Active Hepatitis A virus VP1 protein protein fragment (ab68635)
- Product nameActive Hepatitis A virus VP1 protein protein fragment
- SourceE. coli
- Amino Acid Sequence
- Amino acids502 to 605
Our Abpromise guarantee covers the use of ab68635 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Biological activityab68635 is immunoreactive with sera from HAV-infected individuals.
- Purity> 90
% by SDS-PAGE.
ab68635 was purified by a proprietary chromatographic technique.
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Constituents: 10mM Calmodulin Binding buffer (25 mM Tris (pH 8.0). recipe 150 mM NaCl. 1 mM magnesium acetate. 1 mM imidazole), 50% Glycerol, 0.1% SDS, pH 9.6
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- HAV VP1
- Protein VP1
- Virion protein 1
- RelevanceHepatitis A virus (HAV) is the sole member of the Hepatovirus genus within the family Picornaviridae. The capsid of HAV encloses a single-stranded RNA genome of about 7.5 kb which is translated into a single polyprotein. The virion proteins VP1 to VP4 and the nonstructural proteins are generated from the polyprotein by a cascade of proteolytic cleavages. Only one protease, viral protease 3C, has been implicated in the nine protein scissions. Processing of the capsid protein precursor region generates a unique intermediate, PX (VP1-2A), which accumulates in infected cells and is assumed to serve as precursor to VP1 found in virions, although the details of this reaction have not been determined. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. VP1 is a major viral antigen.
- Cellular localizationCytoplasmic
References for Active Hepatitis A virus VP1 protein protein fragment (ab68635)
ab68635 has not yet been referenced specifically in any publications.