| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HMGCR |
| Uniprot No | P04035-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-835aa |
| 氨基酸序列 | MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYEC PKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTI FSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQ DEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMS VLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPN PVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKR IEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSL KNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVI KPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQ ILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLS KKLSEPSSLQYLPYRDYNYSLLGGGASSRVLADGMTRGPVVRLPRACDSA EVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGD AMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRG KSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHA ANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIG TVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSL MAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA |
| 预测分子量 | 118 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HMGCR重组蛋白的3篇代表性文献，简要整理如下：
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1. **文献名称**：*Expression, purification, and enzymatic characterization of human HMG-CoA reductase in Escherichia coli*
**作者**：Gil G, et al.
**摘要**：研究报道了人源HMGCR基因在大肠杆菌中的重组表达与纯化，分析了其酶活性及对底物(HMG-CoA)的亲和力，验证了重组蛋白的催化功能与天然蛋白的一致性。
2. **文献名称**：*Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis*
**作者**：Istvan ES, et al.
**摘要**：通过X射线晶体学解析了HMGCR催化结构域的三维结构，揭示了其底物结合位点及他汀类药物(如洛伐他汀)的作用机制，为胆固醇合成调控提供了结构基础。
3. **文献名称**：*Regulated degradation of HMG-CoA reductase in the endoplasmic reticulum through a novel ubiquitination pathway*
**作者**：Sever N, et al.
**摘要**：研究阐明了HMGCR在哺乳动物细胞中的降解机制，发现其通过内质网相关泛素化途径被调控，胆固醇水平升高会触发重组蛋白的泛素化依赖型降解。
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**说明**：以上文献聚焦于HMGCR重组蛋白的表达、结构解析及调控机制，覆盖了基础酶学、结构生物学和代谢调控方向。如需扩展，可补充杆状病毒表达系统(如Roitelman J, 1992)或功能突变体研究。
HMGCR (3-hydroxy-3-methylglutaryl-coenzyme A reductase) is a rate-limiting enzyme in the mevalonate pathway, responsible for cholesterol biosynthesis and isoprenoid production. As a key regulatory node in cellular metabolism, it catalyzes the conversion of HMG-CoA to mevalonate, requiring NADPH as a cofactor. Its activity directly influences cholesterol homeostasis, making it a primary therapeutic target for statins, widely prescribed drugs to lower LDL cholesterol and reduce cardiovascular risk.
Recombinant HMGCR proteins are engineered versions expressed in heterologous systems like *E. coli*, yeast, or mammalian cells (e.g., HEK293 or CHO), enabling standardized studies of its structure, function, and inhibition. These proteins retain catalytic domains (approximately 50 kDa soluble fragment) while omitting the N-terminal membrane-anchoring region to improve solubility. Affinity tags (His, GST, or FLAG) are often incorporated to facilitate purification and detection.
Applications include enzymatic assays to evaluate statin efficacy, investigate drug resistance mutations, and explore post-translational modifications (e.g., ubiquitination regulating protein degradation). Recombinant HMGCR also serves as an antigen for antibody development and a tool to study lipid metabolism disorders. Structural studies using crystallized recombinant protein have revealed binding mechanisms of statins, guiding the design of novel lipid-lowering agents. Current research leverages recombinant HMGCR to dissect its role in diseases beyond atherosclerosis, including cancer and neurodegenerative conditions linked to dysregulated cholesterol synthesis.
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