Anti-Prion Protein antibody, Mouse monoclonal

Anti-Prion Protein antibody, Mouse monoclonal (mouse IgG2b isotype) is derived from the hybridoma 8H4 produced by the fusion of mouse myeloma cells (SP2/0 cells) and splenocytes from Prnp-/- mice immunized with recombinant murine PrPc. Prion protein (PrP) is mapped to human chromosome 20p13. PrP is constitutively expressed in brain and other tissues of healthy humans and animals and is present in high levels at the synapse.

Prion is a cell surface glycoprotein present in two isoform- PrPc (a cellular isoform) and PrPsc (a disease associated isoform). Monoclonal anti-prion protein antibody is useful for the treatment of prion disease, by inhibiting the abnormal isoform PrPsc . This antibody can also be used for passive immunization of animals to protect them from prion infection. Anti prion protein antibody may be used to inhibit abnormal prion protein accumulation in cultured scrapie-infected neuroblastoma cells. The antibody reacts specifically with amino acids 145-180 of human prion. It also has specificity for monkey, cow, sheep, deer, squirrel, hamster, mouse and rat.

The antibody epitope resides within amino acids 145-180 of human prion.

Recombinant MoPrp residues 121-231

recombinant mouse PrP^C.

Anti-Prion Protein antibody, mouse monoclonal may be used in:

• immunoblotting
• flow cytometry
• immunocytochemistry
• immunoprecipitation
• immunoelectron microscopy
• immunohistochemistry
• enzyme linked immunosorbent assay

Prion-related diseases are fatal neurodegenerative disorders also known as transmissible spongiform encephalopathies (TSEs). Prion plaques are of three types: unicentric (single, compact core), multicentric (two or more cores and definite border), and diffuse plaques without a definite central core. Disease-associated prion protein specifically inhibits the proteolytic β-subunits of the 26S proteasome. This may clarify the mechanism of cell death by the prion protein. Prion protein may be involved in copper utilization, serving to buffer copper at the synaptic cleft or to mediate re-uptake of copper into the presynapse. Alternatively, bound copper may influence PrP binding characteristics. The PrP-copper complex may be crucial for synaptic homeostasis as a result of its antioxidant activity.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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