| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GYPC |
| Uniprot No | P04921-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-57aa |
| 氨基酸序列 | MWSTRSPNST AWPLSLEPDP GMASASTTMH TTTIAEPDPG MSGWPDGRME TSTPTIM |
| 预测分子量 | 8 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GYPC重组蛋白的参考文献示例(注：内容为模拟虚构，仅用于格式参考)：
1. **文献名称**：*Recombinant Expression and Functional Characterization of Human Glycophorin C in Erythrocyte Membrane Assembly*
**作者**：Smith J, et al.
**摘要**：本研究通过大肠杆菌系统成功表达重组GYPC蛋白，并验证其与红细胞膜骨架蛋白4.1R的结合能力，揭示了GYPC在维持细胞膜机械稳定性中的关键作用。
2. **文献名称**：*Structural Insights into GYPC-Mediated Plasmodium falciparum Invasion Using Recombinant Protein Domains*
**作者**：Li X, et al.
**摘要**：通过昆虫细胞表达系统获得高纯度GYPC胞外域重组蛋白，结合X射线晶体学解析其与疟原虫侵袭蛋白PfRh4的互作界面，为抗疟药物设计提供结构基础。
3. **文献名称**：*Development of a GYPC-Based ELISA for Detecting Autoantibodies in Hereditary Elliptocytosis*
**作者**：Garcia R, et al.
**摘要**：利用哺乳动物细胞表达的重组GYPC蛋白建立新型诊断方法，可特异性检测遗传性椭圆形红细胞增多症患者血清中的自身抗体，显著提升临床诊断灵敏度。
4. **文献名称**：*Optimization of Recombinant GYPC Production in Pichia pastoris for Vaccine Development*
**作者**：Wang Y, et al.
**摘要**：通过毕赤酵母表达系统优化GYPC重组蛋白的分泌表达，证明其在小鼠模型中可诱导针对疟疾抗原的强效中和抗体，提示其作为候选疫苗的潜力。
(注：以上文献信息为模拟生成，实际引用请通过学术数据库检索确认。)
GYPC recombinant protein is derived from the glycophorin C (GPC) and glycophorin D (GPD) antigens encoded by the *GYPC* gene, which is located on human chromosome 2q14-q21. These transmembrane sialoglycoproteins are primarily expressed on the surface of erythrocytes and play critical roles in maintaining membrane integrity, cellular adhesion, and signal transduction. GPC and GPD, generated through alternative splicing of the *GYPC* transcript, are part of the Gerbich blood group system and serve as receptors for pathogens, including *Plasmodium falciparum* malaria parasites. Their extracellular domains contain conserved O-glycosylation sites, which are essential for ligand interactions and antigenic specificity.
The recombinant form of GYPC is typically produced using expression systems like *E. coli* or mammalian cell lines (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, particularly glycosylation. Purification involves affinity chromatography tags (e.g., His-tag) followed by validation via SDS-PAGE, Western blotting, or mass spectrometry. Structurally, recombinant GYPC retains the N-terminal extracellular domain (∼60 kDa for GPC; ∼30 kDa for GPD), a single transmembrane helix, and a short cytoplasmic tail, mirroring native protein topology.
Research applications of GYPC recombinant protein span blood typing, malaria pathogenesis studies, and investigations into rare Gerbich-related hemolytic disorders. It also serves as a tool to study cellular senescence and tumorigenesis, as GYPC expression is altered in certain cancers. Additionally, it aids in developing diagnostic assays for autoimmune hemolytic anemia and evaluating therapeutic antibodies. The protein's role in *Plasmodium* invasion mechanisms has spurred interest in antimalarial drug design. By enabling structure-function analysis, recombinant GYPC provides insights into erythrocyte biology and disease mechanisms while circumventing challenges associated with isolating native proteins from blood samples.
×
