A part of MilliporeSigma

AB5058 | Anti-Prion Protein Antibody, NT, a.a. 78-97

200 µL  
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      Replacement Information

      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H ELISA, WB, IH(P) Gt Serum Polyclonal Antibody
      Catalogue NumberAB5058
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Prion Protein Antibody, NT, a.a. 78-97
      Alternate Names
      • PrP
      • CD230
      Product Information
      PresentationGoat serum. Liquid containing 0.01% thimerosal
      ApplicationAnti-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).
      Key Applications
      • ELISA
      • Western Blotting
      • Immunohistochemistry (Paraffin)
      Application NotesImmunohistochemistry: >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.
      Biological Information
      ImmunogenSynthetic peptide that corresponds to amino acids 79-97 of the N-terminus of the human PrP27-30.
      EpitopeN-terminus, a.a. 78-97
      SpecificitySpecific 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.
      Species Reactivity
      • Human
      Antibody TypePolyclonal 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
      • CD230
      • PrP33-35C
      • PRP
      • ASCR
      • PrP27-30
      • GSS
      • CJD
      • PRIP
      • PrP
      • PrPc
      • MGC26679
      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.
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      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 ConditionsMaintain at -20°C in undiluted aliquots for up to 12 months. Avoid repeated freeze/thaw cycles.
      Packaging Information
      Material Size200 µL
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      GOAT ANTI-PRION PROTEIN (PrP27-30) 2479819


      Reference overviewPub Med ID
      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
      Molecular and genetic features of a labeled class of spinal substantia gelatinosa neurons in a transgenic mouse.
      Adam W Hantman, Edward R Perl
      The Journal of comparative neurology 492 90-100 2005

      Show Abstract
      16175558 16175558
      Toluidine blue-O staining of prion protein deposits.
      A Sánchez, A Guzmán, A Ortiz, D Rembao, B Espinosa, E Zenteno, J Guevara
      Histochemistry and cell biology 116 519-24 2001

      Show Abstract
      11810193 11810193
      Copper has differential effect on prion protein with polymorphism of position 129.
      B S Wong, C Clive, S J Haswell, R A Williamson, D R Burton, P Gambetti, M S Sy, I M Jones, D R Brown
      Biochemical and biophysical research communications 269 726-31 2000

      Show Abstract
      10720484 10720484
      Selective oxidation of methionine residues in prion proteins.
      B S Wong, H Wang, D R Brown, I M Jones
      Biochemical and biophysical research communications 259 352-5 1999

      Show Abstract
      10362513 10362513

      Data Sheet

      Anti-Prion Protein, N-terminus, a.a. 78-97 - Data Sheet

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