Recombinant Rubella Virus Nucleoprotein
Specification
Related Products
| Cat#: |
RUB-565 |
| Product Name: |
Recombinant Rubella Virus Nucleoprotein |
| Description: |
Rubella Virus Nucleoprotein is produced by recombinant expression of Rubella structural polyprotein (amino acids 1-300, NCBI accession number NP_062884.1) in HEK293 cells. It contains a C-terminal 10 amino acid glycine-serine linker followed by a 6x histidine tag. |
| Gene: |
NP |
| Species: |
Rubella virus (Strain F-Therien) |
| Source: |
HEK293 |
| Synonyms: |
Rubella Virus Nucleoprotein (Strain F-Therien) |
| Formulation: |
20mM TRIS-HCl pH8.0,50mM NaCl,0.5% SDS.Note that withdrawal of SDS will lead to concentration dependent aggregation of Rubella virus nucleoprotein. |
| Concentration: |
0.17 mg/mL |
| Purity: |
Greater than 95% purity |
| Storage: |
Short Term Storage: +2 centigrade to +8 centigrade
Long Term Storage: -80 centigrade |
| Notes: |
This product is intended for research and manufacturing uses only. It is not a diagnostic device. The user assumes all responsibility for care, custody and control of the material, including its disposal, in accordance with all regulations. |
| Freezing: |
Can be frozen, but avoid multiple freeze/thaw cycles. |
| Sequence Strain: |
F-Therien |
| Background: |
Rubella virus is an enveloped, positive single-stranded RNA virus and a member of the genus Rubivirus, which belongs to the Togaviridae family. The structural proteins of Rubella virus are synthesized as a polyprotein precursor in association with the endoplasmic reticulum in the host cell. It consists of three structural proteins: a capsid protein and two membrane-spanning glycoproteins, E1 and E2, localized in the virus envelope (Oker-Blom, et al., 1983). The polyprotein is cotranslationally cleaved by the host-cell signal peptidase and the C terminus of the capsid protein remains attached to the E2 signal peptide, which anchors this viral protein to intracellular membranes (Suomalainen, et al., 1990).
The capsid protein, excluding the E2 signal peptide, is a 277-amino-acid residue protein that forms disulfide-linked dimers (Baron & Forsell, 1991). It interacts with the RNA genome and forms the nucleocapsid, which is surrounded by a lipid membrane upon which E1 and E2 are arranged (Hobman & Chantler, 2007). The capsid protein is an essential component of the virus and a key factor for successful replication of the virus in host cells (Mangala Prasad, et al., 2013). It not only packages the RNA genome but also is involved in viral transcription and replication, regulating viral RNA replication by interacting with the virus-encoded nonstructural proteins (Chen & Icenogle, 2004).
Crystal structures of the C-terminal part of the protein (amino acids 127–277) suggest that variability in the relative positions of the secondary structure elements may contribute to flexibility in the capsid protein structure; this flexibility may be required for other non-structural cellular functions to facilitate virus replication and assembly inside host cells (Ilkow, et al., 2010; Mangala Prasad, et al., 2013). |
For research or industrial raw materials, not for personal medical use!
