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Updated Date: Stock Protein updated on 20170405
Research areas: Microbiology
Target / Protein: HA
Biologically active: Not Tested
Expression system: E.coli
Species of origin: Influenza A virus (strain A/Hickox/1940 H1N1)
Delivery time: 3-7 business days
Uniprot ID: Q0HD60
AA Sequence: DTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGKCNIAGWILGNPECESLLSKRSWSYIAETPNSENGTCYPGDFADYEELREQLSSVSSFERFEIFPKERSWPNHNINIGVTAACSHAGKSSFYKNLLWLTEKDGSYPNLNKSYVNKKEKEVLVLWGVHHPSNIENQKTLYRKENAYVSVVSSNYNRRFTPEIAERPKVRGQAGRMNYYWTLLEPGDTIIFEANGNLIAPWYAFALSRGLGSGIITSNASMDECDTKCQTPQGAINSSLPFQNIHPFTIGECPKYVRSTKLRMVTGLRNIPSIQS
Tag info: N-terminal 6xHis-SUMO-tagged
Expression Region: 18-343aa
Protein length: Full Length
MW: 52.6 kDa
Alternative Name(s): Cleaved into the following 2 chains: Hemagglutinin HA1 chain Hemagglutinin HA2 chain
Relevance: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. 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 induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore
Reference: "The NIAID influenza genome sequencing project."Spiro D., Ghedin E., Sengamalay N., Halpin R., Boyne A., Zaborsky J., Feldblyum T., Subbu V., Sparenborg J., Shumway M., Sitz J., Katzel D., Koo H., Salzberg S.L., Griesemer S., St George K., Bennett R., Taylor J. Tatusova T.Submitted (AUG-2006)
Purity: Greater than 90% as determined by SDS-PAGE.
Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.