Recombinant MPXV A30L Protein, ＞95% (SDS-PAGE), high purity

Item Number

rp155933

• Product Name: Recombinant MPXV A30L Protein, ＞95% (SDS-PAGE), high purity
• Synonyms: Envelope protein OPG155; Protein A30; OPG155; A30L; IMV surface protein A30L; Monkeypox virus A30L; Monkeypox virus
• Grade: Animal Free, Azide Free, Carrier Free
• Specifications & Purity: Animal Free, Carrier Free, Azide Free, ≥95%(SDS-PAGE)
• Purity: ＞95% (SDS-PAGE)
• Expression System: HEK293
• Species: Monkeypox virus
• Amino Acids: 26-146 aa
• Sequence: MIYENYGNIKEFNATHAAFEYSKSIGGTPALDRRVQDVNDTISDVKQKWRCVVYPGNGFVSASIFGFQAEVGPNNTRSIRKFNTMRQCIDFTFSDVINIDIYNPCIAPNINNTECQFLKSVLENLYFQGHHHHHH
• Protein Tag: C-His
• Accession #: Q8V4U9
• Predicted molecular weight: 15.5 kDa
• SDS-PAGE: 25-30 kDa, reducing conditions; 23-28 kDa, non-reducing conditions

Product Description

Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.
Envelope protein required for virus entry into host cell and for cell-cell fusion (syncytium formation).
Description：
Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A30L protein is required for the association of electron-dense, granular, proteinaceous material with the concave surfaces of crescent membranes, an early step in viral morphogenesis. The A30L protein is believed to be located in the matrix between the core and membrane. In vivo and in vitro experiments provided evidence for the direct interaction of the A30L and G7L proteins and demonstrated that the stability of each one was dependent on its association with the other. A presumption was that the A30L protein is a key element in the linkage between the viral core and the membrane. And some data indicate that protein-protein interactions are needed for the association of the dense viroplasm with IV membranes. Of the two interacting proteins identified, the G7L protein appears to be a component of the core whereas the A30L protein may be a component of the matrix between the core and membrane.