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

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 Size	Availability	Price/USD
20 μg	20 days	$ 360.00
100 μg	20 days	$ 678.00
1 mg	20 days	$ 2,300.00

Pack Size

Availability

Price/USD

Quantity

20 μg

20 days

$ 360.00

100 μg

20 days

$ 678.00

1 mg

20 days

$ 2,300.00

Description

Species	HaPyV
Expression System	E. coli
Tag	N-terminal 10xHis-tagged and C-terminal Myc-tagged
Accession Number	P03092
Amino Acid	MCKPLWKPCPKPANVPKLIMRGGVGVLDLVTGEDSITQIEAYLNPRMGQNKPGTGTDGQYYGFSQSIKVNSSLTADEVKANQLPYYSMAKIQLPTLNEDLTCDTLQMWEAVSVKTEVVGVGSLLNVHGYGSRSETKDIGISKPVEGTTYHMFAVGGEPLDLQGLVQNYNANYEAAIVSIKTVTGKAMTSTNQVLDPTAKAKLDKDGRYPIEIWGPDPSKNENSRYYGNFTGGTGTPPVMQFTNTLTTVLLDENGVGPLCKGDGLYLSAADVMGWYIEYNSAGWHWRGLPRYFNVTLRKRWVKNPYPVTSLLASLYNNMLPTIEGQPMEGEAAQVEEVRIYEGTEAVPGDPDVNRFIDKYGQQHTKPPAKPAN Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Construction	1-372 aa
Protein Purity	> 85% as determined by SDS-PAGE.
Molecular Weight	48.3 kDa as predicted

Formulation	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	A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage	Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shipping	In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
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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Hamster polyomavirus (HaPyV) VP1 Protein (His & Myc)

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