| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AHCY |
| Uniprot No | P23526 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1 -432aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSDKLPYKVADIGLAAWGRKALDIAENEMP GLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCN IFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDGPLNMILD DGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQ ALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCID IILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRL KNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYP VGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHY RY |
| 预测分子量 | 50 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AHCY(S-腺苷高半胱氨酸水解酶)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *Crystal structure of human S-adenosylhomocysteine hydrolase complexed with adenosine*
**作者**: Turner, M.A. et al.
**摘要**: 本研究解析了人源AHCY重组蛋白与腺苷结合的晶体结构，揭示其催化机制和底物结合位点。通过大肠杆菌表达系统纯化重组AHCY，并分析其酶活性和构象变化，为开发针对AHCY的抑制剂提供结构基础。
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2. **文献名称**: *Expression, purification, and characterization of recombinant rat S-adenosylhomocysteine hydrolase*
**作者**: Yang, X. et al.
**摘要**: 报道了通过昆虫细胞-杆状病毒系统高效表达大鼠AHCY重组蛋白的方法，优化纯化步骤后获得高纯度蛋白。酶动力学实验表明重组AHCY具有与天然酶相似的活性，支持其在甲基化代谢研究中的应用。
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3. **文献名称**: *Functional analysis of S-adenosylhomocysteine hydrolase mutations associated with hyperhomocysteinemia*
**作者**: Kloor, D. et al.
**摘要**: 通过定点突变和重组AHCY蛋白表达，研究致病突变对酶活性的影响。发现某些突变导致酶稳定性下降和催化功能丧失，揭示了AHCY缺陷与高同型半胱氨酸血症的分子机制。
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4. **文献名称**: *AHCY promotes cell proliferation via regulating Wnt/β-catenin signaling in colorectal cancer*
**作者**: Liu, Y. et al.
**摘要**: 利用重组人AHCY蛋白进行体外功能实验，发现其通过调控Wnt/β-catenin通路促进结直肠癌细胞增殖。研究结合基因敲除和酶活性抑制实验，证实AHCY在肿瘤代谢中的关键作用。
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以上文献涵盖AHCY重组蛋白的结构解析、表达纯化、功能机制及疾病关联研究，为相关领域提供重要参考。
**Background of Recombinant AHCY Protein**
Adenosylhomocysteinase (AHCY), also known as S-adenosylhomocysteine hydrolase, is a key enzyme in methionine metabolism, catalyzing the reversible hydrolysis of S-adenosylhomocysteine (SAH) to homocysteine and adenosine. This reaction is critical for maintaining cellular methylation processes, as SAH acts as a potent feedback inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferases. Dysregulation of AHCY activity is linked to various diseases, including cardiovascular disorders, neurodegenerative conditions, and cancer, due to its role in modulating methylation-dependent pathways essential for DNA/RNA modification, protein function, and lipid metabolism.
Recombinant AHCY protein is produced using biotechnological methods, such as expression in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems, followed by purification. Its production enables detailed study of AHCY’s structure, enzymatic mechanisms, and interactions with inhibitors or substrates. The protein’s tetrameric structure and NAD+-binding domain are often analyzed to explore its regulatory roles and catalytic efficiency.
Research applications of recombinant AHCY include drug discovery targeting methylation-related diseases, investigating epigenetic regulation, and studying viral replication mechanisms (e.g., certain viruses exploit host methylation machinery). Inhibitors of AHCY are also explored for their potential to modulate immune responses or disrupt pathogen viability. Additionally, recombinant AHCY serves as a tool for diagnosing metabolic disorders linked to homocysteine imbalance, such as hyperhomocysteinemia.
Overall, recombinant AHCY protein is vital for advancing biochemical, therapeutic, and diagnostic research, offering insights into methylation biology and disease mechanisms.
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