Anti-Prion Protein antibody, Mouse monoclonal

MDL number:	MFCD01865558
NACRES:	NA.41

Кат. номер

P0110-200UL

P0110-25UL

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.
Specificity
The antibody epitope resides within amino acids 145-180 of human prion.
recombinant mouse PrPC.
Recombinant MoPrp residues 121-231
Anti-Prion Protein antibody, mouse monoclonal may be used in:

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

Biochem/physiol Actions
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
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.

Quality Level	200
biological source	mouse
antibody form	purified immunoglobulin
antibody product type	primary antibodies
clone	8H4, monoclonal
form	buffered aqueous solution
mol wt	antigen 25-35 kDa
species reactivity	monkey, bovine, rat, human, sheep, mouse
packaging	antibody small pack of 25 µL
concentration	~1.5 mg/mL
application(s)	electron microscopy: suitable","flow cytometry: suitable","immunocytochemistry: suitable","immunohistochemistry: suitable","immunoprecipitation (IP): suitable","indirect ELISA: suitable","western blot: 2-4 µg/mL using mouse brain extract
isotype	IgG2b
conjugate	unconjugated
UniProt accession no.	P04156,
shipped in	dry ice
storage temp.	20°C
Gene Information	bovine ... PRNP(281427) human ... PRNP(5621) mouse ... Prnp(19122) rat ... Prnp(24686) sheep ... PRNP(493887)

RIDADR	NONH for all modes of transport
WGK Germany	nwg
Flash Point F	Not applicable
Flash Point C	Not applicable