Anti-HHAV Protease 3C Polyclonal Antibody (VK802014) is a rabbit polyclonal antibody detecting Protease 3C. Suitable for Simian hepatitis A virus genotype V, Human hepatitis A virus genotype IIA, Human hepatitis A virus genotype IB, Human hepatitis A virus genotype IIIB, Human hepatitis A virus genotype IIB, Human hepatitis A virus genotype IA, and Human hepatitis A virus genotype IIIA.
Highlights
●Multi-Species — Cross-reactive for translational research.
Species reactivity
Hepatitis A virus (HAV)
Applications
ELISA, IHC, WB
Host species
Rabbit
Isotype
IgG
Clonality
Polyclonal
Immunogen
E. coli - derived recombinant HHAV Protease 3C (Ser1520-Gln1738).
Target
Assembly signal 2A, Capsid protein VP0, Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, Capsid protein VP4, EC:2.7.7.48, EC:3.4.22.28, EC:3.6.1.15, Genome polyprotein, P1A, P1B, P1C, P1D, P2B, P2C, P3, P3A, P3B, P3C, P3D-POL, Picornain 3C, Protease 3C, Protein 2B, Protein 2BC, Protein 2C, Protein 3A, Protein 3AB, Protein 3ABC, Protein 3ABCD, Protein 3B, Protein 3CD, Protein VP1-2A, RNA-directed RNA polymerase 3D-POL, VP4-VP2, VPX, VPg, Viral protein genome-linked, Virion protein 1, Virion protein 2, Virion protein 3, Virion protein 4, pX
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
Product Usage Information
Application
Dilution
ELISA
1:5000-1:20000
IHC
1:50-1:500
WB
1:500-1:2000
Background
Genome polyprotein (Protease 3C) is a ~251 kDa protein. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.
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