ArtNr |
CSB-EP323858PQB-1 |
Hersteller |
Cusabio
|
Menge |
1mg |
Quantity options |
1mg
10ug
100ug
20ug
200ug
50ug
500ug
|
Kategorie |
|
Typ |
Proteins Recombinant |
Format |
Liquid or Lyophilized powder |
Specific against |
other |
Purity |
Greater than 90% as determined by SDS-PAGE. |
ECLASS 10.1 |
32160409 |
ECLASS 11.0 |
32160409 |
UNSPSC |
12352202 |
Lieferbar |
|
Research Areas |
Others |
Uniprot ID |
P18546 |
Gene Names |
N/A |
Organism |
Porcine parvovirus (strain NADL-2) (PPV) |
AA Sequence |
MAPPAKRARGLTLPGYKYLGPGNSLDQGEPTNPSD AAAKEHDEAYDKYIKSGKNPYFYFSAADEKFIKET EHAKDYGGKIGHYFFRAKRAFAPKLSETDSPTTSQ QPEVRRSPRKHPGSKPPGKRPAPRHIFINLAKKKA KGTSNTNSNSMSENVEQHNPINAGTELSATGNESG GGGGGGGGRGAGGVGVSTGTFNNQTEFQYLGE |
Expression Region |
1-207aa |
Sequence Info |
Partial |
Source |
E.coli |
Tag Info |
N-terminal 6xHis-tagged |
MW |
26.1 kDa |
Alternative Name(s) |
Coat protein VP1 |
Relevance |
Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus |
Reference |
Porcine parvovirus: DNA sequence and genome organization. Ranz A.I., Manclus J.J., Diaz-Aroca E., Casal J.I. J. Gen. Virol. 70:2541-2553(1989) |
Purity |
Greater than 90% as determined by SDS-PAGE. |
Form |
Liquid or Lyophilized powder |
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 -20C/-80C. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
Storage |
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 -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C. |
Notes |
Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week. |
Function |
Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (By similarity). |
Subcellular Location |
Virion, Host nucleus |
Protein Families |
Parvoviridae capsid protein family |
Tag Information |
N-terminal 6xHis-tagged |
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