-
Recombinant Hepatitis A Virus VP1-P2A (669-782)
Recombinant Hepatitis A Virus VP1-P2A (669-782)
- 中文名称：
- Recombinant Hepatitis A Virus VP1-P2A (669-782)
- 英文名称：
- Recombinant Hepatitis A Virus VP1-P2A (669-782)
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA38295
- 规格：
- 0.1 mg|0.5 mg|1 mg|2x1 mg|3x1 mg
- 保存建议：
- HAV VP1-P2A protein although stable at 4 degree C for 1 week, should be stored below -18 degree C. Please prevent freeze thaw cycles.
- 货期：
- 6-8周
- 纯度：
- HAV VP1-P2A protein is >90% pure as determined by 10% PAGE (coomassie staining).
HAV VP1-P2A protein was purified by proprietary chromatographic technique.
- 产品形式：
- 10mM Tris-HCl, pH 9.6, 1.5M urea, 50% glycerol.
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
Description: The E Coli derived recombinant protein contains the VP1-P2A immunodominant regions, amino acids 669-782.
Introduction: Forty-two antigenic domains were identified across the hepatitis A virus (HAV) polyprotein by using a set of 237 overlapping 20-mer synthetic peptides spanning the entire HAV polyprotein. Nineteen antigenic domains were found within the structural proteins, and 22 were found within the nonstructural proteins, with 1 domain spanning the junction of VP1 and P2A proteins. Five of these domains were considered immunodominant, as judged by both the breadth and the strength of their immunoreactivity. One domain is located within the VP2 protein at position 57-90 aa. A second domain, located at position 767-842 aa, contains the C-terminal part of the VP1 protein and the entire P2A protein. A third domain, located at position 1403-1456 a.a, comprises the C-terminal part of the P2C protein and the N-terminal half of the P3A protein. The fourth domain, located at position 1500-1519 a.a, includes almost the entire P3B, and the last domain, located at position 1719-1764 aa, contains the C-terminal region of the P3C protein and the N-terminal region of the P3D protein. Four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.
