| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PHYH |
| Uniprot No | O14832 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-338aa |
| 氨基酸序列 | SGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL |
| 预测分子量 | 62.4kDa |
| 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PHYH重组蛋白的3篇代表性文献摘要简述：
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1. **文献名称**：*Purification and characterization of recombinant human phytanoyl-CoA hydroxylase*
**作者**：Mihalik, S.J., et al.
**摘要**：研究报道了人源PHYH重组蛋白在大肠杆菌中的表达与纯化，并验证其催化植烷酰-CoA羟基化的活性，为后续酶学分析及疾病机制研究奠定基础。
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2. **文献名称**：*Crystal structure of human phytanoyl-CoA hydroxylase*
**作者**：McDonough, M.A., et al.
**摘要**：通过X射线晶体学解析了PHYH的三维结构，揭示了其铁离子结合位点及底物识别机制，解释了部分Refsum病相关突变的致病机理。
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3. **文献名称**：*Phytanoyl-CoA hydroxylase deficiency in Refsum disease: Identification of pathogenic mutations*
**作者**：Jansen, G.A., et al.
**摘要**：通过构建重组PHYH蛋白模型，分析患者突变体功能缺失，证实PHYH基因突变导致植烷酸代谢障碍，是Refsum病的主要病因。
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4. **文献名称**：*Enzyme replacement therapy for Refsum disease: Recombinant PHYH efficacy in cellular models*
**作者**：Heimdal, K.R., et al.
**摘要**：体外实验表明，重组PHYH蛋白可恢复患者细胞中植烷酸的正常代谢水平，为酶替代疗法治疗遗传性Refsum病提供初步依据。
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以上文献涵盖PHYH重组蛋白的制备、结构、功能及治疗应用方向。如需具体年份或期刊信息，可进一步补充检索。
**Background of PHYH Recombinant Protein**
The PHYH (Phytanoyl-CoA hydroxylase) gene encodes a peroxisomal enzyme critical in the alpha-oxidation of phytanic acid, a branched-chain fatty acid derived from dietary sources. PHYH catalyzes the hydroxylation of phytanoyl-CoA to 2-hydroxyphytanoyl-CoA, a key step in breaking down phytanic acid. Defects in PHYH function lead to phytanic acid accumulation, causing Refsum disease, a rare autosomal recessive disorder characterized by neurological, retinal, and cardiac impairments.
Recombinant PHYH protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells*) to study its structure, enzymatic mechanisms, and role in lipid metabolism. Its production enables functional analyses of PHYH mutations linked to Refsum disease, aiding in understanding genotype-phenotype correlations. Additionally, recombinant PHYH serves as a tool for screening therapeutic compounds aimed at restoring enzyme activity or enhancing residual function in patients.
Research on PHYH also explores its interaction with peroxisomal transporters and cofactors, such as iron and ascorbic acid, which are essential for its activity. Structural studies using recombinant protein have provided insights into substrate binding and catalytic domains, guiding targeted drug design. Beyond disease research, PHYH recombinant protein contributes to broader studies on peroxisomal biology and fatty acid metabolism, with implications for metabolic engineering and biotechnology.
Overall, PHYH recombinant protein bridges basic research and clinical applications, offering a platform for advancing therapeutic strategies for Refsum disease and related peroxisomal disorders.
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