Alternative Name(s):

HE; Hemagglutinin-esterase-fusion glycoprotein; HEF; EC 3.1.1.53) [Cleaved into: Hemagglutinin-esterase-fusion glycoprotein chain 1; HEF1); Hemagglutinin-esterase-fusion glycoprotein chain 2; HEF2)]

Species: (Organism)

Influenza C virus (strain C/California/1978)

Gene Names:

HE

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

EKIKICLQKQVNSSFSLHNGFGGNLYATEEKRMFELVKPKAGASVLNQSTWIGFGDSRTDQSNSAFPRSLMSAKTADKFRSLSGGSLMLSMFGPPGKVDYLYQGCGKHKVFYEGVNWSPHAAIDCYRKNWTDIKLNFQKSIYELASQSHCMSLVNALDKTIPLQVTKGVAKNCNNSFLKNPALYTQEVKPLEQICGEENLAFFTLPTQFGTYECKLHLVASCYFIYDSKEVYNKRGCGNYFQVIYDSSGKVVGGLDNRVSPYTGNSGDTPTMQCDMLQLKPGRYSVRSSPRFLLMPERSYCFDMKEKGPVTAVQSIWGKGRKSDYAVDQACLSTPGCMLIQKQKPYIGEADDHHGDQEMRELLSGLDYEARCISQSGWVNETSPFTEEYLLPPKFGRCPLAAKEESIPKIPDGLLIPTSGTDTTVTKPKSRIFGIDDLIIGLLFVAIVEAGIGGYLLGSRKESGGGVTKESAEKGFEKIGNDIQILRSSTNIAIEKLNDRISHDEQAIRDLTLEIENARSEALLGELGIIRALLVGNISIGLQESLWELASEITNRAGDLAVEVSPGCWIIDNNICDQSCQNFIFKFNETAPVPTIPPLDTKIDLQSDPFYWGSS

Expression Region:

15-629aa

Subcellular Location:

Virion membrane, Single-pass type I membrane protein, Host cell membrane, Single-pass type I membrane protein

Tissue Specificity:

Protein Length:

Extracellular Domain

Pathway:

Mol. Weight:

70.1 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:

Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O-acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell.

Involvement in disease:

Relevance:

Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the mbrane of the endocytosed virus particle with the endosomal mbrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O-acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to 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:

Influenza viruses hemagglutinin family

Reference:

Influenza C virus hemagglutinin comparison with influenza A and B virus hemagglutinins.Nakada S., Creager R.S., Krystal M., Aaronson R.P., Palese P.J. Virol. 50:118-124(1984)