纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | IDH2 |
Uniprot No | P48735 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-452aa |
氨基酸序列 | MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPV VEMDGDEMTRIIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDS ALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFRE PIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKD GSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMST KNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKS SGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGT VTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEK VCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALG RQDYKDDDDK |
预测分子量 | 52 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篇关于IDH2重组蛋白的示例性参考文献(注:文献标题和作者为虚构示例,仅供格式参考):
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1. **标题**:*Expression and Functional Characterization of Recombinant IDH2 R140Q Mutant Protein in Cancer Metabolism*
**作者**:Smith A, et al.
**摘要**:研究通过大肠杆菌表达系统成功纯化IDH2 R140Q突变体重组蛋白,发现其丧失正常催化活性,并产生致癌代谢物2-羟基戊二酸(2-HG),揭示了突变IDH2在肿瘤代谢重编程中的作用。
2. **标题**:*Structural Insights into IDH2 Heterodimer Formation Using Cryo-EM*
**作者**:Chen L, et al.
**摘要**:利用冷冻电镜解析了重组人源IDH2野生型与突变型(R172K)的异源二聚体结构,阐明了突变导致酶活性位点构象变化的分子机制,为靶向药物设计提供结构基础。
3. **标题**:*High-Throughput Screening of IDH2 Inhibitors Using Purified Recombinant Enzyme Assays*
**作者**:Wang Y, et al.
**摘要**:建立基于重组IDH2蛋白的高通量筛选平台,鉴定出多个小分子抑制剂,可选择性抑制突变型IDH2的2-HG合成,为治疗IDH2突变相关白血病提供潜在候选药物。
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(注:以上文献为示例,实际引用请查询真实数据库如PubMed。)
**Background of IDH2 Recombinant Protein**
Isocitrate dehydrogenase 2 (IDH2) is a mitochondrial enzyme encoded by the *IDH2* gene, playing a critical role in cellular metabolism. It catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG) in the tricarboxylic acid (TCA) cycle, simultaneously reducing NADP+ to NADPH. This reaction supports energy production, redox balance, and biosynthesis. IDH2 is distinct from its cytosolic counterpart, IDH1. due to its mitochondrial localization and tissue-specific expression.
Mutations in *IDH2*, particularly at residues R140 and R172. are implicated in various cancers, including acute myeloid leukemia (AML), gliomas, and chondrosarcomas. These mutations confer a neomorphic activity, converting α-KG to the oncometabolite D-2-hydroxyglutarate (2-HG), which disrupts cellular epigenetics and differentiation by inhibiting α-KG-dependent enzymes like TET proteins and histone demethylases. This oncogenic mechanism has made mutant IDH2 a therapeutic target.
Recombinant IDH2 protein is engineered for research and drug development. Produced via expression systems like *E. coli* or mammalian cells, it retains enzymatic activity and structural integrity. Purification tags (e.g., His-tag) facilitate isolation, ensuring high purity and functionality. Researchers use recombinant IDH2 to study enzyme kinetics, screen inhibitors, and investigate mutation-driven metabolic dysregulation.
In drug discovery, recombinant IDH2 aids in developing selective inhibitors, such as enasidenib (AG-221), an FDA-approved therapy for IDH2-mutant AML. It also serves as a tool for diagnostic assays and biomarker validation. By elucidating IDH2's role in cancer metabolism, recombinant proteins contribute to advancing precision medicine and understanding metabolic reprogramming in disease.
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