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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Gly |
| Uniprot No | P34896 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-483aa |
| 氨基酸序列 | MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGLPDF |
| 预测分子量 | 53 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. |
以下是关于重组糖蛋白(假设"Gly"指糖蛋白，glycoprotein)的参考文献示例，包含文献名称、作者及摘要概述：
1. **《Recombinant glycoprotein production in mammalian cell cultures: engineering sialylation》**
*作者：Jenkins, N., et al.*
**摘要**：探讨在哺乳动物细胞培养中优化重组糖蛋白唾液酸化水平的策略，分析糖基化模式对药物药代动力学的影响。
2. **《Efficient expression of SARS-CoV-2 spike glycoprotein in insect cells for vaccine development》**
*作者：Watanabe, Y., et al.*
**摘要**：报道利用杆状病毒-昆虫细胞系统高效表达新冠病毒刺突糖蛋白，验证其作为疫苗候选抗原的免疫原性。
3. **《Glycosylation and stability of recombinant human erythropoietin》**
*作者：Egrie, J.C., et al.*
**摘要**：研究糖基化修饰对重组人促红细胞生成素(rhEPO)稳定性和体内活性的作用，比较不同宿主表达系统的糖型差异。
4. **《CHO cell engineering for improved therapeutic glycoprotein production》**
*作者：Hossler, P., et al.*
**摘要**：综述通过基因编辑和代谢工程优化CHO细胞，提升重组治疗性糖蛋白的产量和质量控制策略。
注：若“Gly”特指其他含义(如甘氨酸标签蛋白)，建议进一步明确关键词以便精准检索。
**Background of Glycoengineered Recombinant Proteins**
Glycoengineered recombinant proteins are genetically modified proteins designed with tailored glycosylation patterns, a critical post-translational modification where carbohydrate chains (glycans) are attached to specific amino acid residues. Glycosylation profoundly influences protein stability, solubility, immunogenicity, and interactions with cellular receptors. Recombinant protein technology enables their production in heterologous systems (e.g., mammalian cells, yeast, or plants), bypassing limitations of natural sources.
Historically, therapeutic proteins (e.g., antibodies, hormones) produced in non-human systems faced challenges due to incompatible glycosylation, leading to reduced efficacy or immune reactions. For example, early erythropoietin (EPO) therapies derived from non-mammalian systems exhibited poor activity. Advances in glycoengineering now allow precise control over glycan structures by modifying host cell glycosylation pathways or using enzymes to remodel glycans post-production. Mammalian systems like CHO cells remain dominant for human-like glycosylation, while engineered yeast (e.g., *Pichia pastoris*) and plant platforms offer cost-effective alternatives.
Applications span therapeutics, vaccines, and diagnostics. Glycoengineered monoclonal antibodies with optimized Fc glycosylation show enhanced antibody-dependent cellular cytotoxicity (ADCC) in cancer treatments. In vaccines, viral glycoproteins (e.g., HIV gp120. SARS-CoV-2 spike) are engineered to present immunodominant glycan-epitopes. Additionally, modulating glycosylation improves pharmacokinetics, such as prolonging serum half-life via sialic acid capping.
Challenges persist in ensuring glycosylation consistency, as heterogeneity can arise from culture conditions or host variability. Analytical tools (mass spectrometry, HPLC) are critical for quality control. Ongoing research focuses on automating glycan design and expanding "humanized" glycosylation in non-mammalian systems. Glycoengineered recombinant proteins thus represent a cornerstone of precision biologics, balancing functionality, safety, and scalability.
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