Anti-Prion Protein PrP Antibody [2G11] (A279227)

Anti-Prion Protein PrP Antibody [2G11]

Mouse monoclonal [2G11] antibody to Prion Protein PrP.

This antibody recognises CD230 and can be used to detect the plaques which are formed during the progression of prion disease. Transmissible spongiform encephalopathies (TSEs) or prion diseases are fatal infectious neurodegenerative diseases of humans and animals. These diseases are biologically unique, as they are believed by some to be transmitted by an infectious agent comprised only of protein, with no nucleic acid component. Clinically, these diseases present with motor disturbances and behavioural changes. The major pathological changes seen are neuronal loss, vacuolation (spongiform change), proliferation and branching of glial cells, astrocytic proliferation and accumulation of the prion protein PrPSc, which can form amyloid plaques. CD230. also known as the prion protein (PrP) exists in two alternate forms; a normal cellular form (PrPc) and a disease-associated form (PrPSc).The normal and pathological forms of the prion protein have identical amino acid sequences and differ only in their folded tertiary structure and biochemical properties.MCA2460 was raised against a synthetic peptide (146-R154R171-182 ) of the ovine PrP peptide and specifically recognises the R151-R159 sequence.

IHC-P, ELISA

ELISA: 1:50 - 1:1,000, Tested on peptide.

Sheep

Synthetic peptide 146-R¹⁵⁴R¹⁷¹-182 of Bovine PrP.

Mouse

Monoclonal

2G11

IgG2a

Unconjugated

1 mg/ml

Liquid

Supplied in Phosphate Buffered Saline with 0.09% Sodium Azide.

Shipped at ambient temperature. Upon delivery aliquot and store at -20°C. When thawed, aliquot the sample as needed. Short term (up to 4 weeks): store at 4°C. Long term: store at -20°C. Avoid freeze / thaw cycles. Storage in frost free freezers is not recommended.

Mouse anti Sheep CD230 (aa151 - aa159) antibody, clone 2G11 recognizes CD230 and can be used to detect the plaques which are formed during the progression of prion disease. Transmissible spongiform encephalopathies (TSEs) or prion diseases are fatal infectious neurodegenerative diseases of humans and animals. These diseases are biologically unique, as they are believed by some to be transmitted by an infectious agent comprised only of protein, with no nucleic acid component. Clinically, these diseases present with motor disturbances and behavioural changes. The major pathological changes seen are neuronal loss, vacuolation (spongiform change), proliferation and branching of glial cells, astrocytic proliferation and accumulation of the prion protein PrPSc, which can form amyloid plaques. CD230. also known as the prion protein (PrP) exists in two alternate forms; a normal cellular form (PrPc) and a disease-associated form (PrPSc).The normal and pathological forms of the prion protein have identical amino acid sequences and differ only in their folded tertiary structure and biochemical properties.MCA2460 was raised against a synthetic peptide (146-R154R171-182 ) of the ovine PrP peptide and specifically recognises the R151-R159 sequence.

Alternative prion protein; major prion protein, AltPrP, ASCR, CD230, CD230 antigen, CJD, GSS, KURU, Major prion protein, p27 30, Prion protein, Prion related protein, PRIO_HUMAN, PRIP, PRNP, PrP, PrP27 30, PrP27-30, PrP33-35C, PrPC, PrPSc, Sinc