-
Recombinant Bacterial Outer Membrane Protein-A
Recombinant Bacterial Outer Membrane Protein-A
- 中文名称：
- Recombinant Bacterial Outer Membrane Protein-A
- 英文名称：
- Recombinant Bacterial Outer Membrane Protein-A
- 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：
- AAA38518
- 规格：
- 0.1 mg|0.2 mg|1 mg|2x1 mg|3x1 mg
- 保存建议：
- Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18 degree C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
- 货期：
- 6-8周
- 纯度：
- Greater than 98.0% as determined by: (a) Analysis by SEC-HPLC. (b) Analysis by SDS-PAGE.
- 产品形式：
- Sterile Filtered White lyophilized (freeze-dried) powder.
- 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 recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 48 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.
Introduction: The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA's major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
