纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | OGC |
Uniprot No | Q02978 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-314aa |
氨基酸序列 | MAATASAGAGGIDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQ LSGEGAKTREYKTSFHALTSILKAEGLRGIYTGLSAGLLRQATYTTTRLG IYTVLFERLTGADGTPPGFLLKAVIGMTAGATGAFVGTPAEVALIRMTAD GRLPADQRRGYKNVFNALIRITREEGVLTLWRGCIPTMARAVVVNAAQLA SYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIAKTRIQNM RMIDGKPEYKNGLDVLFKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFL EQMNKAYKRLFLSG |
预测分子量 | 60 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OGC(假设为有机阴离子转运蛋白相关重组蛋白)重组蛋白研究的虚构示例参考文献(仅供示例参考,非真实文献):
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1. **文献名称**:Optimized Expression and Purification of Recombinant OGC Protein in E. coli
**作者**:Zhang L., et al.
**摘要**:本研究通过优化大肠杆菌表达系统的质粒设计和培养条件,成功实现OGC重组蛋白的高效可溶性表达,并利用亲和层析技术纯化获得高纯度蛋白,为后续功能研究奠定基础。
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2. **文献名称**:Structural Insights into OGC-Mediated Substrate Transport by Cryo-EM
**作者**:Tanaka K., et al.
**摘要**:通过冷冻电镜技术解析了OGC重组蛋白的三维结构,揭示了其底物结合口袋的关键氨基酸残基,阐明了其转运有机阴离子的分子机制。
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3. **文献名称**:Functional Characterization of OGC Recombinant Protein in Drug Delivery Systems
**作者**:Gupta R., Patel S.
**摘要**:利用体外细胞模型验证了OGC重组蛋白在增强药物跨膜转运中的功能,证明其可作为靶向递送抗肿瘤药物的潜在载体。
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4. **文献名称**:Role of OGC in Mitochondrial Membrane Dynamics: A Recombinant Protein Study
**作者**:Müller J., et al.
**摘要**:通过重组OGC蛋白与线粒体膜蛋白的相互作用实验,发现OGC在调控线粒体阴离子平衡和膜电位稳定性中起关键作用。
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**注意**:以上文献为模拟示例,实际研究中建议通过PubMed、Web of Science或Google Scholar等平台,以关键词“OGC recombinant protein”“organic anion transporter recombinant”等检索真实文献。若OGC指代其他特定蛋白(如某基因缩写),需结合具体背景调整检索策略。
**Background of Recombinant Proteins (OGC Context)**
Recombinant proteins are engineered through recombinant DNA technology, enabling the production of specific proteins by inserting target genes into host organisms (e.g., bacteria, yeast, or mammalian cells). This approach revolutionized biotechnology since its inception in the 1970s, offering scalable and precise methods to synthesize proteins for research, therapeutics, and industrial applications.
In the context of the **OGC (COVID-19-related example)**, recombinant protein technology gained prominence during the pandemic for developing vaccines. For instance, Novavax’s COVID-19 vaccine utilizes a recombinant spike protein of SARS-CoV-2. produced in insect cells, to elicit immune responses. Such proteins mimic viral antigens without containing live virus, ensuring safety and facilitating rapid adaptation to emerging variants.
Beyond vaccines, recombinant proteins are pivotal in treating diseases like diabetes (insulin), cancer (monoclonal antibodies), and rare genetic disorders (enzyme replacement therapies). They also serve as critical tools in diagnostics (e.g., ELISA kits) and biomedical research to study protein functions.
Production involves cloning genes into expression vectors, optimizing host systems for high yield, and purifying proteins to meet clinical standards. Challenges include ensuring proper post-translational modifications (e.g., glycosylation) in eukaryotic systems and minimizing immunogenicity.
Advancements in synthetic biology and CRISPR-based genome editing continue to refine recombinant protein platforms, enhancing efficiency and broadening applications. As a cornerstone of modern biotechnology, recombinant proteins remain essential in addressing global health challenges and driving innovation across sectors.
*(Note: OGC is interpreted here in a COVID-19 vaccine context for illustrative purposes; adjust specifics based on intended focus.)*
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