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P0110

Sigma-Aldrich

Anti-Prion Protein antibody, Mouse monoclonal

clone 8H4, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-Prion Protein antibody produced in mouse, 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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

8H4, monoclonal

form

buffered aqueous solution

mol wt

antigen 25-35 kDa

species reactivity

bovine, mouse, monkey, human, sheep, rat

packaging

antibody small pack of 25 μL

concentration

~1.5 mg/mL

technique(s)

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

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

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General description

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.

Specificity

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

Immunogen

Recombinant MoPrp residues 121-231
recombinant mouse PrPC.

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
A special report I. Prion protein (Prp)-amyloid plaques in the transmissible spongiform encephalopathies (TSEs) or prion disease revisited.
Liberski PP, et al.
Polish Journal of Pathology : Official Journal of the Polish Society of Pathologists, 52(4), 169-186 (2001)
Prion diseases: from protein to cell pathology
Kovacs GG and Budka H
The American Journal of Pathology, 172(3), 555-565 (2008)
Holly L Valentine et al.
Toxicology, 274(1-3), 10-17 (2010-05-11)
Previous studies have demonstrated that N,N-diethyldithiocarbamate (DEDC) elevates copper and promotes oxidative stress within the nervous system. However, whether these effects resolve following cessation of exposure or have the potential to persist and result in cumulative injury has not been
Mutational analysis of PRNP in Alzheimer?s disease and frontotemporal dementia in China
Zhang W, et al.
Scientific Reports, 6, 38435-38435 (2016)

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