AB5058
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
Recommended Products
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
NCBI accession no.
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.
Western blots: >1:2,000
ELISA: >1:35,000
Optimal working dilutions must be determined by the end user.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
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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Description
Pricing
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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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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