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MAB1562 Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4

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MAB1562
100 µg  
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Overview

Replacement Information

Key Specifications Table

Species ReactivityKey ApplicationsHostFormatAntibody Type
H, HtELISA, IHC, IH(P), IP, WBMPurifiedMonoclonal Antibody
Description
Catalogue NumberMAB1562
Brand Family Chemicon®
Trade Name
  • Chemicon
DescriptionAnti-Prion Protein Antibody, a.a. 109-112, clone 3F4
Alternate Names
  • PrP
  • CD230
Background InformationPrions are thought to cause a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and the Creutzfeldt-Jakob disease (CJD) in humans. All thus-far hypothesized prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and thought to be fatal. Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing cell death and tissue damage. This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult.
References
Product Information
FormatPurified
HS Code3002 15 90
Control
  • Brain tissue.
PresentationPurified mouse monoclonal IgG2a in buffer containing PBS and no preservative.
Quality LevelMQ100
Applications
ApplicationThis Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4 is validated for use in ELISA, IH, IH(P), IP, WB for the detection of Prion Protein.
Key Applications
  • ELISA
  • Immunohistochemistry
  • Immunohistochemistry (Paraffin)
  • Immunoprecipitation
  • Western Blotting
Application NotesImmunohistochemistry(paraffin):
Representative images from a previous lot. Optimal Staining With Citrate Buffer, pH 6.0, Epitope Retrieval: Human Brain

Immunohistochemistry (Kitamoto et al., 1987):
1:100-1:1,000 *See protocol below.

Epitope must be re-exposed in fixed tissue by pretreatment of tissue using one of the following procedures:
a. formic acid for 10 minutes at room temperature (Kitamoto et al., 1987)
b. hydrolytic autoclaving (Kitamoto et al., 1991)
c. microwaving (BioGenex, San Ramon, CA)

Western Blot: (Kascsak, R.J., 1991; Kascsak, R.J., 1987):
1:10,000-1:100,000 dilution of a previous lot was used.

Immunoprecipitation: (Kascsak, R.J., 1991; Kascsak, R.J., 1987):
1:10-1:100 dilution of a previous lot was used.

ELISA: (Kascsak, R.J., 1991; Kascsak, R.J., 1987):
1:100,000 dilution of a previous lot was used.

Optimal working dilutions must be determined by end user.
Biological Information
Epitopea.a. 109-112
Clone3F4
HostMouse
SpecificityPrion protein, amino acid residues 109-112 of human, hamster and feline. Does not react with PrP from any other mammalian species. MAB1562 is reactive to native and denatured forms of PrP. Tissue or cells which have been fixed requires that the epitope be re-exposed (see below). Recognizes both protease sensitive and protease resistant forms of PrP.
IsotypeIgG2a
Species Reactivity
  • Human
  • Hamster
Antibody TypeMonoclonal Antibody
Entrez Gene Number
Entrez Gene SummaryThe protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. Alternative splicing results in multiple transcript variants encoding the same protein.
Gene Symbol
  • PRNP
  • ASCR
  • PrP27-30
  • GSS
  • CD230
  • CJD
  • PRIP
  • PrPc
  • PrP
  • PrP33-35C
  • MGC26679
  • PRP
Purification MethodProtein A Purfied
UniProt Number
UniProt SummaryFUNCTION: SwissProt: P04156 # The physiological function of PrP is not known.
SIZE: 253 amino acids; 27661 Da
SUBUNIT: PrP has a tendency to aggregate yielding polymers called rods.
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
PTM: The glycosylation pattern (the amount of mono-, di- and non- glycosylated forms or glycoforms) seems to differ in normal and CJD prion.
DISEASE: SwissProt: P04156 # PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs. & Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:123400]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness. & Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:600072]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia. & Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:137440]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births. & Defects in PRNP are the cause of Huntington disease-like 1 (HDL1) [MIM:603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features. & Defects in PRNP are the cause of kuru [MIM:245300]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset. & Defects in PRNP are the cause of prion disease with protracted course [MIM:606688]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.
SIMILARITY:SwissProt: P04156 ## Belongs to the prion family.
Molecular Weight12.3 kDa
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality AssuranceImmunohistochemistry(paraffin):
Prion Protein (cat. # MAB1562) staining pattern/morphology in normal brain. Tissue was pretreated with Citrate, pH 6.0. This lot of antibody was diluted to 1:500, using IHC-Select® Detection with HRP-DAB. Immunoreactivity is seen predominantly as cell body staining of neurons.
Optimal Staining With Citrate Buffer, pH 6.0, Epitope Retrieval: Human Brain
Usage Statement
  • 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.
Storage and Shipping Information
Storage ConditionsStable for 1 year at -20ºC from date of receipt.
Packaging Information
Material Size100 µg
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number GTIN
MAB1562 04053252399336

