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P5999

Sigma-Aldrich

Monoclonal Anti-Prion Protein antibody produced in mouse

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

Sinônimo(s):

Anti-AA960666, Anti-CD230, Anti-PRIP, Anti-PrP, Anti-PrP<C>, Anti-PrPSc, Anti-Prn-i, Anti-RP23-401J24.1, Anti-Sinc

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

mouse

conjugado

unconjugated

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

IPC1, monoclonal

forma

buffered aqueous solution

peso molecular

antigen 25-35 kDa

reatividade de espécies

hamster, mouse, rat

concentração

1 mg/mL

técnica(s)

microarray: suitable
western blot: 0.05-0.1 μg/mL using mouse brain extract

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

mouse ... Prnp(19122)
rat ... Prnp(24686)

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Descrição geral

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.

Imunogênio

recombinant mouse PrPC.

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

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

Exoneração de responsabilidade

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.

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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Visite a Biblioteca de Documentos

Microglia and the pathogenesis of spongiform encephalopathies.
Rezaie P and Lantos PL
Brain Research Reviews, 35(1), 55-72 (2001)
The cellular prion protein (PrP(C)): its physiological function and role in disease.
Westergard L
Biochimica et Biophysica Acta, 1772(6), 629-644 (2007)
Transplanted neural precursors enhance host brain-derived myelin regeneration.
Einstein O, et al.
The Journal of Neuroscience, 29(50), 15694-15702 (2009)
Yaron Haviv et al.
Archives of neurology, 65(6), 762-775 (2008-06-11)
The misfolding and aggregation of specific proteins has emerged as a key feature of several neurodegenerative diseases. In prion diseases, progressive disease and neuronal loss are associated with the accumulation of PrP(Sc), the misfolded isoform of PrP(C). Previous in vitro
Robert Hnasko et al.
PloS one, 4(2), e4440-e4440 (2009-02-13)
Intracerebral inoculation of 263K Scrapie brain homogenate (PrPsc) with a self-assembling RADA-peptide (RADA) significantly delayed disease onset and increased hamster survival. Time of survival was dependent on the dose of RADA and pre-incubation with PrPsc prior to inoculation. RADA treatment

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