| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Hyp |
| Uniprot No | P78562 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-749aa |
| 氨基酸序列 | MEAETGSSVETGKKANRGTRIALVVFVGGTLVLGTILFLVSQGLLSLQAKQEYCLKPECIEAAAAILSKVNLSVDPCDNFFRFACDGWISNNPIPEDMPSYGVYPWLRHNVDLKLKELLEKSISRRRDTEAIQKAKILYSSCMNEKAIEKADAKPLLHILRHSPFRWPVLESNIGPEGVWSERKFSLLQTLATFRGQYSNSVFIRLYVSPDDKASNEHILKLDQATLSLAVREDYLDNSTEAKSYRDALYKFMVDTAVLLGANSSRAEHDMKSVLRLEIKIAEIMIPHENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVIDTRLYPHLKDISPSENVVVRVPQYFKDLFRILGSERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLLPQWDKCVNFIESALPYVVGKMFVDVYFQEDKKEMMEELVEGVRWAFIDMLEKENEWMDAGTKRKAKEKARAVLAKVGYPEFIMNDTHVNEDLKAIKFSEADYFGNVLQTRKYLAQSDFFWLRKAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFWGTEYPRSLSYGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKCMINQYSNYYWKKAGLNVKGKRTLGENIADNGGLREAFRAYRKWINDRRQGLEEPLLPGITFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAFNCPPNSTMNRGMDSCRLW |
| 预测分子量 | 86,4 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Hyp重组蛋白的3篇参考文献示例(注：以下内容为虚构示例，实际文献需通过学术数据库查询)：
1. **文献名称**：*Enhanced Hyp Recombinant Collagen Production in E. coli via Co-expression of Prolyl Hydroxylase*
**作者**：Smith A, et al.
**摘要**：研究通过在大肠杆菌中共表达脯氨酰羟化酶，成功实现羟脯氨酸(Hyp)修饰的重组胶原蛋白高效表达，并证明其结构稳定性优于未修饰蛋白，适用于生物材料领域。
2. **文献名称**：*High-yield Hyp-containing Recombinant Gelatin Production in Pichia pastoris*
**作者**：Lee J, et al.
**摘要**：利用毕赤酵母表达系统生产高羟脯氨酸含量的重组明胶，通过优化培养条件提高Hyp修饰效率，所得产物在药物缓释载体中展现优异性能。
3. **文献名称**：*Plant-based Transient Expression System for Hyp-modified Therapeutic Proteins*
**作者**：Zhang Y, et al.
**摘要**：开发了一种基于植物瞬时表达的技术，低成本生产含Hyp的重组蛋白，应用于组织工程和疫苗开发，证实其生物活性与哺乳动物细胞来源相当。
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**提示**：实际文献建议通过PubMed、Web of Science等平台检索关键词“recombinant hydroxyproline protein”或结合具体应用方向(如胶原蛋白、药物递送)获取。
**Background of Hyp Recombinant Proteins**
Hyp (hydroxyproline)-recombinant proteins are engineered biomolecules that incorporate hydroxyproline, a post-translationally modified amino acid critical for stabilizing collagen-like structures and modulating protein function. Hydroxyproline is not directly encoded by DNA but is formed via the hydroxylation of proline residues catalyzed by prolyl hydroxylases, a process often dependent on oxygen and iron availability. This modification is particularly abundant in collagen, where it enhances structural integrity and influences interactions in extracellular matrices.
Recombinant proteins containing hydroxyproline are typically produced using heterologous expression systems, such as *E. coli*, yeast, or mammalian cells. However, achieving proper hydroxyproline incorporation poses challenges. Prokaryotic systems lack endogenous hydroxylation machinery, necessitating co-expression of hydroxylase enzymes or chemical modification post-production. Eukaryotic systems, like CHO cells, naturally perform hydroxylation but may require optimization for high-yield Hyp-protein synthesis.
These proteins hold significant biomedical relevance. Hyp-rich domains are crucial in designing synthetic collagens, wound-healing scaffolds, and drug delivery vehicles. They also serve as tools to study hypoxia-responsive pathways, such as HIF-1α regulation, due to hydroxyproline’s role in oxygen sensing. Additionally, Hyp-modified recombinant therapeutics, including antibody-drug conjugates or engineered growth factors, benefit from enhanced stability and targeted bioactivity.
Despite advances, scalable production remains a hurdle, balancing cost, yield, and post-translational fidelity. Innovations in synthetic biology, such as engineered hydroxylase pathways and *in vitro* enzymatic systems, aim to address these limitations, expanding Hyp-recombinant protein applications in regenerative medicine and biopharmaceuticals.
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