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Hamster polyomavirus (HaPyV) VP1 Protein (His & Myc)

Catalog No. TMPH-00789

Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.

Hamster polyomavirus (HaPyV) VP1 Protein (His & Myc)

Hamster polyomavirus (HaPyV) VP1 Protein (His & Myc)

Catalog No. TMPH-00789
Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.
Pack SizePriceAvailabilityQuantity
20 μg$36020 days
100 μg$67820 days
1 mg$2,30020 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.
Species
HaPyV
Expression System
E. coli
TagN-10xHis, C-Myc
Accession NumberP03092
Synonyms
Major structural protein VP1,Major capsid protein VP1
Amino Acid
MCKPLWKPCPKPANVPKLIMRGGVGVLDLVTGEDSITQIEAYLNPRMGQNKPGTGTDGQYYGFSQSIKVNSSLTADEVKANQLPYYSMAKIQLPTLNEDLTCDTLQMWEAVSVKTEVVGVGSLLNVHGYGSRSETKDIGISKPVEGTTYHMFAVGGEPLDLQGLVQNYNANYEAAIVSIKTVTGKAMTSTNQVLDPTAKAKLDKDGRYPIEIWGPDPSKNENSRYYGNFTGGTGTPPVMQFTNTLTTVLLDENGVGPLCKGDGLYLSAADVMGWYIEYNSAGWHWRGLPRYFNVTLRKRWVKNPYPVTSLLASLYNNMLPTIEGQPMEGEAAQVEEVRIYEGTEAVPGDPDVNRFIDKYGQQHTKPPAKPAN
Construction
1-372 aa
Protein Purity
> 85% as determined by SDS-PAGE.
Molecular Weight48.3 kDa (predicted)
FormulationIf 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
Reconstitute the lyophilized protein in sterile deionized water. The product concentration should not be less than 100 μg/mL. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background
Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.

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