The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application notesOptimal working dilutions are best determined by the investigator.
RelevanceThe hepatitis C virus (HCV) core protein represents the first 191 amino acids of the viral precursor polyprotein and is cotranslationally inserted into the membrane of the endoplasmic reticulum. Hepatitis C virus (HCV) core is a viral structural protein; it also participates in some cellular processes, including transcriptional regulation. However the mechanisms of core-mediated transcriptional regulation remain poorly understood. Hepatitis C virus (HCV) core protein is thought to contribute to HCV pathogenesis through its interaction with various signal transduction pathways. In addition, HCV core antigen is a recently developed marker of hepatitis C infection. The HCV core protein has been previously shown to circulate in the bloodstream of HCV-infected patients and inhibit host immunity through an interaction with gC1qR.
Hepatitis C Virus is a positive, single stranded RNA virus in the Flaviviridae family. The genome is approximately 10,000 nucleotides and encodes a single polyprotein of about 3,000 amino acids. The polyprotein is processed by host cell and viral proteases into three major structural proteins and several non structural proteins necessary for viral replication.
Hepatitis C virus (HCV) causes most cases of non-A, non-B hepatitis and results in most HCV infected people developing chronic infections, liver cirrhosis and hepatocellular carcinoma. T cell responses, including interferon-gamma production are severely suppressed in chronic HCV patients.
Cellular localizationEndoplasmic reticulum
Core protein p19 antibody
HCV core antigen antibody
HCV core protein antibody
Hepatitis C Virus core protein antibody
References for Anti-Hepatitis C Virus Core Antigen antibody [1F6] (Biotin) (ab2587)
This product has been referenced in:
Yang S et al. Defective mitophagy driven by dysregulation of rheb and KIF5B contributes to mitochondrial reactive oxygen species (ROS)-induced nod-like receptor 3 (NLRP3) dependent proinflammatory response and aggravates lipotoxicity. Redox Biol3:63-71 (2014).
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