Catalog # PM3971


Prion Protein (a.a. 109-112)

Mouse Monoclonal

Application Dilution
ELISA1:2000
IHC1:100
WB1:1000

Size 100 μl

Species Reactivity Hu

MW 27 kDa

Isotype IgG2a

$245

Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species. These diseases involve conversion of normal cellular prion protein (PrPc) into a form that is insoluble and resistant to proteases (PrPSc). The protease resistant form can polymerize into fibrils which accumulate in infected tissues and cause cell death and tissue damage. PrPs have an N-terminal signal sequence and a C-terminal linkage to glycosylphosphatidylinositol anchor. The mature protein is a glycosylated protein that associates with cell membranes. Phosphorylation of PrPC at Ser-43 by Cdk5 promotes proteinase K resistance, prion aggregation, and fibril formation in vitro. In addition, Ser-43 phosphorylation is upregulated in scrapie-infected mouse brain relative to controls. Thus, phosphorylation of Ser-43 may be an important mechanism leading conversion of PrPc to PrPSc and the onset of disease.

 

References
Gianoupolous, P.N. et al. (2009) J. Neurosci. 29:8743.
Monari, L. et al. (1994) Proc. Natl. Acad. Sci. 91:2839.
Kascsak, R.J. et al. (1987) J. Virology. 61:3688.
Prusiner, S.B. (1982) Science. 216:136.
Clone 3F4 antibody binds to amino acids 109 to 112 in human prion protein. This sequence is conserved in feline and hamster, but is less conserved in rat and mouse Prion protein.

*For more information, see UniProt Accession P04156
Mouse monoclonal antibody purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.

The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.

The antibody detects endogenous prion protein in human PC3 and A431 cell lines. In addition, the antibody strongly detects human recombinant Prion protein, and weakly detects bovine recombinant Prion protein.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.

Western blot of GST recombinant human full-length prion protein that was untreated (lanes 1 and 3) or phosphorylated with Cdk5/p25 (lanes 2 & 4). Endogenous prion phosphorylation was examined in human PC3 cells untreated (lanes 5 & 7) or treated with Calyculin A (100 nM) for 30 min (lanes 6 & 8). The blots were probed with anti-Prion protein (3F4) (lanes 1, 2, 5, & 6) or anti-Prion protein (Ser-43) (lanes 3, 4, 7, & 8).



This kit contains:

KIT SUMMARY