| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HEPH |
| Uniprot No | Q9BQS7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1158aa |
| 氨基酸序列 | MESGHLLWALLFMQSLWPQLTDGATRVYYLGIRDVQWNYAPKGRNVITNQPLDSDIVASSFLKSDKNRIGGTYKKTIYKEYKDDSYTDEVAQPAWLGFLGPVLQAEVGDVILIHLKNFATRPYTIHPHGVFYEKDSEGSLYPDGSSGPLKADDSVPPGGSHIYNWTIPEGHAPTDADPACLTWIYHSHVDAPRDIATGLIGPLITCKRGALDGNSPPQRQDVDHDFFLLFSVVDENLSWHLNENIATYCSDPASVDKEDETFQESNRMHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISCQVNSHFRDGMQALYKVKSCSMAPPVDLLTGKVRQYFIEAHEIQWDYGPMGHDGSTGKNLREPGSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHLEEDRHLGILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGLVAKPFEKVTYRWTVPPHAGPTAQDPACLTWMYFSAADPIRDTNSGLVGPLLVCRAGALGADGKQKGVDKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDVHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNVSQCPGHQATPRQRYQAARIYYIMAEEVEWDYCPDRSWEREWHNQSEKDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEHLGILGPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTVWPLAAEPGEVVTYQWNIPERSGPGPNDSACVSWIYYSAVDPIKDMYSGLVGPLAICQKGILEPHGGRSDMDREFALLFLIFDENKSWYLEENVATHGSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVDLHTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTVFSRTEHLSPLTVITKETEKAVPPRDIEEGNVKMLGMQIPIKNVEMLASVLVAISVTLLLVVLALGGVVWYQHRQRKLRRNRRSILDDSFKLLSFKQ |
| 预测分子量 | 130,4 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HEPH重组蛋白的3篇参考文献及其摘要概括：
1. **《Recombinant Hephaestin Expressed in HEK293 Cells Exhibits Ferroxidase Activity》**
- 作者：Chen, H.; Vulpe, C.D.
- 摘要：研究报道了在HEK293细胞中成功重组表达HEPH蛋白，并证实其具有亚铁氧化酶活性，揭示了HEPH在肠道铁转运中的关键作用。
2. **《Structural and Functional Analysis of the Ferroxidase Domain of Hephaestin》**
- 作者：Wyman, S.; et al.
- 摘要：通过重组表达HEPH的亚铁氧化酶结构域，分析了其晶体结构和催化机制，发现其与铜蓝蛋白的结构差异可能导致功能特异性。
3. **《Hephaestin Gene Knockout in Mice Alters Iron Homeostasis: Insights from Recombinant Protein Rescue Experiments》**
- 作者：Anderson, G.J.; et al.
- 摘要：利用重组HEPH蛋白在小鼠模型中恢复铁代谢功能，证明HEPH缺陷导致肠道铁吸收障碍，重组蛋白可部分逆转表型。
(注：以上文献为示例，实际引用时请核实真实存在的论文信息。)
**Background of HEPH Recombinant Protein**
The HEPH (hephaestin) protein is a multicopper ferroxidase critical for cellular iron homeostasis, primarily known for its role in intestinal iron absorption and systemic iron transport. Initially identified through studies on iron metabolism defects, hephaestin shares structural and functional homology with ceruloplasmin, another ferroxidase. It facilitates the oxidation of Fe²⁺ to Fe³⁺, enabling iron binding to transferrin for circulation. Mutations or dysregulation of HEPH are linked to iron-related disorders, such as anemia and neurodegenerative diseases.
Recombinant HEPH protein is produced using biotechnological platforms (e.g., mammalian or bacterial expression systems) to express and purify the protein for research and therapeutic applications. Its recombinant form allows detailed study of iron-handling mechanisms, interactions with other proteins (e.g., ferroportin), and potential therapeutic targeting for iron metabolism imbalances. Structural studies of recombinant HEPH highlight conserved copper-binding domains and a transmembrane region essential for its enzymatic activity and cellular localization.
Research on HEPH recombinant protein has expanded into cancer biology, as iron dysregulation is a hallmark of tumor progression. It also aids in developing diagnostic tools for iron deficiency and overload syndromes. Despite advances, challenges remain in optimizing its stability and activity in vitro, driving ongoing engineering efforts to enhance its functional mimicry of endogenous hephaestin.
In summary, recombinant HEPH serves as a vital tool for deciphering iron-related pathways and designing interventions for diseases rooted in iron homeostasis disruption.
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