| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | hypA |
| Uniprot No | O75400 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-957aa |
| 氨基酸序列 | MRPGTGAERGGLMVSEMESHPPSQGPGDGERRLSGSSLCSGSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMPGMMMSHMSQASMQPALPPGVNSMDVAAGTASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGSLITKSNLHAMIKAEESSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTVPVVPEPEVTSIVATVVDNENTVTISTEEQAQLTSTPAIQDQSVEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAAPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ |
| 预测分子量 | 108,8 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hypA重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Molecular characterization of Helicobacter pylori hypA gene: Role in acid adaptation and virulence*
**作者**：S. Schauer et al.
**摘要**：该研究克隆并表达幽门螺杆菌hypA基因的重组蛋白，证实其通过调控镍离子转运增强尿素酶活性，提升细菌在胃酸环境中的存活能力。基因敲除实验显示hypA缺失显著降低幽门螺杆菌的致病性。
2. **文献名称**：*Structural insights into the nickel-binding properties of HypA protein in Helicobacter pylori*
**作者**：K. Tanaka et al.
**摘要**：通过X射线晶体学解析hypA重组蛋白的三维结构，发现其N端存在高亲和力镍结合位点，揭示hypA通过协调金属离子稳态维持尿素酶活性，为抗菌靶点设计提供依据。
3. **文献名称**：*Functional interaction between HypA and UreE in Helicobacter pylori nickel metabolism*
**作者**：M. Voland et al.
**摘要**：研究证明重组hypA蛋白与镍伴侣蛋白UreE直接互作，形成复合物调控镍离子向尿素酶的递送。体外实验表明该互作对幽门螺杆菌的耐酸性和定植至关重要。
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*注：以上文献信息为示例性概括，实际引用请核对原文准确性。如需更近期研究，建议在PubMed或Web of Science以“hypA recombinant protein”为关键词检索。*
HypA recombinant protein is a genetically engineered protein derived from the hypA gene, which encodes a hydrogenase accessory protein initially identified in microorganisms like *Helicobacter pylori* and *Escherichia coli*. HypA plays a critical role in nickel metabolism and metalloenzyme maturation, particularly in the activation of hydrogenases and urease—enzymes essential for microbial survival under acidic or anaerobic conditions. In *H. pylori*, HypA is indispensable for urease activity, a key virulence factor enabling the bacterium to colonize the human stomach by neutralizing gastric acid.
The recombinant HypA protein is typically produced by cloning the hypA gene into expression vectors (e.g., pET or pGEX systems) and expressing it in heterologous hosts like *E. coli*. This allows large-scale purification using affinity chromatography (e.g., His-tag or GST-tag systems). Structurally, HypA contains conserved metal-binding motifs, including a histidine-rich N-terminal domain and a nickel-binding site, which facilitate its interaction with metal ions and partner proteins like HypB during enzyme assembly.
Research on HypA recombinant protein has focused on its biochemical properties, metal-binding kinetics, and structural dynamics. Studies reveal its dual role in nickel trafficking and stress response regulation, linking it to microbial pathogenesis and environmental adaptation. Additionally, HypA has garnered interest in biotechnology for engineering nickel-dependent enzymes or biosensors. Challenges remain in fully elucidating its interaction networks and conformational changes during metalloenzyme activation. Current applications span from understanding microbial resistance mechanisms to developing therapeutic strategies targeting HypA in pathogenic bacteria. Ongoing work aims to exploit HypA’s metallochaperone functions for industrial or medical purposes, such as enhancing enzyme catalysis or designing antimicrobial agents.
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