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Prion Protein Monoclonal Antibody - Sha31

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    Prion Protein Monoclonal Antibody - Sha31
  • Prion Protein Monoclonal Antibody - Sha31
Cat No: A03213
Antibodies - Monoclonal Antibodies
Bertin Bioreagent

Prion Protein (PrP) and namely its abnormal isoform, partially resistant to proteinase K (PrPres), is the only specific molecular marker of the Transmissible Spongiform Encephalopathies (TSEs) such as Bovine Spongiform Encephalopathie (BSE) or its huma...

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: 200 µg

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Territorial Availability: Available worldwide directly through Bertin or your local distributor
Synonyms:
  • Prion Protein Monoclonal Antibody - Sha31
Correlated keywords:
  • proteins
  • mad
  • cow
  • diseases
  • bovine
  • spongiform
  • encephalopathy
  • scrapie
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Product Overview:
Prion Protein (PrP) and namely its abnormal isoform, partially resistant to proteinase K (PrPres), is the only specific molecular marker of the Transmissible Spongiform Encephalopathies (TSEs) such as Bovine Spongiform Encephalopathie (BSE) or its human form, the New Variant of Creutzfeld-Jakob disease.
This antibody recognises the human protein sequence within amino acids 145-152 (human numbering).
Size 200 µg
Shipping Dry Ice
Host Mouse
Antigen This anti-prion protein (PrP) monoclonal antibody was raised against proteinase K treated and non-denatured scrapie-associated fibrils from Syrian hamster infected brain (263K).
Clone Sha 31
Isotype IgG1k
Application(s)

Reconstitute the content of the vial in 1 mL of water.

For EIA, the optimal working dilution must be determined empirically (currently be-tween 0.1 and 1 µg/mL). For western blot analysis of PrPc, dilute the antibody to a final concentration of 1 µg/mL.

Specificity
Application Media Reconstitute the content of the vial in 1 mL of water.
Formulation lyophilized IgG with BSA
Custom Code 3822000000
UNSPSC code 12352203

Vulin J, Biacabe AG, Cazeau G, Calavas D, and Baron T Molecular typing of protease-resistant prion protein in transmissible spongiform encephalopathies of small ruminants, France, 2002-2009. Emerg Infect Dis, Jan 2011; 17(1): 55-63.

Morel N., Simon S., Frobert Y., Volland H., Mourton-Gilles C., Negro A., Sorgato M.C., Creminon C., and Grassi J. Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils.

J Biol Chem, 279 :30143-9 (2004)

Notari S., Capellari S., Langeveld J., Giese A., Strammiello R., Gambetti P., Kretzschmar H.A., and Parchi P. A refined method for molecular typing reveals that co-occurrence of PrP(Sc) types in Creutzfeldt-Jakob disease is not the rule.

Lab Invest 87, 1103-12 (2007).

Feraudet C, Morel N, Simon S, Volland H., Frobert Y., Creminon C., Vilette D., Lehmann S., and Grassi J. Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells.

J Biol Chem 2005, 280:11247–11258

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