Cat. No.
MABL-2743
Application
crystallization, functional assays, SPR, WB, ELISA
Isotype
Engineer antibody
Species Reactivity
Human, Mouse
Clone No.
Nb484
From
Recombinant Antibody
Specificity
This antibody is specific for major prion proteins, with a demonstrated specificity for a discontinuous epitope on the human prion protein (HuPrP). It binds to specific structural elements and loops within HuPrP, particularly the β0-β1 loop (residues 123−125), the β2-α2 loop (residues 164−170), and the α2-helix (residues 174−185). It has also been shown to bind mouse prion protein (MoPrP), where it binds residues 123 and 125 of the β0-β1 loop; residue 128 of the β1 strand; residues 164, 167, 168, and 169 of the β2-α2 loop; and residues 173, 174, 177, 178, 182, 185 and 189 of the α2-helix.
Alternative Names
CD230; PrP; PrP27-30; PrP33-35C; HuPrP; MoPrP; ASCR; Major prion protein
UniProt
P04156; P04925
Immunogen
The original antibody was generated by immunizing a llama with a segment of the mouse prion protein (MoPrP(23-230)).
Application Notes
The original version of this antibody (alpaca VHH) bound mouse and human prion proteins (MoPrP and HuPrP, respectively) as demonstrated by SPR binding assays with a Kd of 40 nM, 50 nM, 9.54 nM, and 7 µM for MoPrP(23-230), MoPrP(89-230), HuPrP(90-231), and HuPrP(23-144), respectively. The addition of this antibody to MoPrP(23−230) extended the lag phase of fibrillization by about 40 hours in an amyloid seeding assay (ASA), indicating that the interaction of this antibody with the full-length MoPrP inhibited the formation of prion protein infectious scrapie agent (PrPSc)-like aggregates. This antibody's ability to inhibit prion propagation was further confirmed by treating scrapie-infected murine cells (ScGT1) with different antibody concentrations. The treatment resulted in a dramatic, dose-dependent reduction in PrPSc levels, as measured by PK assay and Western blotting.
Antibody First Published
Abskharon et al., Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody. J Am Chem Soc. 2014 Jan 22;136(3):937-44. PMID:
Note on publication
The original publication explores the crystallization of full-length human prion protein in complex with nanobody Nb484, revealing the structural conversion of its N-terminal β-sheet motif and implications for prion disease pathogenesis.
Size
100 μg Purified antibody.
Concentration
1 mg/ml.
Purification
Protein A affinity purified
Buffer
PBS with 0.02% Proclin 300.
Storage Recommendation
Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at - 20⁰C.
