Hepatitis A Virus Coat Protein VP1
recombinant, E. coli
For in vitro use only!
Shipping: shipped on blue ice
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: 48 kDa
Purity: > 90 % (SDS-PAGE)
Form: liquid (Supplied in 10 mM CBB pH 9.6, 0.1% SDS and 50% glycerol)
Recombinant HAV-VP1 Antigen may be used in ELISA and Western blots, excellent for detection of HAV with minimal specificity problems.
The E.coli derived 48 kDa recombinant protein contains the VP1 immunodominant regions, amino acids 502-605. Hepatitis A Virus VP1 protein is purified by proprietary chromatographic techniques.
Background: HAV, the prototype of the genus Hepatovirus, belongs to the family Picornaviridae. Its 7.5-kb single-stranded RNA genome bears different distinct regions: the 5' and 3' noncoding regions (NCR), the P1 region, which encodes the structural proteins VP1, VP2, VP3, and a putative VP4, and the P2 and P3 regions encoding nonstructural proteins associated with replication. Hepatitis A virus (HAV) encodes a single polyprotein which is posttranslationally processed into the functional structural and nonstructural proteins. Only one protease, viral protease 3C, has been implicated in the nine protein scissions.
Specificity: Immunoreactive with sera of HAV-infected individuals.
Haro et al. (2003) Liposome entrapment and immunogenic studies of a synthetic lipophilic multiple antigenic peptide bearing VP1 and VP3 domains of the hepatitis A virus: a robust method for vaccine design. FEBS Lett. 540:133.
Costa-Mattioli et al. (2002) Molecular evolution of hepatitis A virus: a new classification based on the complete VP1 protein. J. Virol. 76:9516.
Emerson et al. (2002) Identification of VP1/2A and 2C as virulence genes of hepatitis A virus and demonstration of genetic instability of 2C. J. Virol. 76:8551.
Kang et al. (2002) A proposed vestigial translation initiation motif in VP1 of hepatitis A virus. Virus Res. 87:11.
Martin et al. (1999) Maturation of the hepatitis A virus capsid protein VP1 is not dependent on processing by the 3Cpro proteinase. J. Virol. 73:6220.
Graff et al. (1999) Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus. J. Virol. 73:6015.