Recombinant JC polyomavirus Major capsid protein VP1
貨號:
CSB-YP355946JAK
規格:
來源:
Yeast
其他:
在線留言
中文名稱:
Recombinant JC polyomavirus Major capsid protein VP1
貨號:
CSB-EP355946JAK
規格:
來源:
E.coli
其他:
在線留言
中文名稱:
Recombinant JC polyomavirus Major capsid protein VP1
貨號:
CSB-EP355946JAK-B
規格:
來源:
E.coli
共軛:
Avi-tag Biotinylated
E. coli biotin ligase
(BirA) is highly specific in covalently attaching biotin to the 15
amino
acid AviTag peptide. This recombinant protein was biotinylated in
vivo
by AviTag-BirA technology, which method is BriA catalyzes amide
linkage
between the biotin and the specific lysine of the AviTag.
其他:
在線留言
中文名稱:
Recombinant JC polyomavirus Major capsid protein VP1
貨號:
CSB-BP355946JAK
規格:
來源:
Baculovirus
其他:
在線留言
中文名稱:
Recombinant JC polyomavirus Major capsid protein VP1
The tag type will
be
determined during production process. If you have specified tag
type, please tell us and we will develop the specified tag
preferentially.
產品提供形式:
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.
復溶:
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.
儲存條件:
Store at -20°C/-80°C upon receipt, aliquoting is
necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質期:
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.
貨期:
Delivery time may
differ from different purchasing way or location, please kindly
consult your local distributors for specific delivery time.
Note: All of our
proteins are default shipped with normal blue ice packs, if you
request to ship with dry ice, please communicate with us in
advance
and extra fees will be charged.
注意事項:
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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.
基因功能參考文獻:
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