Anti-PrP, clone DRM2-118 Antibody

Evaluated by Western Blotting in mouse brain tissue lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected PrP in 10 µg of mouse brain tissue lysate.

Anti-PrP, clone DRM2-118 | MABN768 is an antibody against PrP for use in Western Blotting, Immunohistochemistry, ELISA.

Research Category
Neuroscience

Research Sub Category
Developmental Signaling

Western Blotting Analysis: 0.5 µg/mL from a representative lot detected PrP in 10 µg of rat brain tissue lysate.
ELISA Analysis: A representative lot detected PrP in recombinant PrP proteins from multiple species by ELISA using DRM1-31, DRM1-60, and DRM2-118 (Stanker, L.H., et al. (2012). 31(5):314-24).
Immunohistochemistry Analysis: A representative lot detected PrP in hamster brain sections tissue with DRM1-31, DRM1-60, and DRM2-118 (Stanker, L.H., et al. (2012). 31(5):314-24).
Western Blotting Analysis: A representative lot detected PrP in normal brain extract from multiple spcecies using DRM2-118. DRM1-60, and DRM1-31 lysate (Stanker, L.H., et al. (2012). 31(5):314-24).

DRM1-60 showed strong binding to only one peptide (#29: NQVYYRPVDQYS) suggesting a linear epitope corresponding to SHaPrP(159–170), located in b2-a2 loop. This epitope assignment is consistent with the binding of DRM1-60 to PrPC to all species tested, except human and horse, which both harbor substitutions in this region. While antibodies with epitopes similar to DRM2-118 have been described,(36) DRM1-60 and DRM1-31 have unique epitopes not previously reported. DRM1-60 appears to bind a linear epitope localized to the b2-a2 loop, while DRM1-31 has a conformational epitope located on the exposed surface formed by the close proximity of the b2-a2- helix loop, the N-terminus of the a2 helix, and the C-terminus of the a3 helix.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

The protein named PrP is the cellular gene for the prion protein. The normal form appears to play a role in neuronal development and synaptic plasticity, iron transport and myelin sheath maintenance. PrP has both membrane associated and cytoplasmic/nuclear isoforms. The primary isoform is localized to the cellular membrane in lipid anchor clusters, as well as in the Golgi. Isoform 2 is cytoplasmic that becomes localized to the nucleus. Prp is normally a monomeric protein but a disease associated mutated form will form protease resistant oligomers often with another protein beta amyloid. The mutated form is found in high quantity in the brain of humans and animals infected with the degenerative neurological diseases such as Kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), Scrapie, and Bovine Spongiform Encephalopathy (BSE) and Transmissible Mink Encephalopathy.

~36 kDa observed. Uncharacterized band(s) may appear in some lysates.

Recombinant protein corresponding to syrian hamster PrP.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG2bκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.