| 纯度 | > 80 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AMD1 |
| Uniprot No | P17707 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 68-334aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMSSMFV SKRRFILKTC GTTLLLKALV PLLKLARDYS GFDSIQSFFY SRKNFMKPSH QGYPHRNFQE EIEFLNAIFP NGAAYCMGRM NSDCWYLYTL DFPESRVISQ PDQTLEILMS ELDPAVMDQF YMKDGVTAKD VTRESGIRDL IPGSVIDATM FNPCGYSMNG MKSDGTYWTI HITPEPEFSY VSFETNLSQT SYDDLIRKVV EVFKPGKFVT TLFVNQSSKC RTVLASPQKI EGFKRLDCQS AMFNDYNFVF TSFAKKQQQQ QS |
| 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AMD1重组蛋白的3-4篇参考文献的简要列举(注：文献标题和作者为虚拟示例，实际研究中请根据具体论文调整)：
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1. **标题**：*"Heterologous expression and functional analysis of human AMD1 in E. coli for polyamine biosynthesis studies"*
**作者**：Chen L, et al.
**摘要**：研究利用大肠杆菌表达系统成功克隆并纯化了人源AMD1重组蛋白，验证其催化腺苷甲硫氨酸脱羧的活性，并探讨其在多胺代谢中的调控作用。
2. **标题**：*"Structural characterization of recombinant AMD1 from Drosophila melanogaster using cryo-EM"*
**作者**：Wang X, et al.
**摘要**：通过冷冻电镜技术解析果蝇AMD1重组蛋白的三维结构，揭示其底物结合位点和酶促反应机制，为靶向AMD1的抑制剂设计提供结构基础。
3. **标题**：*"Optimization of AMD1 recombinant protein production in HEK293 cells for cancer therapeutics screening"*
**作者**：Gupta R, et al.
**摘要**：优化了哺乳动物细胞(HEK293)中AMD1重组蛋白的高效表达和纯化流程，证明其在体外癌细胞模型中抑制多胺合成的能力。
4. **标题**：*"Enzymatic activity and kinetic analysis of recombinant plant AMD1 under stress conditions"*
**作者**：Tanaka K, et al.
**摘要**：从拟南芥中表达AMD1重组蛋白，分析其在盐胁迫条件下的酶动力学变化，阐明其在植物应激响应中的生物学意义。
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**提示**：实际文献检索建议通过PubMed、Web of Science或Google Scholar使用关键词“AMD1 recombinant protein”“adenosylmethionine decarboxylase expression”进行筛选，并优先选择近五年内发表的、实验方法详实的论文。
**Background of AMD1 Recombinant Protein**
AMD1 (adenosylmethionine decarboxylase 1) is a key enzyme in the polyamine biosynthesis pathway, essential for cellular proliferation and differentiation. It catalyzes the decarboxylation of S-adenosylmethionine (SAM) to produce decarboxylated SAM (dcSAM), a critical donor of propylamine groups required for synthesizing spermidine and spermine—polyamines vital for stabilizing nucleic acids, regulating ion channels, and maintaining cellular homeostasis. Dysregulation of AMD1 is linked to various diseases, including cancer, as elevated polyamine levels often support tumor growth.
Recombinant AMD1 protein is engineered through genetic cloning, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications. The recombinant form retains enzymatic activity, enabling studies on polyamine metabolism, drug discovery, and molecular mechanisms in disease. Researchers utilize it to screen inhibitors targeting AMD1. aiming to develop therapies for cancers or parasitic infections reliant on polyamines.
Its production also aids structural studies (e.g., X-ray crystallography) to elucidate substrate-binding sites and catalytic mechanisms. Additionally, AMD1 recombinant protein serves as a tool in diagnostic assays or to generate antibodies for detecting endogenous AMD1 expression in tissues. By providing a controlled, pure enzyme source, recombinant AMD1 accelerates both basic research and therapeutic innovation in polyamine-related pathologies.
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