Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Activity

Not Test

Target Names

N/A

Uniprot No.

P03089

Research Area

Others

Alternative Names

Major structural protein VP1

Species

JC polyomavirus (JCPyV) (JCV)

Source

E.coli

Expression Region

1-354aa

Target Protein Sequence

MAPTKRKGERKDPVQVPKLLIRGGVEVLEVKTGVDSITEVECFLTPEMGDPDEHLRGFSKSISISDTFESDSPNRDMLPCYSVARIPLPNLNEDLTCGNILMWEAVTLKTEVIGVTSLMNVHSNGQATHDNGAGKPVQGTSFHFFSVGGEALELQGVLFNYRTKYPDGTIFPKNATVQSQVMNTEHKAYLDKNKAYPVECWVPDPTRNENTRYFGTLTGGENVPPVLHITNTATTVLLDEFGVGPLCKGDNLYLSAVDVCGMFTNRSGSQQWRGLSRYFKVQLRKRRVKNPYPISFLLTDLINRRTPRVDGQPMYGMDAQVEEVRVFEGTEELPGDPDMMRYVDKYGQLQTKML
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

43.7 kDa

Protein Length

Full Length

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

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.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.

Datasheet & COA

Please contact us to get it.

Target Background

Function

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 a N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids on the cell surface to provide virion attachment to target cell. The serotonergic receptor 5HT2AR also acts as a cellular receptor for JCV on human glial cells. Once attached, the virions enter predominantly by a ligand-inducible clathrin-dependent pathway and traffic to the ER. 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 at nuclear domains called promyelocytic leukemia (PML) bodies, and participates in rearranging nucleosomes around the viral DNA.

Gene References into Functions

All viral populations were characterized by rearrangements within the noncoding regulatory region (NCCR) and 1 point mutation, S267L in the VP1 gene, suggestive of neurotropic strains. One patient with Progressive multifocal leukoencephalopathy (PML) had a single neurotropic strain with rearranged noncoding regulatory region (NCCR), and 1 patient had a single strain with small NCCR alterations. PMID: 28453853
found that deletion of nucleotides 376-396 results in decreased levels of viral DNA replication and a lack of VP1 expression. PMID: 25142442
Synthetic antibodies and peptides recognizing progressive multifocal leukoencephalopathy-specific point mutations in polyomavirus JC capsid viral protein 1. PMID: 25879139
These data show that capsid proteins of Mad-1 and WT3 JC Polyomavirus can both engage alpha2,6-linked sialic acid on the lactoseries tetrasaccharide c as well as multiple sialylated gangliosides. PMID: 25855729
This study demonstrated that the 5-fold VP1 pore is an important structural feature of JC polyomavirus and that minor modifications to this structure have significant impacts on infectious entry. PMID: 25609820
C80 of JCV Vp1 is required for Vp1 stability and pentamer formation, and C247 is involved in capsid assembly in the nucleus PMID: 24130786
These results demonstrate that viruses from progressive multifocal leukoencephalopathy patients with single point mutations in VP1 disrupt binding to sialic acid motifs and render these viruses noninfectious. PMID: 23760462
VP1 C terminus mutants were replication-competent and remains stable overtime in vitro. PMID: 21940415
mutations of JCV VP1 might favor progressive multifocal leukoencephalopathy onset; VP1 substitutions may favor JCV brain invasion by abrogation of sialic acid binding with peripheral cells while maintaining sialic acid-independent binding with brain cells PMID: 21628664
model of the interaction between VP1 and the sialic acid component of the human JCV receptor PMID: 15347668
frequent amino acid substitutions in the outer loops of VP1 of JCPyV associated with progressive multifocal leukoencephalopathy (PML) PMID: 15958683
A unique deletion was found in the C terminus may be instrumental in facilitating entry or replication of JCV into granule cell neurons. PMID: 16894191
A possible role for merkel cells Polyomavirus as an etiologic agent in the carcinogenesis of merkel cell carcinoma. PMID: 18593898
JCV VP1 loop mutations are associated with a favorable prognosis for PML PMID: 19043822
several amino acids on surface of VP1 display accelerated evolution in viral sequences isolated from progressive multifocal leukoencephalopathy patients but not healthy subjects; evidence that some mutations are involved in binding of sialic acid PMID: 19197354

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Subcellular Location

Virion. Host nucleus.

Protein Families

Polyomaviruses coat protein VP1 family

Database Links

KEGG: vg:1489518

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Code	CSB-EP355946JAKa0
MSDS	MSDS
Size	$306
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant JC polyomavirus Major capsid protein VP1

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