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Key Documents

P0110

Sigma-Aldrich

Anti-Prion Protein antibody, Mouse monoclonal

clone 8H4, purified from hybridoma cell culture

Sinonimo/i:

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

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

8H4, monoclonal

Forma fisica

buffered aqueous solution

PM

antigen 25-35 kDa

Reattività contro le specie

bovine, mouse, monkey, human, sheep, rat

Confezionamento

antibody small pack of 25 μL

Concentrazione

~1.5 mg/mL

tecniche

electron microscopy: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 2-4 μg/mL using mouse brain extract

Isotipo

IgG2b

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

bovine ... PRNP(281427)
human ... PRNP(5621)
mouse ... Prnp(19122)
rat ... Prnp(24686)
sheep ... PRNP(493887)

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Descrizione generale

Anti-Prion Protein antibody, Mouse monoclonal (mouse IgG2b isotype) is derived from the hybridoma 8H4 produced by the fusion of mouse myeloma cells (SP2/0 cells) and splenocytes from Prnp-/- mice immunized with recombinant murine PrPc. Prion protein (PrP) is mapped to human chromosome 20p13. PrP is constitutively expressed in brain and other tissues of healthy humans and animals and is present in high levels at the synapse.
Prion is a cell surface glycoprotein present in two isoform- PrPc (a cellular isoform) and PrPsc (a disease associated isoform). Monoclonal anti-prion protein antibody is useful for the treatment of prion disease, by inhibiting the abnormal isoform PrPsc . This antibody can also be used for passive immunization of animals to protect them from prion infection. Anti prion protein antibody may be used to inhibit abnormal prion protein accumulation in cultured scrapie-infected neuroblastoma cells. The antibody reacts specifically with amino acids 145-180 of human prion. It also has specificity for monkey, cow, sheep, deer, squirrel, hamster, mouse and rat.

Specificità

The antibody epitope resides within amino acids 145-180 of human prion.

Immunogeno

Recombinant MoPrp residues 121-231
recombinant mouse PrPC.

Applicazioni

Anti-Prion Protein antibody, mouse monoclonal may be used in:
  • immunoblotting
  • flow cytometry
  • immunocytochemistry
  • immunoprecipitation
  • immunoelectron microscopy
  • immunohistochemistry
  • enzyme linked immunosorbent assay

Azioni biochim/fisiol

Prion-related diseases are fatal neurodegenerative disorders also known as transmissible spongiform encephalopathies (TSEs). 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. Disease-associated prion protein specifically inhibits the proteolytic β-subunits of the 26S proteasome. This may clarify the mechanism of cell death by the prion protein. Prion protein 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 antioxidant activity.

Stato fisico

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Nurul Sulimai et al.
Biomolecules, 11(9) (2021-09-29)
Neuroinflammatory diseases, such as Alzheimer's disease (AD) and traumatic brain injury (TBI), are associated with the extravascular deposition of the fibrinogen (Fg) derivative fibrin and are accompanied with memory impairment. We found that during the hyperfibrinogenemia that typically occurs during
G Zanusso et al.
Proceedings of the National Academy of Sciences of the United States of America, 95(15), 8812-8816 (1998-07-22)
By immunizing prion knockout mice (Prnp-/-) with recombinant murine prion protein (PrPc), we obtained a panel of mAbs specific for murine PrPc. These mAbs can be applied to immunoblotting, cell surface immunofluorescent staining, and immunohistochemistry at light and electron microscopy.
The affinity of copper binding to the prion protein octarepeat domain: evidence for negative cooperativity
Walter ED, et al.
Biochemistry, 45(43), 13083-13092 (2006)
The intricate mechanisms of neurodegeneration in prion diseases
Soto C and Satani N
Trends in Molecular Medicine, 17(1), 14-24 (2011)
Prion diseases: from protein to cell pathology
Kovacs GG and Budka H
The American Journal of Pathology, 172(3), 555-565 (2008)

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