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Merck

P5999

Sigma-Aldrich

Monoclonal Anti-Prion Protein antibody produced in mouse

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

Sinónimos:

Anti-AA960666, Anti-CD230, Anti-PRIP, 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

origen biológico

mouse

conjugado

unconjugated

forma del anticuerpo

purified immunoglobulin

tipo de anticuerpo

primary antibodies

clon

IPC1, monoclonal

formulario

buffered aqueous solution

mol peso

antigen 25-35 kDa

reactividad de especies

hamster, mouse, rat

concentración

1 mg/mL

técnicas

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

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

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

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Descripción general

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.

Inmunógeno

recombinant mouse PrPC.

Aplicación

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

Acciones bioquímicas o 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.

Cláusula de descargo de responsabilidad

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 clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

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


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Characterization of cell-surface prion protein relative to its recombinant analogue: insights from molecular dynamics simulations of diglycosylated, membrane-bound human prion protein.
DeMarco ML and Daggett V
Journal of Neurochemistry, 109(1), 60-73 (2009)
Ofira Einstein et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 29(50), 15694-15702 (2009-12-18)
In multiple sclerosis lesions resident oligodendrocyte progenitor cells (OPCs) are present, but fail to remyelinate. In the current study we examined whether neural precursor cell (NPC) transplantation can facilitate host brain-derived remyelination. We used the chronic cuprizone-induced demyelination model in
Function of PrPC as a copper-binding protein at the synapse.
Prion Diseases, 239-249 (2000)
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)

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