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MAB5424 Anti-Prion Protein Antibody

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MAB5424
100 µg  
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      Overview

      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      B, M, Sh, Elk, MdELISA, WB, IHCMPurifiedMonoclonal Antibody
      Description
      Catalogue NumberMAB5424
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Prion Protein Antibody
      Alternate Names
      • PrP
      • CD230
      References
      Product Information
      FormatPurified
      PresentationPurified immunoglobulin. Liquid in PBS. Contains no preservative.
      Quality LevelMQ100
      Applications
      ApplicationAnti-Prion Protein Antibody is an antibody against Prion Protein for use in ELISA, WB, IH.
      Key Applications
      • ELISA
      • Western Blotting
      • Immunohistochemistry
      Application NotesWestern blot: 1:50,000-1:200,000

      Immunohistochemistry: 1:100-1:500. 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

      b. hydrolytic autoclaving

      c. heat induced epitope retrieval

      ELISA: 1:20,000-1:50,000

      Optimal working dilutions must be determined by end user.
      Biological Information
      ImmunogenRecombinant PrP amino acids 23-237.
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      HostMouse
      SpecificityReacts with prion protein (PrP) from bovine, sheep, mule deer, elk and mouse. The monoclonal recognizes both protease sensitive and protease resistant forms of PrP (after denaturing).
      IsotypeIgG1
      Species Reactivity
      • Bovine
      • Mouse
      • Sheep
      • Elk
      • Mule Deer
      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
      • 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
      Dimensions
      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 to -70°C in undiluted aliquots for up to 6 months after date of receipt.

      Avoid repeated freeze/thaw cycles.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      MAB5424 04053252467172

      Documentation

      Anti-Prion Protein Antibody MSDS

      Title

      Safety Data Sheet (SDS) 

      Anti-Prion Protein Antibody Certificates of Analysis

      TitleLot Number
      MOUSE ANTI-PRION PROTEIN - 3415661 3415661
      MOUSE ANTI-PRION PROTEIN - 3697982 3697982
      MOUSE ANTI-PRION PROTEIN MONOCLONAL ANTIBODY 2876669
      MOUSE ANTI-PRION PROTEIN MONOCLONAL ANTIBODY - 2279558 2279558
      MOUSE ANTI-PRION PROTEIN MONOCLONAL ANTIBODY -2621739 2621739

      References

      Reference overviewPub Med ID
      Using small molecule reagents to selectively modify epitopes based on their conformation.
      Silva, CJ
      Prion  6  163-73  2001

      Show Abstract
      22436143 22436143