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Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Plays an important role in virus-media

Fluorescent proteins have become a useful and ubiquitous tool for making chimeric proteins, where they function as a fluorescent protein tag. Typically they tolerate N- and C-terminal fusion to a broad variety of proteins. They have been expressed in most known cell types and are used as a noninvasive fluorescent marker in living cells and organisms. They enable a wide range of applications where they have functioned as a cell lineage tracer, reporter of gene expression, or as a measure of

KT3 epitope tag can be used to monitor expression of the protein products transfected with cDNA constructs.

E Tag is a commonly used epitope tag engineered onto the N- or C- terminus of a protein of interest so that the tagged protein can be analyzed and visualized.$nBecause of the small size of the epitope, it is unlikely to alter the activity of the cloned sequence.

HSV tag is a peptide epitope tag, sequence: QPELAPEDPED.

Vesicular stomatitis virus (VSV), an enveloped RNA virus from the Rhabdoviridae family, is released from the plasma membrane of host cells by a process called budding. The glycoprotein (VSV-g) contains a domain in its extracellular membrane proximal stem that appears to be needed for efficient VSV budding.