Supporting Your Research Beyond Traditional Models

Prion disease research now extends far beyond traditional models such as mice and hamsters. Research and surveillance programmes increasingly involve a wide range of mammalian species, from ruminants to camelids.

In this context, an antibody’s ability to recognise its target across different species becomes a key consideration.

The anti-PrP monoclonal antibodies SAF32 (A03202) and Sha31 (A03213) have documented use across 10 mammalian species from 5 taxonomic orders in the publications reviewed, providing a useful basis for comparative studies and surveillance programmes (1-11).

Two Antibodies, Two Epitopes

SAF32 targets the N-terminal region of the PrP protein, specifically the octapeptide repeat domain. Its use has been documented in several species, including humans (8, 9), mice (7), dromedary camels (1) and the red-tailed phascogale (Phascogale calura) (4).

Sha31, meanwhile, recognises the α1 helix within the C-terminal globular domain. Its epitope sequence (YEDRYYRE) has been described as conserved across multiple species (10), which contributes to its widespread use in PrP detection studies and TSE surveillance programmes. Its use has been documented in humans, mice, hamsters and sheep (11), cattle (3, 6), white-tailed deer and raccoons (2), bank voles (5) and dromedary camels (1).

For More Consistent Studies

The documented species coverage of these two clones helps minimise reagent changes when moving from one animal model to another and facilitates multi-species studies by allowing the use of the same detection antibody.

This approach helps reduce experimental variability and improves the comparability of results within a single research project.

Versatility Demonstrated in the Scientific Literature

Several publications report the use of SAF32 and Sha31 in a variety of experimental settings, including studies involving sheep, cattle, white-tailed deer, raccoons and dromedary camels:

• Vilette et al. (2016): Sha31 was used to detect PrPres from multiple species within the same study (11),
• Cassmann et al. (2022): Sha31 was employed in research investigating the transmission of Chronic Wasting Disease (CWD) in white-tailed deer (2),
• Amara et al. (2025): SAF32 and Sha31 were used together in the first identification of camel prion disease in Tunisia (1, preprint).

Discover the documented species coverage of SAF32 (A03202) and Sha31 (A03213) and identify the anti-PrP antibody best suited to your research applications.

References

1. Amara A, Di Bari MA, Elmehatli K, Bruno R, Andolsi R, Chiappini B, Vanni I, Esposito E, Riccardi G, Ben Abid OA, Marcon S, Malek A, Ben Smida B, Kessa H, Chandoul W, Handous M, Khorchani R, Nonno R, Zrelli M, Agrimi U, Vaccari G, Pirisinu L. First identification of camel prion disease in Tataouine, Tunisia: an emerging animal prion disease in North Africa. bioRxiv. 2025. DOI: 10.1101/2025.09.17.675824. [preprint]
2. Cassmann ED, Frese AJ, Moore SJ, Greenlee JJ. Transmission of Raccoon-Passaged Chronic Wasting Disease Agent to White-Tailed Deer. Viruses. 2022;14(7):1578.
3. Cassmann ED, Frese AJ, Becker KA, Greenlee JJ. Short incubation periods of atypical H-type BSE in cattle with EK211 and KK211 prion protein genotypes after intracranial inoculation. Frontiers in Veterinary Science. 2023;10:1301998.
4. De Dios K, Kumar S, Alvandi E, Adhikari UK, David MA, Tayebi M. Phylogeny and Molecular Characterisation of PRNP in Red-Tailed Phascogale (Phascogale calura). Brain Sciences. 2025;15(3):250.
5. Eraña H, Charco JM, Díaz-Domínguez CM, Pérez-Castro MÁ, Fernández-Borges N, Elezgarai SR, González-Miranda E, Vázquez-Fernández E, Requena JR, Castilla J. A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of bona fide prions. Nature Communications. 2024;15:46360-2.
6. Kim YC, Kwon DH, Gim GM, Wickersham L, Ye J, Moon B, Eom KH, Lee YR, Sohn HJ, Kang HE, Lee H, Kim J, Ku BK, Kim DY, Jung D, Park J, Heo S, Yum SY, Jang G. Long-term viability and stable germline transmission of prion-free cattle over multiple generations. Scientific Reports. 2026.
7. Kobayashi A, Matsuura Y, Takeuchi A, Yamada M, Miyoshi I, Mohri S, Kitamoto T. A domain responsible for spontaneous conversion of bank vole prion protein. Brain Pathology. 2018;29(2):155-163.
8. Lutsenko S, et al. Prion protein promotes copper toxicity in Wilson disease. Nature Communications. 2025;16.
9. Martellucci S, Manganelli V, Santacroce C, Santilli F, Piccoli L, Sorice M, Mattei V. Role of Prion protein-EGFR multimolecular complex during neuronal differentiation of human dental pulp-derived stem cells. Prion. 2018;12(2):117-126.
10. Sarradin P, Viglietta C, Limouzin C, Andréoletti O, Daniel-Carlier N, Barc C, et al. Transgenic Rabbits Expressing Ovine PrP Are Susceptible to Scrapie. PLoS Pathogens. 2015;11(8):e1005077.
11. Vilette D, Courte J, Peyrin JM, Coudert L, Chapuis J, Moudjou M, Beringue V. Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification. Scientific Reports. 2016;6:29116.

The species listed are those reported in the publications reviewed. They do not constitute a manufacturer validation of reactivity. Validation in your own model remains your responsibility. For research use only. Not for use in diagnostic procedures.