Magic™ Anti-Prion protein PrP polyclonal antibody (DPATB-H81917)

Rabbit Anti-Human Prion protein PrP (Phospho S43) polyclonal antibody for WB, IP, IHC-P


Host Species
Antibody Isotype
Species Reactivity
Prion protein PrP phosphorylated at Ser43.


Alternative Names
AltPrP; ASCR; CD230; CD230 antigen; CJD; GSS


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We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More

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Cellular prion protein neither binds to alpha-synuclein oligomers nor mediates their detrimental effects


Authors: La Vitola, Pietro; Beeg, Marten; Balducci, Claudia; Santamaria, Giulia; Restelli, Elena; Colombo, Laura; Caldinelli, Laura; Pollegioni, Loredano; Gobbi, Marco; Chiesa, Roberto; Forloni, Gianluigi

alpha-Synuclein oligomers are crucial players in the pathogenesis of Parkinson's disease. Some mechanisms involved in -synuclein oligomer detrimental effects include membrane damage, neuroinflammation and protein-protein interactions. Recently, the cellular prion protein (PrPC) emerged as an interactor of -synuclein oligomers, apparently mediating their detrimental activities. Through direct in vivo and in vitro approaches we herein investigated the existence of a direct cross-talk between -synuclein oligomers and PrPC. In vitro, we assessed -synuclein oligomer toxicity by comparing the effect in Prnp(+/+) versus PrPC knockout (Prnp(0/0)) hippocampal neurons. Through an in vivo acute mouse model, where -synuclein oligomers injected intracerebroventricularly induce memory impairment and neuroinflammation, we verified whether these detrimental effects were preserved in Prnp(0/0) mice. In addition, PrPC--synuclein oligomer direct binding was investigated through surface plasmon resonance. We found that PrPC was not mandatory to mediate -synuclein oligomer detrimental effects in vitro or in vivo. Indeed, -synuclein oligomer toxicity was comparable in Prnp(+/+) and Prnp(0/0) neurons and both Prnp(+/+) and Prnp(0/0) mice injected with -synuclein oligomers displayed memory deficit and hippocampal gliosis. Moreover, surface plasmon resonance analyses ruled out PrPC--synuclein oligomer binding. Our findings indicate that PrPC neither binds -synuclein oligomers nor mediates their detrimental actions. Therefore, it is likely that PrPC-dependent and PrPC-independent pathways co-exist in Parkinson's disease.

PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins


Authors: Corbett, Grant T.; Wang, Zemin; Hong, Wei; Colom-Cadena, Marti; Rose, Jamie; Liao, Meichen; Asfaw, Adhana; Hall, Tia C.; Ding, Lai; DeSousa, Alexandra; Frosch, Matthew P.; Collinge, John; Harris, David A.; Perkinton, Michael S.; Spires-Jones, Tara L.; Young-Pearse, Tracy L.; Billinton, Andrew; Walsh, Dominic M.

Neurodegenerative diseases are an enormous public health problem, affecting tens of millions of people worldwide. Nearly all of these diseases are characterized by oligomerization and fibrillization of neuronal proteins, and there is great interest in therapeutic targeting of these aggregates. Here, we show that soluble aggregates of alpha-synuclein and tau bind to plate-immobilized PrP in vitro and on mouse cortical neurons, and that this binding requires at least one of the same N-terminal sites at which soluble A beta aggregates bind. Moreover, soluble aggregates of tau, alpha-synuclein and A beta cause both functional (impairment of LTP) and structural (neuritic dystrophy) compromise and these deficits are absent when PrP is ablated, knocked-down, or when neurons are pre-treated with anti-PrP blocking antibodies. Using an all-human experimental paradigm involving: (1) isogenic iPSC-derived neurons expressing or lacking PRNP, and (2) aqueous extracts from brains of individuals who died with Alzheimer's disease, dementia with Lewy bodies, and Pick's disease, we demonstrate that A beta, alpha-synuclein and tau are toxic to neurons in a manner that requires PrP (c). These results indicate that PrP is likely to play an important role in a variety of late-life neurodegenerative diseases and that therapeutic targeting of PrP, rather than individual disease proteins, may have more benefit for conditions which involve the aggregation of more than one protein.

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