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Key Documents

AB5058

Sigma-Aldrich

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

serum, Chemicon®

Synonyme(s) :

PrP, CD230

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About This Item

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

Source biologique

goat

Niveau de qualité

Forme d'anticorps

serum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

human

Fabricant/nom de marque

Chemicon®

Technique(s)

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PRNP(5621)

Spécificité

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.

Immunogène

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

Forme physique

Goat serum. Liquid containing 0.01% thimerosal

Stockage et stabilité

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

Informations légales

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

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 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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