Prion Disease Research Tools

Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders that include Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker syndrome, kuru and fatal familial insomnia. Prion diseases are thought to be caused by the misfolding of native cellular prion protein (PrP^C) into the aggregation prone form (PrP^Sc). PrP^Sc refers to the misfolded infectious form that differs from PrP^C because it has a higher content of β-sheet structure and it aggregates to form medium and large size polymers. The conversion of PrP^C into PrP^Sc is the main event in prion disease.

The Central Role of PrP^Sc

There is no doubt that the formation and accumulation of PrP^Sc in the brain is the triggering factor of prion disease. PrP^Sc accumulates in different brain regions as distinct types of deposits depending on the animal species and strains of the agent. The loss of the critical biological function of PrP^C is one possible mechanism by which PrP^Sc formation might result in neurodegeneration. Studies have proposed various functions of PrP^C, such as the roles in apoptosis, oxidative stress, neuroprotection, transmembrane signaling, myelination, cell adhesion, and trafficking of metal ions. Another possible mechanism by which PrP^Sc formation might be linked to the disease is by direct toxicity of the misfolded protein.

Therapeutic Development

Currently, no therapeutic or prophylactic regimens exist for prion diseases. A variety of therapeutic strategies have been proposed but most of them directed at preventing prion conversion. The targets include inhibition of PrP^C expression, enhancement of PrP^C degradation, inhibition of PrP^C-PrP^Sc interaction, inhibition of PrP^Sc oligomer formation, and enhancement of PrP^Sc degradation. PrP^C and PrP^Sc have been widely studied to understand the enigmatic nature of prions. Additionally, some cellular factors have been implicated as possible targets in PrP^C-mediated or PrP^Sc-induced neurodegenerative processes. One example is the growth arrest and DNA-damage-inducible protein GADD34. GADD34 promotes dephosphorylation of the α-subunit of eukaryotic translation initiation factor 2 and reverses translational suppression caused by the prion infection-induced unfolded protein response in the endoplasmic reticulum.

Targets and Canditaes Related to Prion Disease

Creative Biolabs aims to provide biological products to help promote your prion diseases project research. These reagents include but are not limited to site-specific modified peptides, conjugated peptides, monoclonal antibodies (mAbs), polyclonal antibodies (pAbs), labeled antibodies, proteins, analytical kits, and small molecule activators and inhibitors.

Loading...

iNeuMab™ Rabbit Anti-PMP22 Monoclonal Antibody (CBP1645) [CAT#: NAB-08-PZ1031]

Rabbit Monoclonal Antibody to PMP22

Host Species:

Rabbit

Species Reactivity:

Rat; Human

Applications:

WB

Conjugation:

Unconjugated; APC; PE; HRP; Biotin; FITC

Compare Inquiry

Datasheet MSDS