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SARS Coronavirus Nucleoprotein Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 3
- PROTOCOLS
- BACKGROUND
Application 
| E |
|---|---|
| Primary Accession | P59595 |
| Reactivity | SARS |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 46025 Da |
| Antigen Region | 393-422 aa |
| Other Names | Nucleoprotein, Nucleocapsid protein, NC, Protein N, N |
|---|---|
| Target/Specificity | This SARS virus PUP5 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 393~422 amino acids from the C-terminus region of SARS nucleocapsid protein. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | SARS Coronavirus Nucleoprotein Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | N {ECO:0000255|HAMAP-Rule:MF_04096} |
|---|---|
| Function | Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455). |
| Cellular Location | Virion {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170, ECO:0000269|PubMed:19106108}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host cytoplasm, host perinuclear region. Host nucleus. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04096} |
Provided below are standard protocols that you may find useful for product applications.
Background
An outbreak of atypical pneumonia, referred to as severe acute respiratory syndrome (SARS) and first identified in Guangdong Province, China, has spread to several countries. The severity of this disease is such that the mortality rate appears to be ~3 to 6%. A number of laboratories worldwidehave undertaken the identification of the causative agent. The National Microbiology Laboratory in Canada obtained the Tor2 isolate from a patient in Toronto, and succeeded in growing a coronavirus-like agent in African Green Monkey Kidney (Vero E6) cells. This coronavirus has been named publicly by the World Health Organization and member laboratories as ?SARS virus? The SARS membrane proteins, including the major proteins S (Spike) and M (Membrane), are inserted into the endoplasmic reticulum Golgi intermediate compartment (ERGIC) while full length replicated RNA (+ strands) assemble with the N (nucleocapsid) protein. The virus then migrates through the Golgi complex and eventually exits the cell, likely by exocytosis. The site of viral attachment to the host cell resides within the S protein. Oligomeric spike (S) glycoproteins extend from SARS membranes. These integral membrane proteins assemble within the endoplasmic reticulum of infected cells and are subsequently endoproteolyzed in the Golgi, generating noncovalently associated S1 and S2 fragments. Once on the surface of infected cells and virions, peripheral S1 fragments bind carcinoembryonic antigen-related cell adhesion molecule (CEACAM) receptors, and this triggers membrane fusion reactions mediated by integral membrane S2 fragments.
References
He, R., et al., Biochem. Biophys. Res. Commun. 316(2):476-483 (2004).
Snijder, E.J., et al., J. Mol. Biol. 331(5):991-1004 (2003).
Marra, M.A., et al., Science 300(5624):1399-1404 (2003).
Krokhin, O., et al., Mol Cell Proteomics 2(5):346-356 (2003).
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