Documentation

Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4 SDS

Title

Safety Data Sheet (SDS) 

Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4 Certificates of Analysis

TitleLot Number
Anti-Prion Protein, a.a. 109-112, clone -2549020 2549020
Anti-Prion Protein, a.a. 109-112, clone -2639455 2639455
Anti-Prion Protein, a.a. 109-112, clone 3F4 2943134
Anti-Prion Protein, a.a. 109-112, clone 3F4 - 2326314 2326314
Anti-Prion Protein, a.a. 109-112, clone 3F4 - 2424620 2424620
Anti-Prion Protein, a.a. 109-112, clone 3F4 - 2449205 2449205
Anti-Prion Protein, a.a. 109-112, clone 3F4 - 1972270 1972270
Anti-Prion Protein, a.a. 109-112, clone 3F4 - 1990410 1990410
Anti-Prion Protein, a.a. 109-112, clone 3F4 - 2015540 2015540
Anti-Prion Protein, a.a. 109-112, clone 3F4 - 2032215 2032215

References

Reference overviewPub Med ID
Human prion protein sequence elements impede cross-species chronic wasting disease transmission.
Kurt, TD; Jiang, L; Fernández-Borges, N; Bett, C; Liu, J; Yang, T; Spraker, TR; Castilla, J; Eisenberg, D; Kong, Q; Sigurdson, CJ
The Journal of clinical investigation  125  1485-96  2015

Show Abstract
25705888 25705888
Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs.
Rouvinski, A; Karniely, S; Kounin, M; Moussa, S; Goldberg, MD; Warburg, G; Lyakhovetsky, R; Papy-Garcia, D; Kutzsche, J; Korth, C; Carlson, GA; Godsave, SF; Peters, PJ; Luhr, K; Kristensson, K; Taraboulos, A
The Journal of cell biology  204  423-41  2014

Show Abstract
24493590 24493590
Brain microglia were activated in sporadic CJD but almost unchanged in fatal familial insomnia and G114V genetic CJD.
Shi, Q; Xie, WL; Zhang, B; Chen, LN; Xu, Y; Wang, K; Ren, K; Zhang, XM; Chen, C; Zhang, J; Dong, XP
Virology journal  10  216  2013

Show Abstract
23816234 23816234
Sialylated and O-glycosidically linked glycans in prion protein deposits in a case of Gerstmann-Sträussler-Scheinker disease.
Viviana Zomosa-Signoret,Miguel Mayoral,Daniel Limón,Blanca Espinosa,Minerva Calvillo,Edgar Zenteno,Victor Martínez,Jorge Guevara
Neuropathology : official journal of the Japanese Society of Neuropathology  31  2011

Show Abstract
20667006 20667006
Phospholipid composition of membranes directs prions down alternative aggregation pathways.
Robinson, PJ; Pinheiro, TJ
Biophysical journal  98  1520-8  2010

Show Abstract
20409471 20409471
Reference materials for the evaluation of pre-mortem variant Creutzfeldt-Jakob disease diagnostic assays.
J K Cooper,K Ladhani,P D Minor
Vox sanguinis  92  2007

Show Abstract
17456154 17456154
Creutzfeldt-Jakob disease in Mexico.
Leora Velásquez-Pérez, Daniel Rembao-Bojorquez, Jorge Guevara, Rosa María Guadarrama-Torres, Araceli Trejo-Contreras
Neuropathology : official journal of the Japanese Society of Neuropathology  27  419-28  2007

Show Abstract
18018474 18018474
Synaptic prion protein immuno-reactivity in the rodent cerebellum.
A M Haeberlé, C Ribaut-Barassin, G Bombarde, J Mariani, G Hunsmann, J Grassi, Y Bailly, A M Haeberlé, C Ribaut-Barassin, G Bombarde, J Mariani, G Hunsmann, J Grassi, Y Bailly
Microscopy research and technique  50  66-75  2000

Show Abstract
10871550 10871550
Redox-regulation of intrinsic prion expression in multicellular prostate tumor spheroids.
Sauer, H, et al.
Free Radic. Biol. Med., 27: 1276-83 (1999)  1999

Show Abstract
10641721 10641721
Formic acid pretreatment enhances immunostaining of cerebral and systemic amyloids.
Kitamoto, T, et al.
Lab. Invest., 57: 230-6 (1987)  1987

2441141 2441141