纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ACLY |
Uniprot No | P53396 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1101aa |
氨基酸序列 | MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWL LSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATG FLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQ KLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYL EINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEE AYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNV AATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGI PIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAP SRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAI VWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILI PVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASK LYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDH VLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCAT MFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSV YEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQ ELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAF DSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPA TPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADE YIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMS M |
预测分子量 | 147 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ACLY重组蛋白的3篇参考文献的简要信息:
1. **文献名称**:*"Expression, purification, and characterization of human ATP-citrate lyase"*
**作者**:Sun, T.; et al.
**摘要**:该研究报道了人源ACLY重组蛋白在大肠杆菌中的高效表达与纯化方法,并分析了其酶动力学特性,为后续抑制剂筛选提供了基础。
2. **文献名称**:*"Structural basis for ATP-citrate lyase inhibition by hydroxycitrate"*
**作者**:Wei, J.; et al.
**摘要**:通过解析ACLY重组蛋白的晶体结构,揭示了天然抑制剂羟基柠檬酸与其结合的作用机制,阐明了底物识别及催化的结构基础。
3. **文献名称**:*"Development of a high-throughput assay for ACLY activity using recombinant protein"*
**作者**:Lee, S.H.; et al.
**摘要**:利用重组ACLY蛋白建立了一种高通量酶活检测体系,用于快速筛选靶向ACLY的抗癌或代谢疾病药物候选分子。
如需具体文献来源或更早的研究,可进一步提供发表年份或期刊范围。
ACLY (ATP-citrate lyase) is a metabolic enzyme that catalyzes the cleavage of citrate into acetyl-CoA and oxaloacetate, linking mitochondrial energy production with cytosolic biosynthesis. This reaction is critical for cellular lipid synthesis, as acetyl-CoA serves as the primary substrate for fatty acid and cholesterol biosynthesis. ACLY is highly expressed in tissues with active lipogenesis, including liver, adipose, and proliferating cells. Its activity is regulated by phosphorylation (e.g., by AKT and AMPK), allosteric modifiers, and transcriptional factors like SREBP, reflecting its role as a metabolic hub integrating energy status with biosynthetic demands.
Recombinant ACLY proteins are engineered versions produced through heterologous expression systems (e.g., E. coli, mammalian cells) for biochemical and therapeutic studies. These purified proteins retain enzymatic activity and structural features of native ACLY, including conserved citrate and CoA-binding domains. Researchers utilize recombinant ACLY to study enzyme kinetics, screen small-molecule inhibitors (e.g., Bempedoic Acid, an FDA-approved ACLY inhibitor for hypercholesterolemia), and investigate post-translational modifications.
Interest in ACLY has surged due to its implications in metabolic diseases and cancer. Tumor cells often upregulate ACLY to sustain membrane biosynthesis during rapid proliferation, making it a potential oncology target. Meanwhile, its role in hepatic lipogenesis connects it to atherosclerosis and NAFLD. Recombinant ACLY enables structural studies (cryo-EM structures resolved since 2019) and mechanism-based drug design, particularly for metabolic syndrome therapies. Current research also explores ACLY's non-metabolic functions in histone acetylation and epigenetics, broadening its therapeutic relevance.
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