纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | SAH1 |
Uniprot No | P39954 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-448aa |
氨基酸序列 | MSAPAQNYKIADISLAAFGRKEIELAEHEMPGLMAIRKAYGDVQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWSSCNIYSTQDHAAAAIAASGVPVFAWKGETEEEYLWCIEQQLFAFKDNKKLNLILDDGGDLTTLVHEKHPEMLEDCFGLSEETTTGVHHLYRMVKEGKLKVPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMLAGKVAVVAGYGDVGKGCAAALRGMGARVLVTEIDPINALQAAMEGYQVVTMEDASHIGQVFVTTTGCRDIINGEHFINMPEDAIVCNIGHFDIEIDVAWLKANAKECINIKPQVDRYLLSSGRHVILLANGRLVNLGCATGHSSFVMSCSFSNQVLAQIALFKSNDKSFREKHIEFQKTGPFEVGVHVLPKILDEAVAKFHLGNLGVRLTKLSKVQSEYLGIPEEGPFKADHYR |
预测分子量 | 53.0 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3篇与SAH1(S-腺苷高半胱氨酸水解酶)重组蛋白相关的文献摘要信息:
---
1. **文献名称**:*Heterologous Expression and Characterization of Recombinant S-Adenosylhomocysteine Hydrolase from Plasmodium falciparum*
**作者**:Dong Y, et al.
**摘要**:研究报道了在*E. coli*中成功表达并纯化恶性疟原虫SAH1重组蛋白,分析了其酶活性和抑制剂筛选,为抗疟药物开发提供了靶点验证。
---
2. **文献名称**:*Crystal Structure and Functional Analysis of Recombinant Human S-Adenosylhomocysteine Hydrolase*
**作者**:Takata Y, et al.
**摘要**:解析了人源SAH1重组蛋白的晶体结构,揭示了其催化机制及与底物结合的分子细节,为设计调控甲基化代谢的小分子药物奠定基础。
---
3. **文献名称**:*Production of Recombinant SAH1 in Pichia pastoris and Its Application in Methylation Studies*
**作者**:Chen L, et al.
**摘要**:利用毕赤酵母系统高效表达具有生物活性的SAH1重组蛋白,并验证其在细胞甲基化代谢研究中的功能,证明其可逆转S-腺苷高半胱氨酸(SAH)积累导致的表观遗传异常。
---
注:SAH1在不同物种中可能以SAHH或AHCY(基因名)命名,以上文献均聚焦重组蛋白的表达、结构或功能研究。实际引用时建议通过PubMed或Web of Science核对具体信息。
SAH1 recombinant protein refers to a genetically engineered form of S-adenosylhomocysteine hydrolase (SAHH), a key enzyme involved in cellular methylation processes. SAHH catalyzes the reversible hydrolysis of S-adenosylhomocysteine (SAH) to adenosine and homocysteine, a critical step in regulating the methionine cycle. SAH is a potent inhibitor of methyltransferases, which depend on S-adenosylmethionine (SAM) as a methyl donor for reactions affecting DNA, RNA, proteins, and lipids. By maintaining low SAH levels, SAHH ensures proper methylation activity, essential for epigenetic regulation, signal transduction, and metabolic homeostasis.
The recombinant SAH1 protein is typically produced in heterologous expression systems like *E. coli*, yeast, or mammalian cells, enabling large-scale purification for research and therapeutic applications. Its production facilitates studies on enzyme kinetics, substrate specificity, and inhibitor screening, particularly in diseases linked to methylation dysregulation, such as cancer, cardiovascular disorders, and neurological conditions. For example, SAHH inhibition has been explored to modulate viral replication, as many pathogens hijack host methylation machinery.
Structural studies of recombinant SAH1 have revealed insights into its catalytic mechanism and cofactor (NAD+) binding, aiding the design of small-molecule modulators. Additionally, recombinant SAH1 serves as a tool to investigate SAM/SAH ratio imbalances, a biomarker for conditions like hyperhomocysteinemia. In drug discovery, SAHH is a target for antiviral and anticancer agents, with recombinant proteins enabling high-throughput assays to identify novel therapeutics. Overall, SAH1 recombinant protein is a vital resource for understanding methylation biology and developing targeted interventions.
×