| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ENGASE |
| Uniprot No | Q8NFI3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-377aa |
| 氨基酸序列 | MEAAAVTVTRSATRRRRRQLQGLAAPEAGTQEEQEDQEPRPRRRRPGRSIKDEEEETVFREVVSFSPDPLPVRYYDKDTTKPISFYLSSLEELLAWKPRLEDGFNVALEPLACRQPPLSSQRPRTLLCHDMMGGYLDDRFIQGSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAFLAGDERSYQAVADRLVQITQFFRFDGWLINIENSLSLAAVGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQDELNQHNRVFFDSCDGFFTNYNWREEHLERMLGQAGERRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALFAPSCSVFPGVGNLLCC |
| 预测分子量 | 59.1 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. |
以下是关于ENGASE重组蛋白的3篇参考文献概览：
1. **"Characterization of a recombinant Endo-β-N-acetylglucosaminidase from *Streptomyces plicatus*"**
*作者：Robbins PW 等*
摘要：研究报道了从*Streptomyces plicatus*中克隆并表达重组ENGASE，分析了其酶学特性及在糖蛋白去糖基化中的应用，证实其高效切割复杂N-糖链的能力。
2. **"Expression and substrate specificity of human endo-β-N-acetylglucosaminidase (ENGase) in *E. coli*"**
*作者：Yamamoto K 等*
摘要：通过大肠杆菌系统成功表达人源ENGASE重组蛋白，系统评估其底物特异性，发现其对高甘露糖型和杂合型N-糖链具有选择性，为糖蛋白工程提供工具。
3. **"Crystal structure of ENGase reveals substrate recognition mechanism"**
*作者：Li H 等*
摘要：解析了重组ENGASE的晶体结构，阐明其活性位点与糖链结合的分子机制，为理性设计酶突变体以优化催化效率奠定基础。
提示：若需具体文献年份或DOI，可进一步补充关键词(如物种或应用方向)精确检索。
ENGASE (Endo-β-N-acetylglucosaminidase) is a glycoside hydrolase that specifically cleaves the β-1.4-glycosidic bond within the chitobiose core of N-linked glycans, a critical post-translational modification in eukaryotic proteins. This enzyme is widely distributed across organisms, including bacteria, fungi, plants, and animals, with functional roles in glycan processing, protein quality control, and host-pathogen interactions. Its ability to hydrolyze high-mannose and hybrid-type glycans without damaging the protein backbone makes it a valuable tool for glycobiology research, particularly in analyzing glycan structures and generating homogenous glycoproteins.
Recombinant ENGASE proteins are produced via heterologous expression systems such as *E. coli* or yeast, enabling scalable production and engineering for enhanced stability or substrate specificity. Bacterial-derived ENGASE (e.g., from *Streptococcus pneumoniae*) and fungal variants (e.g., from *Aspergillus oryzae*) are commonly utilized due to their distinct enzymatic properties. For instance, some isoforms exhibit thermostability or broad pH tolerance, expanding their applicability in industrial and therapeutic settings.
In biopharmaceutical development, ENGASE is employed to remodel glycans on therapeutic antibodies, reducing immunogenicity or optimizing effector functions. It also facilitates glycoengineering by trimming excess glycans to expose specific epitopes for downstream conjugation. Additionally, recombinant ENGASE serves as a critical reagent in glycoproteomics for site-specific deglycosylation, improving mass spectrometry analysis of glycoproteins. Recent studies further explore its potential in treating congenital disorders of glycosylation by rescuing misfolded glycoproteins. Ongoing research focuses on structure-function relationships and engineering mutant variants to expand its biocatalytic versatility for synthetic biology and precision medicine applications.
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