Recombinant Human parvovirus B19 Minor capsid protein VP1,partial

Mfr.No.	CSB-EP362102HPM
Description	Capsid protein self-assbles 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, such as the glycosphingolipid globoside or the integrin heterodimer ITGAV/ITGB1. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangents leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal mbrane during entry into host cell. IntraCytoplasmic domain transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids .
Tag	N-terminal 6xHis-tagged
Regulatory	RUO
Relevance	Capsid protein self-assbles 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, such as the glycosphingolipid globoside or the integrin heterodimer ITGAV/ITGB1. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangents leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal mbrane during entry into host cell. IntraCytoplasmic domain transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids .
Source	E.coli
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Expression Region	228-781aa
Mol Weight	64.8 kDa
Nature	Recombinant
Protein Description	Partial

Subcellular Location	Virion, Host nucleus
Uniprot	P07299, P07299
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, such as the glycosphingolipid globoside or the integrin heterodimer ITGAV/ITGB1. 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 nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell. Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids (By similarity).
Protein Families	Parvoviridae capsid protein family
Weight	64.8 kDa

Stotage Note	Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Buffer	Tris-based buffer，50% glycerol
Purity	Greater than 90% as determined by SDS-PAGE.
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 -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Storage Buffer	Tris-based buffer,50% glycerol