Hepatitis C Virus NS3 Antibody [N19B24]

Application: Reactivity: Hepatitis C Virus antigen NS3 helicase domain. Reacts very well with JFH-1 strain (genotype 2a)

Usage Information

Dilution
WB1:1000 IHC1:50

Application
WB, IHC, ELISA

Reactivity
Hepatitis C Virus antigen NS3 helicase domain. Reacts very well with JFH-1 strain (genotype 2a)

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
329 kDa 70 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Huh7 human hepatoma
Negative Control

Datasheet & SDS

Biological Description

Specificity
Hepatitis C Virus NS3 Antibody [N19B24] detects endogenous levels of total Hepatitis C Virus NS3 protein.

Clone
N19B24

Background
Hepatitis C Virus NS3 is a multifunctional non-structural protein essential for HCV replication, comprising an N-terminal serine protease domain (one-third of the protein) and a C-terminal superfamily 2 RNA helicase/NTPase domain, forming the viral replication complex in infected hepatocytes. The protease adopts a chymotrypsin-like fold with two β-barrels and a catalytic triad (His57, Asp81, Ser139), requiring NS4A cofactor for membrane anchoring and activation loop stabilization, while the helicase features three RecA-like domains (1-3) with conserved motifs (Q, Walker A/B) for ATP binding/hydrolysis and a unique α-helix-rich domain 3 for nucleic acid tracking; key residues include hydrophobic patches (Y105, P115, L127) on the protease for multiprotein interactions. It functions as protease-mediated cleavage of the viral polyprotein at NS3/4A, 4A/4B, 4B/5A, and 5A/5B junctions to liberate mature non-structural proteins (NS3-5B), essential for replicase assembly, alongside helicase unwinding of RNA duplexes (3'-5' direction) and displacement of bound proteins to facilitate genome replication and packaging into virions. NS3 coordinates multiprotein complexes for (-) strand RNA synthesis, NS5A hyperphosphorylation, and virion morphogenesis, hijacking host ER membranes while evading immunity via TLR3 modulation; pathways include post-translational processing, RNA replication with NS5A/NS5B, and innate response interference. Disease relevance centers on chronic hepatitis C leading to cirrhosis/hepatocellular carcinoma, with NS3 conservation making it a prime antiviral target ; mutations confer resistance, and its surface patches temporally regulate complex assembly for persistent infection.

Background

Hepatitis C Virus NS3 is a multifunctional non-structural protein essential for HCV replication, comprising an N-terminal serine protease domain (one-third of the protein) and a C-terminal superfamily 2 RNA helicase/NTPase domain, forming the viral replication complex in infected hepatocytes. The protease adopts a chymotrypsin-like fold with two β-barrels and a catalytic triad (His57, Asp81, Ser139), requiring NS4A cofactor for membrane anchoring and activation loop stabilization, while the helicase features three RecA-like domains (1-3) with conserved motifs (Q, Walker A/B) for ATP binding/hydrolysis and a unique α-helix-rich domain 3 for nucleic acid tracking; key residues include hydrophobic patches (Y105, P115, L127) on the protease for multiprotein interactions. It functions as protease-mediated cleavage of the viral polyprotein at NS3/4A, 4A/4B, 4B/5A, and 5A/5B junctions to liberate mature non-structural proteins (NS3-5B), essential for replicase assembly, alongside helicase unwinding of RNA duplexes (3'-5' direction) and displacement of bound proteins to facilitate genome replication and packaging into virions. NS3 coordinates multiprotein complexes for (-) strand RNA synthesis, NS5A hyperphosphorylation, and virion morphogenesis, hijacking host ER membranes while evading immunity via TLR3 modulation; pathways include post-translational processing, RNA replication with NS5A/NS5B, and innate response interference. Disease relevance centers on chronic hepatitis C leading to cirrhosis/hepatocellular carcinoma, with NS3 conservation making it a prime antiviral target ; mutations confer resistance, and its surface patches temporally regulate complex assembly for persistent infection.

References
https://pubmed.ncbi.nlm.nih.gov/8861916/ https://pubmed.ncbi.nlm.nih.gov/21250378/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%