| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | HA-33 |
| Uniprot No | P0DPR0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-286aa |
| 氨基酸序列 | SQTNANDLRNNEVFFISPSNNTNKVLDKISQSEVKLWNKLSGANQKWRLIYDTNKQAYKIKVMDNTSLILTWNAPLSSVSVKTDTNGDNQYWYLLQNYISRNVIIRNYMNPNLVLQYNIDDTLMVSTQTSSSNQFFKFSNCIYEALNNRNCKLQTQLNSDRFLSKNLNSQIIVLWQWFDSSRQKWIIEYNETKSAYTLKCQENNRYLTWIQNSNNYVETYQSTDSLIQYWNINYLDNDASKYILYNLQDTNRVLDVYNSQIANGTHVIVDSYHGNTNQQWIINLI |
| 预测分子量 | 53.6 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. |
以下是关于HA-33重组蛋白的3篇代表性文献的简要总结(基于公开研究背景模拟，非真实文献)：
1. **文献名称**：*Structural characterization of recombinant HA-33 from Clostridium botulinum*
**作者**：Kukreja R, Singh BR
**摘要**：通过X射线晶体学解析了重组HA-33蛋白的三维结构，揭示了其与肠道上皮细胞表面糖链结合的潜在机制，为开发抑制肉毒毒素吸收的抑制剂提供依据。
2. **文献名称**：*Recombinant HA-33 as a carrier for oral vaccine delivery*
**作者**：Arimitsu H, Lee JC, Sakaguchi Y
**摘要**：研究利用重组HA-33蛋白的靶向黏附特性，将其作为口服疫苗载体，在小鼠模型中成功增强抗原的肠道递送效率，并诱导黏膜免疫应答。
3. **文献名称**：*Functional analysis of HA-33 in the hemagglutinin complex of botulinum toxin*
**作者**：Fujinaga Y, Matsumura T, Jin Y
**摘要**：通过体外细胞模型证明重组HA-33蛋白与HA-17形成的复合物可保护肉毒毒素在胃酸环境中的稳定性，并促进毒素跨肠上皮屏障的转运。
如需具体文献，建议通过PubMed或Google Scholar以关键词“recombinant HA-33 botulinum”检索近年研究。
HA-33 recombinant protein is a component derived from the hemagglutinin (HA) complex of *Clostridium botulinum*, a bacterium producing the potent botulinum neurotoxin (BoNT). The HA complex, comprising HA-17. HA-33. and HA-70 subunits, plays a critical role in stabilizing BoNT and facilitating its absorption across the intestinal epithelium during infection. HA-33. the largest subunit, is particularly notable for its carbohydrate-binding activity. It recognizes and binds to glycans on host cell surfaces, such as those containing N-acetylneuraminic acid (sialic acid), enabling the toxin complex to adhere to intestinal cells and penetrate the mucosal barrier.
Recombinant HA-33 is produced using genetic engineering techniques, often expressed in *Escherichia coli* or other microbial systems, followed by purification. Its study provides insights into the molecular mechanisms of botulism, particularly how BoNT survives the harsh gastrointestinal environment and enters the bloodstream. Structurally, HA-33 adopts a β-trefoil fold, a common motif in carbohydrate-binding proteins, which underpins its glycan receptor specificity.
Research on HA-33 has applications in both therapeutics and biotechnology. It serves as a model for understanding bacterial pathogenesis and host-pathogen interactions. Additionally, its lectin-like properties are explored for targeted drug delivery systems or as a tool in glycobiology studies. HA-33’s role in enhancing BoNT oral toxicity also makes it a potential target for antitoxin strategies or vaccine development. Overall, HA-33 recombinant protein is a key molecule for unraveling botulism pathology and engineering novel biomedical solutions.
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