| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GYPA |
| Uniprot No | P02724 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-150aa |
| 氨基酸序列 | MYGKIIFVLL LSAIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM AGVIGTILLI SYGIRRLIKK SPSDVKPLPS PDTDVPLSSV EIENPETSDQ |
| 预测分子量 | 43 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. |
以下是基于常见研究方向模拟的3-4条关于GYPA(血型糖蛋白A)重组蛋白的参考文献示例(注：以下为虚构内容，仅用于演示格式)：
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1. **文献名称**: "High-yield expression and purification of recombinant human GYPA in mammalian cells for structural studies"
**作者**: Chen L, et al.
**摘要**: 本研究在HEK293细胞中表达重组GYPA蛋白，优化分泌表达条件，通过亲和层析纯化获得高纯度蛋白。质谱分析证实其糖基化修饰与天然GYPA一致，为后续受体功能研究提供基础。
2. **文献名称**: "Crystal structure of the extracellular domain of GYPA reveals pathogen binding motifs"
**作者**: Gupta S, et al.
**摘要**: 解析了重组GYPA胞外段晶体结构(分辨率2.8Å)，发现其α-螺旋结构域包含保守的唾液酸结合位点，实验证实该区域与流感病毒血凝素特异性结合，阐明了GYPA在病原体感染中的作用机制。
3. **文献名称**: "Prokaryotic expression of functional GYPA for malaria invasion studies"
**作者**: Okeke C, et al.
**摘要**: 利用大肠杆菌表达系统获得非糖基化GYPA重组蛋白，通过体外实验证明其与疟原虫裂殖子表面蛋白PfRH5相互作用，提示GYPA可能作为疟疾治疗的潜在靶点。
4. **文献名称**: "Recombinant GYPA-based biosensor for blood type antigen detection"
**作者**: Wang Y, et al.
**摘要**: 开发了基于重组GYPA的免疫传感器，通过固定化GYPA蛋白高效识别抗-M/N抗体，实现快速、灵敏的血型分型，在临床输血检测中展示应用潜力。
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提示：实际文献需通过PubMed/Google Scholar检索关键词如"recombinant GYPA glycophorin"或结合具体研究领域筛选。
GYPA (Glycophorin A) is a transmembrane glycoprotein predominantly expressed on the surface of human erythrocytes, playing a critical role in maintaining red blood cell (RBC) membrane integrity and mediating cellular interactions. As a member of the glycophorin family, GYPA is encoded by the *GYPA* gene located on chromosome 4 and is heavily glycosylated, contributing to its antigenic properties. It serves as the carrier for the MN blood group antigens, which are clinically significant in transfusion medicine and prenatal testing. The protein comprises 131 amino acids, with an extracellular domain containing multiple O-linked glycans and a single N-linked glycosylation site, influencing pathogen adhesion and immune recognition.
Recombinant GYPA is engineered using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to study its structural and functional roles. Its production enables research into host-pathogen interactions, particularly with *Plasmodium falciparum* (malaria parasite) and influenza viruses, which exploit GYPA for RBC entry. Additionally, recombinant GYPA is utilized in developing blood typing assays, autoimmune disease studies (e.g., anti-RBC antibodies), and synthetic blood substitutes. Challenges in its production include preserving native glycosylation patterns critical for antigenicity, often addressed via mammalian cell lines like CHO or HEK293.
Beyond infectious disease research, GYPA’s role in cellular signaling, apoptosis, and membrane elasticity underscores its biomedical relevance. Recent studies also explore its potential as a biomarker in cancers with aberrant glycoprotein expression. The development of recombinant GYPA continues to advance understanding of erythrocyte biology, pathogen evasion mechanisms, and therapeutic interventions targeting glycan-mediated interactions.
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