United Kingdom (UK)
Recombinant monoclonal antibody to Prion protein. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma mab 132.
UniProt Accession Number of Target Protein: P04156
Alternative Name(s) of Target: PrPC; ASCR; PrP27-30; PrP33-35C; CD230
Immunogen: The original antibody was generated by immunizing PrP gene-ablated mice with PrP.
Specificity: The antibody recognizes residues 119–127 of mouse PrP and specifically detects PrPSc under partially denatured conditions.
Application Notes: The antibody was employed for detection of PrP in N2a-3 cells, ScN2a-3-22L cells, N2a-3 cells infected with the Chandler strain (ScN2a-3-Ch) and in GT1-7 cells persistently infected with the 22L strain (ScGT1-7-22L) in immunofluorescence analysis. Fluorescent signals in uninfected cells remained at a background level, while granular signal were detected in infected cells (Yamasaki et al., 2012; PMID: 22090211). The specificity of the original format of the antibody was confirmed by ELISA analysis (Kim et al., 2004; PMID: 15003861). The antibody could distinguish between prion-infected cells (ScN2a-3-22L) from uninfected cells (N2a-3) in a cell-based ELISA. The cell-based ELISA was successful also with ScN2a-3-Ch and ScGT1-7-22L. (Shan et al., 2016; PMID: 27565564). The antibody reacted with denatured PrPC and PrPSc in western blot analysis. The antibody reacted with mouse ovine and bovine PrP Sc in western blot analysis (Kim et al., 2004; PMID: 15003861). The antibody genetically conjugated with enhanced green fluorescent protein (EGFP) at the C-terminus of the heavy chain was used for the direct immunostaining of PrPSc in ScN2a-3-22L by IFA (Yamasaki et al., 2014; PMID: 25181483). The antibody was used to detect PrPSc in neurons and glial cells from the brains of prion-infected mice by flow cytometry (Yamasaki et al., 2017; PMID: 29046463). Surface plasmon resonance and ELISA analysis revealed that the binding of monovalent recombinant Fab antibody was significantly weaker than bivalent recombinant IgG antibody, indicating that the bivalent binding is required for the efficient binding to the epitope. The binding kinetics of mono and bivalent antibody to MoPrP was measured using SPR, with KD of 5.5 nM for the Fab fragment and 57 pM for IgG1 (Suzuki et al., 2019; PMID: 31170247).
Antibody first published in:
Kim et al. Antigenic characterization of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies Virology. 2004 Mar 1;320(1):40-51. PMID:15003861
Note on publication:
The paper describes the generation of a panel of antibodies against prion protein.