Key features and details | |
Cat. No. | MABL-2743 |
Name | Anti-Prion protein mAbs |
Clone No. | AFD- Nb484 |
From | Recombinant Antibody |
Isotype | Engineer antibody |
Application | crystallization, functional assays, SPR, WB, ELISA |
Species Reactivity | Human, Mouse |
Basic Information | |
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 Name | 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. |
COA Information （For reference only, actual COA shall prevail） | |
Size | 100 μg Purified antibody. |
Concentration | 1 mg/ml. |
Purification | Protein A affinity purified |
Buffer | PBS with 0.02% Proclin 300. |
Concentration | 1 mg/ml. |
Storage Recommendation | Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at - 20⁰C. |
