P5999

Monoclonal Anti-Prion Protein antibody produced in mouse

1 mg/mL, clone IPC1, purified immunoglobulin, buffered aqueous solution

• Synonym(s): Anti-AA960666, Anti-CD230, Anti-PRIP, Anti-PrP, Anti-PrP<C>, Anti-PrPSc, Anti-Prn-i, Anti-RP23-401J24.1, Anti-Sinc
• MDL number: MFCD01865558
• UNSPSC Code: 12352203
• NACRES: NA.41

Properties

• biological source: mouse
• conjugate: unconjugated
• antibody form: purified immunoglobulin
• antibody product type: primary antibodies
• clone: IPC1, monoclonal
• form: buffered aqueous solution
• mol wt: antigen 25-35 kDa
• species reactivity: hamster, mouse, rat
• concentration: 1 mg/mL
• technique(s): microarray: suitable; western blot: 0.05-0.1 μg/mL using mouse brain extract
• UniProt accession no.: P04156
• shipped in: dry ice
• storage temp.: −20°C
• target post-translational modification: unmodified
• Gene Information: mouse ... Prnp(19122) ; rat ... Prnp(24686)

Description

General description

Monoclonal Anti-Prion Protein (mouse IgG1 isotype) is derived from the hybridoma IPC1 produced by the fusion of mouse myeloma cells (NSO cells) and splenocytes from PrP knock-out mice immunized with recombinant mouse PrPc.

Prion is a cell surface glycoprotein present in two isoform- PrPC (a cellular isoform) and PrPSc (a disease associated isoform). Prion Protein encodes a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. PrPC is found in the neurons of the brain and spinal cord. The prion protein is associated with several diseases like bovine spongiform encephalopathy, Creutzfeldt-Jakob disease and fatal familial insomnia.

Immunogen

recombinant mouse PrP^C.

Application

Monoclonal Anti-Prion Protein antibody produced in mouse is useful in enzyme linked immunosorbent assay (ELISA), immunoblotting and immunoprecipitation.

Biochem/physiol Actions

Prion protein (PrP) is a natural protein synthesized within the secretory pathway and transported to the surface of the cell where it is tethered to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor. The activity of PrP is not well understood; it 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 anti-oxidant activity. 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.

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.

Safety Information

• Storage Class: 10 - Combustible liquids
• wgk_germany: WGK 3
• flash_point_f: Not applicable
• flash_point_c: Not applicable
• ppe: Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)