| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | bglIIM |
| Uniprot No | Q45489 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-360aa |
| 氨基酸序列 | MSEDQYKQIKLHLGMEDDNEDLPNHIPSSFPKQHLNKIYNGDTMNMLLDIPDNSVDLVVTSPPYNINKFKNDRRPLEEYLKWQTEIIEQCHRVLKPSGSIFWQVGTYVNDSGAHIPLDIRFFPIFESLGMFPRNRIVWVRPHGLHANKKFAGRHETILWFTKTPEYKFFLDPIRVPQKYANKKHYKGDKKGELSGDPLGKNPGDVWAFRNVRHNHEEDTIHPTQYPEDMIERIVLSTTEPNDIVLDPFIGMGTTASVAKNLNRYFYGAEIEKEYVDIAYQILSGEPDENNNFPNLKTLRQYCEKNGIIDPSQYTFTRQRKGSKPSLDSKAHPEEHHKKEIVERIEFEAENSVYKKVQNEQ |
| 预测分子量 | 58.0 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. |
以下是关于BglIIM重组蛋白的3篇参考文献示例(注：部分文献为模拟示例，实际引用时请核实原文信息)：
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1. **"Cloning and Expression of the BglII Methyltransferase Gene in Escherichia coli"**
*作者：Smith A, Jones B*
摘要：该研究首次报道了BglII甲基转移酶(BglIIM)基因的克隆，并在大肠杆菌中实现重组表达。通过亲和层析纯化获得高纯度蛋白，并证实其甲基化活性可特异性修饰AGATCT序列中的腺嘌呤，保护DNA免受BglII限制酶切割。
2. **"Kinetic Analysis of Recombinant BglII Methyltransferase"**
*作者：Lee C, Zhang D*
摘要：研究分析了重组BglIIM的酶动力学特性，测定其最适反应pH为7.5.依赖S-腺苷甲硫氨酸(SAM)作为甲基供体。通过凝胶迁移实验验证了甲基化对DNA-蛋白质相互作用的调控作用。
3. **"Application of BglII Methyltransferase in Synthetic Biology Circuits"**
*作者：Wang H et al.*
摘要：利用重组BglIIM构建人工甲基化调控系统，实现对质粒DNA的定向修饰。研究证明该酶在合成生物学中可有效增强基因回路稳定性，并降低宿主限制性内切酶系统的干扰。
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**注**：以上文献为示例性内容，实际研究中建议通过PubMed(https://pubmed.ncbi.nlm.nih.gov)或Google Scholar检索关键词(如“BglII methyltransferase recombinant”)获取真实文献。早期经典研究可能发表于1980-1990年代，近年研究可能侧重工程化改造或应用拓展。
The BglII methyltransferase (BglIIM) is a component of the BglII restriction-modification (R-M) system, originally isolated from *Bacillus globigii*. R-M systems are bacterial defense mechanisms that protect host DNA by methylating specific sequences while cleaving unmethylated foreign DNA. BglIIM functions as a methyltransferase, catalyzing the transfer of a methyl group from S-adenosylmethionine (SAM) to the adenine residue within the recognition sequence 5'-AGATCT-3'. This methylation prevents cleavage by the BglII restriction endonuclease, thereby safeguarding bacterial DNA from self-degradation.
Recombinant BglIIM is produced via heterologous expression, typically in *E. coli*, using genetic engineering techniques to clone and express the *bglIIM* gene. Its recombinant form retains the enzymatic activity of the native protein while offering higher purity and yield for research applications. Structurally, BglIIM belongs to the adenine-specific methyltransferase family, characterized by conserved motifs involved in SAM binding and catalysis.
In molecular biology, recombinant BglIIM is utilized to study DNA methylation effects on gene expression, protein-DNA interactions, and epigenetic regulation. It also serves as a tool to protect DNA from BglII restriction enzyme digestion during cloning experiments, enabling precise manipulation of DNA fragments. Additionally, its role in synthetic biology includes engineering methylation patterns to mimic epigenetic states or to bypass host restriction systems in transgenic organisms.
Research on BglIIM contributes to understanding the evolution of R-M systems and their biotechnological applications, such as developing methylation-specific diagnostics or enhancing DNA stability in gene therapy vectors. Its simplicity and specificity make it a valuable asset in both basic research and applied genetic engineering.
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