纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MLYCD |
Uniprot No | O95822 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 40-493aa |
氨基酸序列 | MDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL |
预测分子量 | 55.9kDa |
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. |
以下是模拟生成的关于MLYCD(丙二酰辅酶A脱羧酶)重组蛋白研究的参考文献示例,供参考:
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1. **文献名称**:*Recombinant Human Malonyl-CoA Decarboxylase: Expression in E. coli and Enzymatic Characterization*
**作者**:Smith J. et al.
**摘要**:研究通过大肠杆菌系统高效表达并纯化重组人源MLYCD蛋白,分析其酶动力学参数及底物特异性,为代谢疾病研究提供工具。
2. **文献名称**:*Structural Insights into MLYCD Deficiency via Cryo-EM Analysis of Recombinant Protein*
**作者**:Chen L. & Wang H.
**摘要**:利用冷冻电镜解析重组MLYCD的三维结构,结合突变体功能实验,揭示其缺乏症患者常见致病突变的分子机制。
3. **文献名称**:*MLYCD Recombinant Protein Rescues Cardiac Dysfunction in a Mouse Metabolic Model*
**作者**:Gomez R. et al.
**摘要**:在小鼠模型中验证重组MLYCD蛋白的治疗潜力,证明其通过调节脂肪酸代谢缓解心脏功能异常,提示潜在临床价值。
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**说明**:以上文献为模拟示例,实际文献需通过PubMed、Google Scholar等平台检索关键词(如“recombinant MLYCD”“malonyl-CoA decarboxylase expression”)获取。建议结合具体研究方向筛选近年高被引论文。
MLYCD (Malonyl-CoA Decarboxylase) is a mitochondrial enzyme that plays a critical role in cellular energy metabolism by catalyzing the decarboxylation of malonyl-CoA to acetyl-CoA and carbon dioxide. This reaction serves as a key regulatory step in fatty acid oxidation, as malonyl-CoA acts both as an intermediate in fatty acid synthesis and a potent inhibitor of carnitine palmitoyltransferase 1 (CPT1), the rate-limiting enzyme responsible for transporting long-chain fatty acids into mitochondria for β-oxidation. By depleting malonyl-CoA levels, MLYCD effectively relieves this inhibition, promoting fatty acid utilization as an energy source.
The MLYCD gene is located on chromosome 16q24. and its deficiency in humans leads to rare autosomal recessive metabolic disorders characterized by developmental delay, cardiomyopathy, and recurrent hypoglycemia. These clinical manifestations underscore the enzyme's importance in maintaining metabolic homeostasis, particularly under fasting conditions when fatty acid oxidation becomes crucial for energy production.
Recombinant MLYCD protein has been produced using various expression systems (e.g., E. coli, mammalian cell lines) to enable detailed biochemical and structural studies. Researchers employ the recombinant protein to investigate substrate specificity, enzymatic kinetics, and regulatory mechanisms. Structural analyses have revealed conserved domains critical for catalytic activity, including a tetrameric organization and a biotin-binding motif essential for its function as a carboxylase/decarboxylase.
Pharmaceutical interest in MLYCD has emerged due to its potential as a therapeutic target for metabolic syndromes. Inhibiting MLYCD could theoretically elevate malonyl-CoA levels, thereby reducing fatty acid oxidation and promoting glucose utilization – a strategy explored for diabetes management. Conversely, enzyme replacement approaches are being investigated for MLYCD deficiency disorders. Recent studies also explore its role in cancer metabolism, where some tumors appear to exploit MLYCD-mediated metabolic reprogramming to support proliferation.
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