| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HMGCL |
| Uniprot No | P35914 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-325aa |
| 氨基酸序列 | MTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSF VSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAGAKEVVI FGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPY EGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVP LAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNL ATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATCKLH HHHHH |
| 预测分子量 | 33 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HMGCL(HMG-CoA裂解酶)重组蛋白的3篇代表性文献，按研究内容分类整理：
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1. **文献名称**：Cloning, expression, and purification of human HMG-CoA lyase in Escherichia coli
**作者**：Roberts JR et al.
**摘要概括**：本研究成功克隆了人类HMGCL基因，并在大肠杆菌中实现高效表达。通过优化诱导条件和纯化步骤(如His标签亲和层析)，获得高纯度重组蛋白，并验证其酶活性，为后续功能研究奠定基础。
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2. **文献名称**：Structural and functional characterization of recombinant HMG-CoA lyase from Pseudomonas putida
**作者**：Zhang Y, et al.
**摘要概括**：报道了恶臭假单胞菌来源的HMGCL重组蛋白的晶体结构解析，揭示其底物结合位点及催化机制。通过酶动力学实验证明其在高浓度乙酰乙酸生产中的潜在工业应用价值。
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3. **文献名称**：Functional analysis of HMGCL mutations in ketogenesis using recombinant enzyme assays
**作者**：Lee S, Kim DH
**摘要概括**：构建了重组人HMGCL蛋白表达系统，用于检测临床患者基因突变对酶活性的影响。研究发现某些错义突变导致蛋白稳定性下降，为遗传性酮体代谢障碍的分子诊断提供工具。
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**备注**：以上文献为示例模板，实际引用时需通过PubMed或Web of Science检索最新研究(如关键词："HMGCL recombinant" "expression purification")，优先选择近5年发表且被引次数较高的文章。
**Background of HMGCL Recombinant Protein**
3-Hydroxy-3-methylglutaryl-CoA lyase (HMGCL) is a mitochondrial enzyme critical in ketogenesis and leucine catabolism. It catalyzes the cleavage of HMG-CoA into acetoacetate and acetyl-CoA, a pivotal step in generating ketone bodies during fasting and metabolic stress. Dysregulation of HMGCL activity is linked to hereditary metabolic disorders, particularly HMGCL deficiency, an autosomal recessive condition causing hypoglycemia, metabolic acidosis, and encephalopathy.
Recombinant HMGCL protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to enable large-scale, high-purity enzyme production. This engineered protein retains native catalytic activity and structural stability, making it valuable for functional studies, drug screening, and diagnostic applications. Researchers utilize recombinant HMGCL to investigate its role in metabolic pathways, disease mechanisms, and potential therapeutic interventions.
In biomedical research, the protein aids in elucidating structural-functional relationships through crystallography and enzymology assays. Clinically, it supports the development of enzyme replacement therapies or small-molecule modulators for metabolic disorders. Additionally, recombinant HMGCL serves as an antigen in antibody production for diagnostic kits, improving detection of HMGCL deficiency and related conditions.
The availability of recombinant HMGCL has advanced understanding of mitochondrial metabolism and accelerated translational research, offering tools to address unmet needs in rare metabolic diseases. Its applications underscore the intersection of enzymology, genetics, and biotechnology in tackling complex metabolic challenges.
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