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Key Documents

AB5058

Sigma-Aldrich

Anti-Prion Protein Antibody, NT, a.a. 78-97

serum, Chemicon®

Synonym(s):

PrP, CD230

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.43

biological source

goat

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... PRNP(5621)

Specificity

Specific for human prion protein (PrP). This antibody immunolabels amyloid plaques in formalin-fixed paraffin sections from Creutzfeld-Jakob Disease (CJD) brain.The prion protein is a large membrane protein that occurs normally in neurons of the human brain and is thought to be involved in synaptic transmission. In prion diseases, such as CJD, Gerstmann-Straussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI), Alpers Syndrome and Kuru, the normal cellular form of this protein (PrPc) is transformed into an altered protein when it comes into contact with an infectious prion protein (PrPsc) from another host. This altered PrPsc accumulates in cytoplasmic vesicles of diseased individuals forming lesions, vacuoles and amyloid deposits.

Immunogen

Epitope: N-terminus, a.a. 78-97
Synthetic peptide that corresponds to amino acids 79-97 of the N-terminus of the human PrP27-30.

Application

Anti-Prion Protein Antibody, N-terminus, a.a. 78-97 detects level of Prion Protein & has been published & validated for use in ELISA, WB, IH(P).
Immunohistochemistry: >1:200 on paraffin embedded, formalin fixed human brain.

Western blots: >1:2,000

ELISA: >1:35,000

Optimal working dilutions must be determined by the end user.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Physical form

Goat serum. Liquid containing 0.01% thimerosal

Storage and Stability

Maintain at -20°C in undiluted aliquots for up to 12 months. Avoid repeated freeze/thaw cycles.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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

WGK 1

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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Viviana Zomosa-Signoret et al.
Neuropathology : official journal of the Japanese Society of Neuropathology, 31(2), 162-169 (2010-07-30)
Prion diseases are caused by an abnormal form of the prion protein (PrP(Sc)). We identified, with lectins, post-translational modifications of brain proteins due to glycosylation in a Gerstmann-Sträussler-Scheinker (GSS) patient. The lectin Amaranthus leucocarpus (ALL), specific for mucin type O-glycosylated
Erik C Gunther et al.
Cell reports, 26(1), 145-158 (2019-01-04)
Cellular prion protein (PrPC) binds the scrapie conformation of PrP (PrPSc) and oligomeric β-amyloid peptide (Aβo) to mediate transmissible spongiform encephalopathy (TSE) and Alzheimer's disease (AD), respectively. We conducted cellular and biochemical screens for compounds blocking PrPC interaction with Aβo.

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