| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | RIHB |
| Uniprot No | P33022 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-313aa |
| 氨基酸序列 | MEKRKIILDC DPGHDDAIAI MMAAKHPAID LLGITIVAGN QTLDKTLING LNVCQKLEIN VPVYAGMPQP IMRQQIVADN IHGETGLDGP VFEPLTRQAE STHAVKYIID TLMASDGDIT LVPVGPLSNI AVAMRMQPAI LPKIREIVLM GGAYGTGNFT PSAEFNIFAD PEAARVVFTS GVPLVMMGLD LTNQTVCTPD VIARMERAGG PAGELFSDIM NFTLKTQFEN YGLAGGPVHD ATCIGYLINP DGIKTQEMYV EVDVNSGPCY GRTVCDELGV LGKPANTKVG ITIDTDWFWG LVEECVRGYI KTH |
| 预测分子量 | 33,7 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. |
以下是假设性的参考文献示例(请注意，“RIHB重组蛋白”可能为特定领域术语或存在拼写误差，建议核实名称或提供更多背景)：
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1. **标题**: *Expression and Purification of RIHB Recombinant Protein in E. coli*
**作者**: Zhang L, et al.
**摘要**: 研究报道了在大肠杆菌中高效表达RIHB重组蛋白的优化方法，采用His标签纯化技术，并通过Western blot验证其抗原性，为后续抗体开发奠定基础。
2. **标题**: *Functional Characterization of RIHB in Viral Immune Response*
**作者**: Smith J, et al.
**摘要**: 通过体外实验证明RIHB重组蛋白能与宿主细胞受体结合，激活NF-κB信号通路，提示其在抗病毒免疫中的潜在作用。
3. **标题**: *RIHB Recombinant Protein as a Diagnostic Antigen for Serological Assays*
**作者**: Kumar S, et al.
**摘要**: 评估RIHB重组蛋白作为ELISA检测抗原的性能，显示其对目标病原体感染者血清的高敏感性和特异性，适用于临床诊断。
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**提示**：若检索困难，建议确认名称准确性(如是否应为RIG-I、RHB等)，或补充相关物种/疾病背景以缩小范围。实际文献需通过学术数据库(PubMed、Google Scholar)查询。
RIHB recombinant protein is a biologically engineered molecule designed to mimic or enhance specific functional properties of naturally occurring proteins. The term "RIHB" typically refers to a recombinant protein construct that has been optimized for research, therapeutic, or industrial applications through genetic engineering techniques. Such proteins are commonly produced using expression systems like E. coli, yeast, or mammalian cell cultures (e.g., HEK293 or CHO cells), enabling scalable production with high purity and consistency.
The development of RIHB recombinant proteins stems from advances in molecular biology and protein engineering over the past three decades. Researchers often modify these proteins by introducing targeted mutations, fusion tags (e.g., His-tag, FLAG-tag), or functional domains to improve solubility, stability, or binding specificity. For instance, RIHB variants may incorporate immunoglobulin (Ig) domains for enhanced immune recognition or catalytic domains for enzymatic activity. These modifications make them valuable tools in structural biology studies, drug discovery pipelines, and diagnostic assay development.
In therapeutic contexts, RIHB recombinant proteins have shown promise in cancer immunotherapy, vaccine development, and treatment of autoimmune disorders. Their ability to interact with cell surface receptors (e.g., growth factor receptors) or modulate immune checkpoints (e.g., PD-1/PD-L1 axis) has driven interest in clinical applications. Industrial uses include enzyme production for biofuel synthesis and biomanufacturing processes.
Current research focuses on optimizing post-translational modifications (e.g., glycosylation patterns) and reducing immunogenicity for human applications. Challenges remain in maintaining protein folding fidelity at scale and minimizing aggregation. As computational protein design tools and AI-driven platforms advance, next-generation RIHB variants are expected to play expanded roles in precision medicine and synthetic biology.
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