Hepatitis B Virus (HBV) (ayw/France/Tiollais/1979) Capsid Protein 2402

$315.00 – $1,050.00

Summary

Expression: E.coli
Pure: Yes (HPLC)
Amino Acid Range: Met1-Val149

SKU: 2402parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P03146
express system	E.coli
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Hepatitis B virus (HBV) core protein, the building block of the HBV capsid, plays multiple roles in viral replication, and is an attractive target for development of antiviral agents with a new mechanism of action.
molecular weight	The protein has a predicted MW of 17.81 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Hepatitis B Virus (HBV) (ayw/France/Tiollais/1979) Capsid Protein 2402

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Hepatitis B virus (HBV) core protein, the building block of the HBV capsid, plays multiple roles in viral replication, and is an attractive target for development of antiviral agents with a new mechanism of action.
Protein names Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
Gene names C,C
Protein family Orthohepadnavirus core antigen family
Mass 490133Da
Function Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions.
Subellular location Virion. Host cytoplasm .
Structure Homodimerizes, then multimerizes. Interacts with cytosol exposed regions of viral L glycoprotein present in the reticulum-to-Golgi compartment. Interacts with human FLNB. Phosphorylated form interacts with host importin alpha; this interaction depends on the exposure of the NLS, which itself depends upon genome maturation and/or phosphorylation of the capsid protein. Interacts with host NUP153.
Post-translational modification Phosphorylated by host SRPK1, SRPK2, and maybe protein kinase C or GAPDH. Phosphorylation is critical for pregenomic RNA packaging. Protein kinase C phosphorylation is stimulated by HBx protein and may play a role in transport of the viral genome to the nucleus at the late step during the viral replication cycle.
Target Relevance information above includes information from UniProt accession: P03146
The UniProt Consortium

HPLC of Hepatitis B Virus (HBV) (ayw/France/Tiollais/1979) Capsid-Prote

The purity of HBV (ayw/France/Tiollais/1979) Capsid is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Hepatitis B Virus (HBV) (ayw/France/Tiollais/1979) Caps

HBV (ayw/France/Tiollais/1979) Capsid on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.