| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AACS |
| Uniprot No | Q86V21 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-672aa |
| 氨基酸序列 | MSKEERPGRE EILECQVMWE PDSKKNTQMD RFRAAVGAAC GLALESYDDL YHWSVESYSD FWAEFWKFSG IVFSRVYDEV VDTSKGIADV PEWFKGSRLN YAENLLRHKE NDRVALYIAR EGKEEIVKVT FEELRQEVAL FAAAMRKMGV KKGDRVVGYL PNSEHAVEAM LAAASIGAIW SSTSPDFGVN GVLDRFSQIQ PKLIFSVEAV VYNGKEHNHM EKLQQVVKGL PDLKKVVVIP YVSSRENIDL SKIPNSVFLD DFLATGTSEQ APQLEFEQLP FSHPLFIMFS SGTTGAPKCM VHSAGGTLIQ HLKEHLLHGN MTSSDILLCY TTVGWMMWNW MVSLLATGAA MVLYDGSPLV PTPNVLWDLV DRIGITVLVT GAKWLSVLEE KAMKPVETHS LQMLHTILST GSPLKAQSYE YVYRCIKSSI LLGSISGGTD IISCFMGHNF SLPVYKGEIQ ARNLGMAVEA WNEEGKAVWG ESGELVCTKP IPCQPTHFWN DENGNKYRKA YFSKFPGIWA HGDYCRINPK TGGIVMLGRS DGTLNPNGVR FGSSEIYNIV ESFEEVEDSL CVPQYNKYRE ERVILFLKMA SGHAFQPDLV KRIRDAIRMG LSARHVPSLI LETKGIPYTL NGKKVEVAVK QIIAGKAVEQ GGAFSNPETL DLYRDIPELQ GF |
| 预测分子量 | 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AACS(Acetoacetyl-CoA synthetase)重组蛋白研究的3篇代表性文献示例(注：以下文献为示例性内容，实际引用请核实真实来源)：
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1. **文献名称**：*Cloning, Expression, and Functional Characterization of Recombinant Acetoacetyl-CoA Synthetase in Escherichia coli*
**作者**：Smith, J.R., et al.
**摘要**：该研究报道了在大肠杆菌中成功克隆并高效表达具有生物活性的AACS重组蛋白，通过亲和层析纯化验证其酶活性，证实其在体外催化乙酰乙酸生成乙酰乙酰辅酶A的能力，为代谢途径研究提供工具。
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2. **文献名称**：*Structural Insights into AACS Catalytic Mechanism via Crystallographic Analysis of Recombinant Human Protein*
**作者**：Li, X., & Wang, H.
**摘要**：作者解析了重组表达的人源AACS蛋白的晶体结构，揭示了其底物结合位点及ATP依赖的催化机制，为设计针对胆固醇合成通路的小分子抑制剂奠定结构基础。
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3. **文献名称**：*Role of Recombinant AACS in Hepatic Lipid Metabolism: In Vitro and In Vivo Studies*
**作者**：Tanaka, K., et al.
**摘要**：通过体外重组AACS蛋白实验及转基因小鼠模型，证明AACS过表达显著促进肝脏脂质积累，提示其在非酒精性脂肪肝疾病中的潜在调控作用。
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如需具体文献，建议在PubMed或Web of Science中检索关键词："Acetoacetyl-CoA synthetase recombinant" 或 "AACS expression purification"。
**Background of AACS Recombinant Protein**
Acetoacetyl-CoA synthetase (AACS), also known as acetyl-CoA acetyltransferase 2 (ACAT2), is a key enzyme involved in lipid metabolism, particularly in the synthesis and degradation of ketone bodies and cholesterol esters. It catalyzes the reversible conversion of acetoacetate into acetoacetyl-CoA, a critical substrate for cholesterol biosynthesis and cellular energy production under metabolic stress. AACS is highly expressed in tissues with active lipid metabolism, such as the liver, brain, and adipose tissue, and its activity is tightly linked to metabolic disorders, including obesity, diabetes, and neurodegenerative diseases.
The recombinant AACS protein is produced using genetic engineering techniques, where the AACS gene is cloned into expression vectors and expressed in host systems like *E. coli* or mammalian cell lines. This allows large-scale production of the purified, functional enzyme for research and therapeutic applications. Recombinant AACS retains the enzymatic properties of the native protein, enabling studies on its structure-function relationships, regulatory mechanisms, and interactions with substrates or inhibitors.
Research on AACS has gained momentum due to its potential role in cancer metabolism, as cancer cells often reprogram lipid metabolism to support rapid proliferation. Inhibitors targeting AACS are being explored as novel therapeutic strategies. Additionally, recombinant AACS is utilized in *in vitro* assays to screen drug candidates or investigate metabolic pathways. Its applications extend to industrial biotechnology, where it aids in biofuel production or synthetic biology projects requiring precise control of lipid intermediates.
Despite progress, challenges remain in optimizing recombinant AACS stability, activity, and scalability. Advances in protein engineering and structural biology continue to refine its production and functional characterization, underscoring its importance in both basic research and translational medicine.
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