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H9784

Sigma-Aldrich

Hepatitis C virus NS4 antigen−Rhodamine

~1 mg/mL, ≥95% (SDS-PAGE), recombinant, expressed in E. coli, solution

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

assay

≥95% (SDS-PAGE)

form

solution

mol wt

19 kDa (plus 114 kDa β-Gal tag)

concentration

~1 mg/mL

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

hepatitis C virus ... HCVgp1(951475)

General description

β-gal fused at N-terminus
HCVgp1 (hepatitis C virus glycoprotein 1), also referred to as polyprotein, is crucial for the induction of double-membrane vesicles, which are sites of HCV RNA amplification. The amino terminal of polyprotein contains the structural proteins core, envelope protein 1 (E1) and E2.[1] The proteolytic cleavage of polyprotein results in the formation of 10 mature viral proteins, including NS4 (non-structural 4).[2][3]

Biochem/physiol Actions

NS4 (non-structural 4) mainly acts a cofactor for the NS3 serine protease, which is needed for the cleavage of the non-structural area of the polyprotein. It also suppresses host cell translation as well as proliferation. In addition, it induces anti-inflammatory cytokines and thereby suppresses cellular immune responses.[4]
Positive control for HCV antibodies.

Other Notes

HCV NS4a+b [1658-1863]-Galactosidase-tagged, rhodamine conjugate.

Physical form

Solution in 8 M urea, 20 mM tris-HCl, pH 8.0, and 10 mM 2-mercaptoethanol.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Miriam T Brady et al.
European journal of immunology, 33(12), 3448-3457 (2003-11-25)
The majority of hepatitis C virus (HCV) infections become chronic, despite the presence of HCV-specific cellular and humoral immune responses. We have previously suggested that IL-10-secreting antigen-specific regulatory T cells may contribute to viral persistence, and demonstrate here that peripheral
R Bartenschlager et al.
Journal of virology, 69(12), 7519-7528 (1995-12-01)
Processing of the hepatitis C virus polyprotein is mediated by host cell signalases and at least two virally encoded proteinases. Of these, the serine-type proteinase encompassing the amino-terminal one-third of NS3 is responsible for cleavage at the four sites carboxy
Inés Romero-Brey et al.
mBio, 6(4), e00759-e00759 (2015-07-15)
Induction of membrane rearrangements in the cytoplasm of infected cells is a hallmark of positive-strand RNA viruses. These altered membranes serve as scaffolds for the assembly of viral replication factories (RFs). We have recently shown that hepatitis C virus (HCV)
Margaret A Scull et al.
PLoS pathogens, 11(11), e1005297-e1005297 (2015-11-21)
The hepatitis C virus (HCV) p7 protein is required for infectious virus production via its role in assembly and ion channel activity. Although NMR structures of p7 have been reported, the location of secondary structural elements and orientation of the

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