSGSSKNLAS WTQESIAPNP LAKEELNFLA RLMGGMEIKK PSGPEPGFRL NLFTTDEEEE QAALTRPEEL SYEVINIQAT QDQQRSEELA RIMGEFEITE QPRLSTSKGD DLLAMMDEL
预测分子量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.

参考文献

以下是基于OSCP1重组蛋白研究的模拟参考文献(内容为示例性概括):

1. **文献名称**:*Recombinant expression and functional characterization of OSCP1 subunit in mitochondrial ATP synthase*

**作者**:Kim J, et al.

**摘要**:本研究成功在大肠杆菌中表达并纯化了人源OSCP1重组蛋白,通过体外重组实验证实其在线粒体ATP合酶组装中的关键作用,并解析了其与F1亚基结合的分子机制。

2. **文献名称**:*Cryo-EM structure of OSCP1 in yeast ATP synthase reveals oligomycin resistance mechanism*

**作者**:Smith TL, et al.

**摘要**:利用冷冻电镜技术解析酵母OSCP1重组蛋白的精细结构,揭示了其与抑制剂寡霉素结合的构象变化,为抗真菌药物靶点设计提供结构基础。

3. **文献名称**:*OSCP1-mediated viral resistance in plants through recombinant protein overexpression*

**作者**:Chen W, et al.

**摘要**:通过农杆菌转化在拟南芥中过表达重组OSCP1蛋白,发现其显著增强植物对RNA病毒的抗性,可能与调控宿主细胞膜稳定性相关。

4. **文献名称**:*High-yield production of OSCP1 in Pichia pastoris and its immunogenicity analysis*

**作者**:Gómez-Ramos A, et al.

**摘要**:优化毕赤酵母系统实现OSCP1重组蛋白的高效分泌表达,并证明其作为抗寄生虫疫苗候选抗原可诱导小鼠产生特异性抗体应答。

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注:以上文献为示例性内容,实际研究中需根据具体课题补充真实文献。建议通过PubMed/Google Scholar以关键词"OSCP1 recombinant"+"expression"/"structure"/"function"检索最新论文。

背景信息

OSCP1 (Oligomycin Sensitivity-Conferring Protein 1) is a critical subunit of the mitochondrial F-type ATP synthase (Complex V), an enzyme essential for oxidative phosphorylation and ATP production in eukaryotic cells. This 20-23 kDa protein, encoded by the nuclear gene ATP5PO in humans, is a core component of the F1 sector of ATP synthase. OSCP1 plays a pivotal role in bridging the catalytic F1 head (where ATP synthesis occurs) and the membrane-embedded FO proton channel, facilitating energy transduction during proton gradient-driven rotation of the enzyme complex. Its name derives from conferring sensitivity to oligomycin, an antibiotic that inhibits ATP synthase by binding to the FO subunit.

Recombinant OSCP1 refers to the protein produced through genetic engineering techniques, typically expressed in heterologous systems like E. coli or yeast. This engineered version retains the functional properties of native OSCP1. including its ability to interact with other ATP synthase subunits and maintain structural integrity of the enzyme complex. Researchers utilize recombinant OSCP1 for structural studies (e.g., X-ray crystallography, cryo-EM), functional assays, and drug discovery targeting mitochondrial disorders. Its production enables detailed investigation of ATP synthase assembly, proton transport mechanisms, and energy conversion defects linked to neurodegenerative diseases, cancer, and metabolic syndromes.

Recent studies highlight OSCP1's emerging role beyond energy production, including mitochondrial permeability regulation and cellular stress responses. Recombinant variants with specific mutations help dissect its contributions to pathological conditions like Alzheimer's disease, where OSCP1 degradation correlates with synaptic dysfunction. This protein's recombinant form has become indispensable for developing therapies targeting mitochondrial bioenergetics and age-related metabolic decline.

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