Recombinant Influenza C virus Hemagglutinin-esterase-fusion glycoprotein (HE), partial

SKU: P07971

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Signal Transduction

Uniprot ID: P07971

Gene Names: HE

Alternative Name(s): (HEF)(HEF1)(HEF2)

Abbreviation: Recombinant Influenza C virus Hemagglutinin-esterase-fusion glycoprotein, partial

Organism: Influenza C virus (strain C/Great lakes/1167/1954)

Source: E.coli

Expression Region: 2-433aa

Protein Length: Partial

Tag Info: N-terminal 10xHis-tagged

Target Protein Sequence: EKIKICLQKQANSSFSLHNGFGGNLYATEEKRMFELVKPKAGASVLNQSTWIGFGDSRTDKSNSAFPRSADVSAKTADKFRSLSGGSLMLSMFGPPGKVDYLYQGCGKHKVFYEGVNWSPHAAIDCYRKNWTDIKLNFQKNIYELASQSHCMSLVNALDKTIPLQVTAEVAKNCNNSFLKNPALYTQEVNPSKQICGEENLAFFTLPTQFGTYECKLHLVASCYFIYDSKEVYNKRGCDNYFQVIYDSSGKVVGGLDNRVSPYTGNTGDTPTMQCDMLQLKPGRYSVRSSPRFLLMPERSYCFDMKEKGLVTAVQSVWGKGRKSDYAVDQACLSTPGCMLIQKQKPYIGEADDHHGDQEMRELLSGLDYEARCISQSGWVNETSPFTEEYLLPPKFGRCPLAAKEESIPKIPDGLLIPTSGTDTTVTKPKSR

MW: 54.2 kDa

Purity: Greater than 90% as determined by SDS-PAGE.

Endotoxin: Not test

Biological_Activity:

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.

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.

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.

Relevance: Capsid protein VP0: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis. Binds packaging signals present in the viral RNA. ; Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP0 and VP1. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis. Binds packaging signals present in the viral RNA. ; Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP0 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis. Binds packaging signals present in the viral RNA. ; Protein 2A H-NC: Is not a protease. ; Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. ; Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. ; Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface. Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place. ; Viral protein genome-linked: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2. During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions. ; Protease 3C: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. ; RNA-directed RNA polymerase 3D-POL: Replicates the viral genomic RNA on the surface of intracellular membranes. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.

Reference: "A comparative analysis of parechovirus protein structures with other picornaviruses." Domanska A., Guryanov S., Butcher S.J. Open Biol. 11: 210008-210008(2021)

Function: