The Minor Capsid Protein VP2 Antibody (PACO34634) is a specialized tool for researchers studying viral capsid proteins, specifically targeting the VP2 protein. This antibody is produced in rabbits and shows high reactivity with samples from various species, making it a versatile option for different experimental setups.VP2 is a crucial component of the viral capsid, playing a key role in viral replication and infection. By targeting this protein, researchers can gain insights into the mechanisms of viral entry, assembly, and pathogenesis. The Minor Capsid Protein VP2 Antibody enables the detection and analysis of VP2 in a variety of cell types, making it an invaluable tool for virology and infectious disease research.
Understanding the function of VP2 can provide important information for the development of antiviral therapies and vaccines. By studying the interactions of VP2 with host cells, researchers can uncover potential targets for intervention and new strategies for combating viral infections. The Minor Capsid Protein VP2 Antibody is a valuable resource for advancing our knowledge of viral biology and developing innovative approaches to viral disease control.
Antibody Name:
Minor capsid protein VP2 Antibody (PACO34634)
Antibody SKU:
PACO34634
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA
Recommended Dilutions:
Species Reactivity:
JC polyomavirus
Immunogen:
Recombinant JC polyomavirus Minor capsid protein VP2 protein (2-344AA)
Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. Isoform VP3:structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Isoform VP3 plays a role in virion assembly within the nucleus. May participate in host cell lysis when associated with VP4. Isoform VP4 is a viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion.
Synonyms:
Minor capsid protein VP2 (Minor structural protein VP2)
UniProt Protein Function:
Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly ().