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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

Synonyme(s) :

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

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

IPC1, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen 25-35 kDa

Espèces réactives

hamster, mouse, rat

Concentration

1 mg/mL

Technique(s)

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

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Description générale

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.

Immunogène

recombinant mouse PrPC.

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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