Alternative Name(s):

Genome polyprotein [Cleaved into: Core protein p21; Capsid protein C; p21); Core protein p19; Envelope glycoprotein E1; gp32; gp35); Envelope glycoprotein E2; NS1; gp68; gp70); p7; Protease NS2-3; p23; EC 3.4.22.-); Serine protease NS3; EC 3.4.21.98; EC 3.6.1.15; EC 3.6.4.13; Hepacivirin; NS3P; p70); Non-structural protein 4A; NS4A; p8); Non-structural protein 4B; NS4B; p27); Non-structural protein 5A; NS5A; p56); RNA-directed RNA polymerase; EC 2.7.7.48; NS5B; p68)]

Species: (Organism)

Hepatitis C virus genotype 1a (isolate 1) (HCV)

Gene Names:

N/A

Tag info:

C-terminal 6xHis-Myc-tagged

Target Protein AA Sequence:

YQVRNSTGLYHVTNDCPNSSIVYEAADAILHTPGCVPCVREGNASRCWVAMTPTVATRDGKLPATQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSIYPGHITGHRMAWDMMMN

Expression Region:

192-325aa

Subcellular Location:

Core protein p21: Host endoplasmic reticulum membrane, Single-pass membrane protein, Host mitochondrion membrane, Single-pass type I membrane protein, Host lipid droplet, Note=The C-terminal transmembrane domain of core protein p21 contains an ER signal leading the nascent polyprotein to the ER membrane, Only a minor proportion of core protein is present in the nucleus and an unknown proportion is secreted, SUBCELLULAR LOCATION: Core protein p19: Virion, Host cytoplasm, Host nucleus, Secreted, SUBCELLULAR LOCATION: Envelope glycoprotein E1: Virion membrane, Single-pass type I membrane protein, Host endoplasmic reticulum membrane, Single-pass type I membrane protein, Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase, After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor, A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain, These events explain the final topology of the protein, ER retention of E1 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane, SUBCELLULAR LOCATION: Envelope glycoprotein E2: Virion membrane, Single-pass type I membrane protein, Host endoplasmic reticulum membrane, Single-pass type I membrane protein, Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase, After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor, A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain, These events explain the final topology of the protein, ER retention of E2 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane, SUBCELLULAR LOCATION: p7: Host endoplasmic reticulum membrane, Multi-pass membrane protein, Host cell membrane, Note=The C-terminus of p7 membrane domain acts as a signal sequence, After cleavage by host signal peptidase, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor, Only a fraction localizes to the plasma membrane, SUBCELLULAR LOCATION: Protease NS2-3: Host endoplasmic reticulum membrane, Multi-pass membrane protein, SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic reticulum membrane, Peripheral membrane protein, Note=NS3 is associated to the ER membrane through its binding to NS4A, SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic reticulum membrane, Single-pass type I membrane protein, Note=Host membrane insertion occurs after processing by the NS3 protease, SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic reticulum membrane, Multi-pass membrane protein, SUBCELLULAR LOCATION: Non-structural protein 5A: Host endoplasmic reticulum membrane, Peripheral membrane protein, Host cytoplasm, host perinuclear region, Host mitochondrion, Note=Host membrane insertion occurs after processing by the NS3 protease, SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host endoplasmic reticulum membrane, Single-pass type I membrane protein

Tissue Specificity:

Protein Length:

Partial

Pathway:

Mol. Weight:

18.7 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Others

Function:

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. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response

Involvement in disease:

Relevance:

Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with HAVCR1 to provide virion attachment to target cell.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Hepacivirus polyprotein family

Reference:

Genetic relatedness of hepatitis A virus strains recovered from different geographical regions.Robertson B.H., Jansen R.W., Khanna B., Totsuka A., Nainan O.V., Siegl G., Widell A., Margolis H.S., Isomura S., Ito K., Ishizu T., Moritsugu Y., Lemon S.M.J. Gen. Virol. 73:1365-1377(1992)