| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | P4Ha1 |
| Uniprot No | P13674 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-534aa |
| 氨基酸序列 | MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEE DKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELEN LVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISK GNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEIS TIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEY IMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIE IVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMR IQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRI ATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRH AACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE |
| 预测分子量 | 85 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P4HA1重组蛋白的3篇参考文献，按文献名称、作者及摘要内容概括整理：
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1. **文献名称**：*Recombinant Human Prolyl 4-Hydroxylase Subunit Alpha 1 (P4HA1) Expression and Characterization in E. coli*
**作者**：Zhang Y, et al.
**摘要**：本研究报道了人源P4HA1重组蛋白在大肠杆菌中的高效表达及纯化方法，分析了其酶活性和热稳定性，证实重组蛋白在体外可有效催化胶原样肽链的脯氨酸羟基化。
2. **文献名称**：*Functional Analysis of P4HA1 in Collagen Maturation Using a Recombinant Protein Model*
**作者**：Smith J, et al.
**摘要**：通过构建重组P4HA1蛋白，研究其在胶原三螺旋结构形成中的作用，发现其羟基化活性对胶原纤维的机械强度和细胞外基质的完整性至关重要。
3. **文献名称**：*Development of a P4HA1-Deficient Cell Line Rescued by Recombinant P4HA1: Implications for Fibrosis Therapy*
**作者**：Chen L, et al.
**摘要**：利用重组P4HA1蛋白恢复缺陷细胞的胶原合成能力，证明其可能作为纤维化疾病的治疗靶点，并验证了重组蛋白在调节病理胶原沉积中的潜力。
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**备注**：上述文献为示例性质，实际文献需通过数据库(如PubMed、Web of Science)检索确认。建议结合具体研究方向补充关键词(如“重组表达”、“酶活性”、“疾病应用”)以获取更精准的参考文献。
**Background of P4Ha1 Recombinant Protein**
Prolyl 4-hydroxylase alpha 1 (P4HA1) is a critical enzyme involved in the post-translational modification of collagen, a major structural protein in the extracellular matrix. It catalyzes the hydroxylation of proline residues in collagen chains, a process essential for stabilizing the triple-helical structure of procollagen, ensuring its thermal stability and proper folding. This enzymatic activity is vital for maintaining tissue integrity, wound healing, and developmental processes.
P4HA1 functions as part of a heterotetrameric complex, comprising two alpha subunits (P4HA1) and two beta subunits (protein disulfide isomerase, PDI). The alpha subunit harbors the catalytic domain responsible for hydroxylation, while the beta subunit facilitates complex assembly and stability. Dysregulation of P4HA1 has been implicated in fibrotic diseases, cancer progression, and connective tissue disorders, where abnormal collagen deposition or remodeling occurs.
Recombinant P4HA1 protein is engineered for research and therapeutic applications. It is typically produced using heterologous expression systems, such as *E. coli* or mammalian cells, to ensure proper folding and enzymatic activity. Researchers utilize recombinant P4HA1 to study collagen biosynthesis mechanisms, screen inhibitors for antifibrotic drug development, or model diseases linked to collagen dysfunction.
In cancer biology, P4HA1 overexpression is associated with tumor metastasis and poor prognosis, as hydroxylated collagen promotes a stiff tumor microenvironment conducive to invasion. Consequently, targeting P4HA1 has emerged as a strategy to disrupt tumor-stroma interactions. Additionally, recombinant P4HA1 aids in tissue engineering by optimizing collagen matrices for regenerative medicine.
Overall, P4HA1 recombinant protein serves as a valuable tool for unraveling collagen-related pathologies and advancing therapeutic interventions. Its study bridges fundamental biochemistry with translational applications in fibrosis, oncology, and biomaterial sciences.
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