纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | STT3B |
Uniprot No | Q8TCJ2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-225 aa |
活性数据 | MSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRTLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKIFKKTV |
分子量 | 52.7 kDa |
蛋白标签 | GST-tag at N-terminal |
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. |
以下是关于重组人STT3B蛋白的模拟参考文献(注:以下内容为示例,非真实文献):
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1. **文献名称**:*Structural and Functional Analysis of Human STT3B in Oligosaccharyltransferase Complex*
**作者**:Smith J, et al.
**摘要**:本研究解析了重组人STT3B蛋白的晶体结构,揭示其作为寡糖基转移酶(OST)复合体催化亚基的关键活性位点,并通过体外实验证明STT3B在N-糖基化起始中的特异性底物识别机制。
2. **文献名称**:*STT3B Deficiency Disrupts Endoplasmic Reticulum Protein Glycosylation and Promotes Tumor Metastasis*
**作者**:Lee H, et al.
**摘要**:通过重组STT3B蛋白的功能回补实验,发现其缺失导致ER中异常蛋白质糖基化,激活未折叠蛋白反应(UPR),并增强癌细胞迁移能力,提示STT3B在肿瘤微环境中的潜在调控作用。
3. **文献名称**:*Recombinant Expression of Human STT3B in HEK293 Cells for Glycoengineering Applications*
**作者**:Wang Y, et al.
**摘要**:报道了在HEK293细胞中高效表达重组人STT3B蛋白的方法,验证其酶活性,并应用于优化抗体类药物的糖基化修饰,提高其稳定性与疗效。
4. **文献名称**:*A Novel STT3B Mutation Causes Congenital Disorder of Glycosylation with Neurological Impairment*
**作者**:Garcia R, et al.
**摘要**:发现一种STT3B突变导致先天性糖基化紊乱(CDG),通过体外重组蛋白实验证明该突变削弱OST复合体活性,阐明了患者神经系统症状的分子机制。
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**说明**:以上文献为模拟生成,实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。
**Background of Recombinant Human STT3B Protein**
STT3B (STT3 Oligosaccharyltransferase Complex Catalytic Subunit B) is a key enzyme involved in N-linked protein glycosylation, a fundamental post-translational modification essential for protein folding, stability, and cellular recognition. It is part of the oligosaccharyltransferase (OST) complex located in the endoplasmic reticulum (ER) membrane. STT3B, encoded by the *STT3B* gene in humans (chromosome 3q21.2), acts as the catalytic subunit, transferring preassembled oligosaccharides from lipid-linked donors to specific asparagine residues (Asn-X-Ser/Thr motifs) on nascent polypeptides.
Unlike its paralog STT3A, which primarily glycosylates co-translationally translated proteins, STT3B is implicated in post-translocational glycosylation, targeting partially translocated or misfolded proteins for retrotranslocation and quality control. This functional divergence highlights its role in glycoprotein fidelity and ER-associated degradation (ERAD). Structurally, STT3B contains multiple transmembrane domains and conserved catalytic residues critical for enzymatic activity.
Mutations in *STT3B* are linked to congenital disorders of glycosylation (CDG), characterized by developmental delays and multisystem abnormalities. Additionally, aberrant STT3B expression is associated with cancers, where altered glycosylation impacts tumor progression and immune evasion.
Recombinant human STT3B protein, produced via heterologous expression systems (e.g., HEK293 cells), is widely used in biochemical studies to dissect glycosylation mechanisms, screen therapeutic inhibitors, or engineer glycosylation pathways in biopharmaceutical production. Its study offers insights into ER biology, disease mechanisms, and therapeutic targeting of glycosylation-related pathologies.
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