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MAB5424 Anti-Prion Protein Antibody

Anti-Prion Protein Antibody is an antibody against Prion Protein for use in ELISA, WB, IH.

Anti-Prion Protein Antibody MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
Research Category: Neuroscience Research Sub-Category: Neurodegenerative Diseases Gene Symbol: PRNP, CD230, PrP33-35C, PRP, ASCR, PrP27-30, GSS, CJD, PRIP, PrP, PrPc, MGC26679 UniProt Number: P04156
MAB5424
100 µg  
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Tabulka spec. kláve

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
Katalogové číslo 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

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