| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PEX1 |
| Uniprot No | O43933 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1283aa |
| 氨基酸序列 | MWGSDRLAGAGGGGAAVTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSHQPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLKPCSHVVSCQQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAASYGRLETDTKLLIQPKTRRAKENTFSKADAEYKKLHSYGRDQKGMMKELQTKQLQSNTVGITESNENESEIPVDSSSVASLWTMIGSIFSFQSEKKQETSWGLTEINAFKNMQSKVVPLDNIFRVCKSQPPSIYNASATSVFHKHCAIHVFPWDQEYFDVEPSFTVTYGKLVKLLSPKQQQSKTKQNVLSPEKEKQMSEPLDQKKIRSDHNEEDEKACVLQVVWNGLEELNNAIKYTKNVEVLHLGKVWIPDDLRKRLNIEMHAVVRITPVEVTPKIPRSLKLQPRENLPKDISEEDIKTVFYSWLQQSTTTMLPLVISEEEFIKLETKDGLKEFSLSIVHSWEKEKDKNIFLLSPNLLQKTTIQVLLDPMVKEENSEEIDFILPFLKLSSLGGVNSLGVSSLEHITHSLLGRPLSRQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKLDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAGLPAVPEHEHSPDAVQSQRLAHALNDMIKEFISMGSLVALIATSQSQQSLHPLLVSAQGVHIFQCVQHIQPPNQEQRCEILCNVIKNKLDCDINKFTDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGMLLSSGLQDGSSSSDSDLSLSSMVFLNHSSGSDDSAGDGECGLDQSLVSLEMSEILPDESKFNMYRLYFGSSYESELGNGTSSDLSSQCLSAPSSMTQDLPGVPGKDQLFSQPPVLRTASQEGCQELTQEQRDQLRADISIIKGRYRSQSGEDESMNQPGPIKTRLAISQSHLMTALGHTRPSISEDDWKNFAELYESFQNPKRRKNQSGTMFRPGQKVTLA |
| 预测分子量 | 142,8 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3篇与PEX1重组蛋白相关的文献摘要整理：
1. **文献名称**：*Recombinant human PEX1 and PEX6 form a stable AAA+ complex for peroxisomal matrix protein import*
**作者**：Tamura S, Matsumoto N, Imamura A, et al.
**摘要**：该研究利用重组表达的PEX1和PEX6蛋白，证明两者在体外形成ATP依赖的AAA+复合物，揭示了其在过氧化物酶体基质蛋白输入中的协同作用机制。
2. **文献名称**：*Functional analysis of PEX1 mutations in vitro using a novel yeast expression system*
**作者**：Francisco T, Liu Y, Smith JJ, et al.
**摘要**：通过酵母表达系统重组表达携带不同突变位点的人源PEX1蛋白，发现特定突变导致ATP酶活性丧失，进而破坏过氧化物酶体膜蛋白的稳态。
3. **文献名称**：*Structural insights into the PEX1-PEX6 ATPase complex by cryo-EM*
**作者**：De La Peña AH, Hsu CH, Svitkina T, et al.
**摘要**：利用冷冻电镜解析重组表达的人源PEX1-PEX6复合体三维结构，揭示其六聚体环状构象及ATP水解驱动的构象变化，为齐薇格综合征的致病机理提供结构基础。
注：以上文献为示例性内容，实际引用时建议通过PubMed或Web of Science核对最新研究。
**Background of PEX1 Recombinant Protein**
PEX1 is a member of the AAA ATPase (ATPases Associated with diverse cellular Activities) protein family, playing a critical role in peroxisome biogenesis and maintenance. Peroxisomes are essential organelles involved in lipid metabolism, reactive oxygen species detoxification, and bile acid synthesis. Mutations in the *PEX1* gene are the most common cause of peroxisome biogenesis disorders (PBDs), such as Zellweger spectrum disorders (ZSDs), which are characterized by severe neurological, hepatic, and developmental abnormalities.
Recombinant PEX1 protein is engineered through genetic engineering techniques to study its structure, function, and interactions within the peroxisomal matrix protein import machinery. PEX1 forms a heterohexameric complex with PEX6. another AAA ATPase, which is essential for recycling the peroxisomal matrix protein receptor PEX5 from the peroxisomal membrane—a key step in the peroxisomal protein import cycle. Dysregulation of this process disrupts peroxisome function, leading to metabolic dysfunction.
The production of recombinant PEX1 typically involves expression in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells) to obtain properly folded, functional protein. Purification methods, such as affinity chromatography and size-exclusion chromatography, ensure high-quality protein for biochemical assays, structural studies (e.g., cryo-EM or X-ray crystallography), and drug discovery efforts.
Research on recombinant PEX1 aims to clarify the molecular mechanisms underlying PBDs, screen potential therapeutic compounds to rescue mutant PEX1 activity, and develop gene therapy strategies. Advances in structural biology and protein engineering have enhanced understanding of PEX1's ATP-dependent conformational changes and its role in disease pathogenesis, offering hope for targeted treatments for peroxisome-related disorders.
In summary, recombinant PEX1 serves as a vital tool for dissecting peroxisome biology and developing interventions for devastating genetic disorders linked to peroxisomal dysfunction.
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