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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | 4hbD |
| Uniprot No | Q63ZY3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-851aa |
| 氨基酸序列 | MAQVLHVPAPFPGTPGPASPPAFPAKDPDPPYSVETPYGYRLDLDFLKYVDDIEKGHTLRRVAVQRRPRLSSLPRGPGSWWTSTESLCSNASGDSRHSAYSYCGRGFYPQYGALETRGGFNPRVERTLLDARRRLEDQAATPTGLGSLTPSAAGSTASLVGVGLPPPTPRSSGLSTPVPPSAGHLAHVREQMAGALRKLRQLEEQVKLIPVLQVKLSVLQEEKRQLTVQLKSQKFLGHPTAGRGRSELCLDLPDPPEDPVALETRSVGTWVRERDLGMPDGEAALAAKVAVLETQLKKALQELQAAQARQADPQPQAWPPPDSPVRVDTVRVVEGPREVEVVASTAAGAPAQRAQSLEPYGTGLRALAMPGRPESPPVFRSQEVVETMCPVPAAATSNVHMVKKISITERSCDGAAGLPEVPAESSSSPPGSEVASLTQPEKSTGRVPTQEPTHREPTRQAASQESEEAGGTGGPPAGVRSIMKRKEEVADPTAHRRSLQFVGVNGGYESSSEDSSTAENISDNDSTENEAPEPRERVPSVAEAPQLRPAGTAAAKTSRQECQLSRESQHIPTAEGASGSNTEEEIRMELSPDLISACLALEKYLDNPNALTERELKVAYTTVLQEWLRLACRSDAHPELVRRHLVTFRAMSARLLDYVVNIADSNGNTALHYSVSHANFPVVQQLLDSGVCKVDKQNRAGYSPIMLTALATLKTQDDIETVLQLFRLGNINAKASQAGQTALMLAVSHGRVDVVKALLACEADVNVQDDDGSTALMCACEHGHKEIAGLLLAVPSCDISLTDRDGSTALMVALDAGQSEIASMLYSRMNIKCSFAPMSDDESPTSSSAEE |
| 预测分子量 | 91,1 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. |
以下是基于常见研究方向推测的3篇可能与“4HB重组蛋白”相关的参考文献示例(注：4hbD可能为术语简写或笔误，建议核实后调整检索关键词)：
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1. **文献名称**：*Design of a Four-Helix Bundle Protein for Molecular Delivery*
**作者**：Zhang Y, et al.
**摘要**：研究团队设计了一种基于四螺旋束(4HB)结构的重组蛋白，通过计算建模优化其稳定性，并在体外验证了其作为药物载体的负载能力，证明其在靶向递送中的潜在应用。
2. **文献名称**：*Expression and Characterization of Recombinant 4-Hydroxybenzoate Decarboxylase in E. coli*
**作者**：Smith J, et al.
**摘要**：报道了4-羟基苯甲酸脱羧酶(4-HBD)的重组表达工艺，通过大肠杆菌系统实现高效可溶性表达，并分析其酶动力学特性，为生物催化应用提供基础数据。
3. **文献名称**：*Self-Assembling 4HB Protein Nanocages for Gene Therapy*
**作者**：Lee S, et al.
**摘要**：开发了一种自组装的四螺旋束蛋白纳米笼结构，能够封装核酸分子，并在细胞实验中展示出低毒性和高转染效率，为基因递送提供新策略。
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**注意**：以上内容为基于领域知识的合理推测，若“4hbD”为特定蛋白缩写(如某专利名称或罕见变体)，建议通过学术数据库(如PubMed、Google Scholar)以精确关键词(如“4HB protein recombinant”或全称)检索最新文献。
**Background of 4HB Recombinant Protein**
The 4HB (four-helix bundle) recombinant protein is a structurally engineered biomolecule inspired by naturally occurring helical motifs critical for protein-protein interactions and stability. The 4HB fold, characterized by four α-helices arranged in a parallel or antiparallel coiled-coil configuration, is a conserved structural domain found in diverse proteins, including viral fusion peptides, cytokines, and transcription factors. Its compact, stable architecture makes it an attractive scaffold for biotechnological applications.
In virology, 4HB domains are central to viral entry mechanisms. For example, class I viral fusion proteins (e.g., HIV-1 gp41) utilize 4HB structures to mediate membrane fusion. This insight drove the design of recombinant 4HB-based inhibitors (e.g., T20/enfuvirtide) to block viral infection. Beyond antivirals, the 4HB motif is exploited in synthetic biology for engineering stable protein therapeutics, nanomaterials, or antigen-presenting platforms due to its modularity and thermal stability.
Recombinant 4HB proteins are typically produced via heterologous expression in *E. coli* or mammalian systems, followed by purification using affinity chromatography. Structural optimization (e.g., helix stabilization via hydrophobic core engineering) enhances functionality. Current research focuses on tailoring 4HB proteins for drug delivery, vaccine design, or as diagnostic tools. For instance, 4HB-based vaccines targeting respiratory syncytial virus (RSV) or coronaviruses leverage the domain’s ability to present conformational epitopes, eliciting potent neutralizing antibodies.
The 4HB recombinant protein exemplifies structure-driven bioengineering, merging biophysical insights with therapeutic innovation. Its versatility continues to expand applications in targeted therapy and synthetic biology.
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