SARS-CoV-2 Nucleocapsid anticorps (SARS-CoV-2 N) (AA 1-419) (Biotin) Primary Antibody
SARS-CoV-2 N Reactivité: SARS Coronavirus-2 (SARS-CoV-2) ELISA Hôte: Human Monoclonal 1A6
N° du produit ABIN6953159
Plus shipping costs $45.00
local_shipping Destination: Etats-Unis
Envoi sous 11 à 14 jours ouvrables
- Type d'anticorp
- Recombinant Antibody
- AA 1-419
- SARS Coronavirus-2 (SARS-CoV-2)
- Cet anticorp SARS-CoV-2 Nucleocapsid est conjugé à/à la Biotin
- Attributs du produit
- Recombinant anti-SARS-CoV-2 Nucleoprotein Mouse ScFv is expressed from 293 cells (HEK293) with a human IgG1 Fc tag on C-terminal.
Mouse scFv fusion with human IgG1 Fc
- Recombinant Human Novel Coronavirus Nucleoprotein (N) (1-419aa)
- scFv fragment
- Indications d'application
- Optimal working dilution should be determined by the investigator.
- For Research Use only
- 50 % Glycerol, 0.01M PBS, pH 7.4, 0.03 % Proclin 300
- Agent conservateur
- Précaution d'utilisation
- This product contains ProClin: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- -20 °C,-80 °C
- Stockage commentaire
- Upon receipt, store at -20°C or -80°C. Avoid repeated freeze
- Autre désignation
- SARS-CoV-2 Nucleocapsid Protein
- Nucleoprotein 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. It plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Coronavirus nucleoproteins are phosphoproteins, and are encoded near the 3' end of the genome. N possesses two RNA-binding domains: an N-terminal domain with adjacent S/R-rich motif and the C-terminal 209 amino acids. N protein is invovled in coronavirus infection with many ways: the C-terminal domain (CTD) of N is important for binding the genomic RNA packaging signal leading to selective genome incorporation, the N3 domain interacts with the endodomain of M to form virions, and the serine-arginine repeat region of N (SR) interacts with the first ubiquitin-like domain of nsp3 in a critical early replication step. Moreover, it has also been demonstrated that N can oligomerize through interactions in the CTD, bind viral RNA through the N-terminal domain, unwind double-stranded nucleic acid in the manner of an RNA chaperone, and pack in a helix through the N-terminal domain, though none of these other functions has yet been demonstrated to be important for infection.
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