| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | amiB2 |
| Uniprot No | P9WQ97 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-462aa |
| 氨基酸序列 | MDPTDLAFAGAAAQARMLADGALTAPMLLEVYLQRIERLDSHLRAYRVVQFDRARAEAEAAQQRLDAGERLPLLGVPIAIKDDVDIAGEVTTYGSAGHGPAATSDAEVVRRLRAAGAVIIGKTNVPELMIMPFTESLAFGATRNPWCLNRTPGGSSGGSAAAVAAGLAPVALGSDGGGSIRIPCTWCGLFGLKPQRDRISLEPHDGAWQGLSVNGPIARSVMDAALLLDATTTVPGPEGEFVAAAARQPGRLRIALSTRVPTPLPVRCGKQELAAVHQAGALLRDLGHDVVVRDPDYPASTYANYLPRFFRGISDDADAQAHPDRLEARTRAIARLGSFFSDRRMAALRAAEVVLSSRIQSIFDDVDVVVTPGAATGPSRIGAYQRRGAVSTLLLVVQRVPYFQVWNLTGQPAAVVPWDFDGDGLPMSVQLVGRPYDEATLLALAAQIESARPWAHRRPSVS |
| 预测分子量 | 69.1 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amiB2重组蛋白相关的文献示例(部分信息经过概括整理，供参考)：
1. **文献名称**：*Functional characterization of the amidase AmiB2 in Mycobacterium tuberculosis*
**作者**：Viljoen A. et al.
**摘要**：研究揭示了结核分枝杆菌中AmiB2蛋白的酰胺酶活性，通过重组蛋白表达证实其参与细胞壁肽聚糖重塑，并发现其缺失导致细菌形态异常及抗生素敏感性增加。
2. **文献名称**：*Structural insights into the peptidoglycan hydrolysis mechanism of AmiB2*
**作者**：Yang Y. et al.
**摘要**：通过重组AmiB2蛋白的晶体结构解析，阐明了其底物结合域和催化机制，证明其具有特异性切割肽聚糖交联结构的功能，为开发新型抗菌药物提供理论依据。
3. **文献名称**：*Heterologous expression and purification of AmiB2 in E. coli for enzymatic assays*
**作者**：Goude R. et al.
**摘要**：报道了在大肠杆菌中高效表达可溶性AmiB2重组蛋白的优化方案，并通过体外酶活实验验证其水解活性，为后续功能研究提供标准化方法。
注：若需具体文献，建议通过学术数据库(如PubMed)以关键词 "AmiB2 recombinant protein" 或 "AmiB2 amidase" 检索最新研究。部分研究可能聚焦于病原菌的耐药机制或酶学特性分析。
AmiB2 is a recombinant protein derived from bacterial amidase enzymes, primarily studied for its role in cell wall metabolism and bacterial autolysis. Amidases are a class of enzymes that hydrolyze the amide bond between N-acetylmuramic acid and L-alanine in bacterial peptidoglycan, a critical process during cell division, growth, and programmed cell death. The AmiB2 variant, often sourced from *Streptococcus pneumoniae* or related Gram-positive pathogens, has garnered attention due to its unique structural and functional characteristics.
Structurally, AmiB2 contains conserved domains typical of amidases, including a catalytic domain with zinc-dependent hydrolase activity and a substrate-binding region. Its recombinant form is engineered for enhanced stability, solubility, and ease of purification, often expressed in *E. coli* systems with affinity tags (e.g., His-tag) for downstream applications. Studies highlight its modular architecture, which allows interaction with regulatory proteins or peptidoglycan fragments, influencing bacterial cell wall remodeling.
Functionally, AmiB2 plays dual roles: it contributes to cell separation during bacterial division by cleaving peptidoglycan crosslinks and acts as a signaling molecule in stress responses. Dysregulation of AmiB2 activity is linked to antibiotic tolerance phenotypes, making it a potential target for novel antimicrobial strategies. Research also explores its utility in biotechnology, such as enzymatic degradation of bacterial biofilms or as a tool in peptidoglycan structural analysis.
Current challenges include optimizing its activity under physiological conditions and understanding species-specific variations. Despite this, AmiB2 remains a promising candidate for both basic research and therapeutic development, bridging microbiology and protein engineering.
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