Anti-Prion protein PrP antibody (ab89750)

Overview

• Product nameAnti-Prion protein PrP antibodySee all Prion protein PrP primary antibodies ...
• Description
  Mouse polyclonal to Prion protein PrP
• Tested applicationsWB, ELISA more details
• Species reactivity
  
  Predicted to work with: Sheep, Cow, Human, Deer
• Immunogen

  Recombinant Sheep Prion protein PrP

• Positive controlRecombinant prion protein PrP

Properties

• FormLiquid
• Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
• Storage bufferPreservative: None
  Constituents: Whole serum
• PurityWhole antiserum
• Clonality Polyclonal
• IsotypeIgG
• Research Areas
  • Stem Cells
  • Hematopoietic Progenitors
  • Surface Molecules

  • Neuroscience
  • Neurology process
  • Neurodegenerative disease
  • Prions

Applications

Target

• FunctionThe function of PrP is still under debate. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis (By similarity). Isoform 2 may act as a growth suppressor by arresting the cell cycle at the G0/G1 phase. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro).
• Involvement in diseaseNote=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 type 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 type 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 (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 spongiform encephalopathy with neuropsychiatric features (SENF) [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.
• Sequence similaritiesBelongs to the prion family.
• DomainThe normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization.
  Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization.
• Post-translational
  modificationsThe glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.
  Isoform 2 is sumoylated by SUMO1.
• Cellular localizationCell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.

Target information above from: UniProt accession P04156 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt
• Database links
  • Entrez Gene: 281427 Cow
  • Entrez Gene: 5621 Human
  • Entrez Gene: 493887 Sheep
  • Omim: 176640 Human
  • SwissProt: P10279 Cow
  • SwissProt: P04156 Human
  • SwissProt: P23907 Sheep
  • Unigene: 472010 Human

  • Unigene: 610285 Human
  • Unigene: 727471 Human

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• Alternative names
  AltPrP antibodyASCR antibodyCD230 antibody

  CD230 antigen antibodyCJD antibodyGSS antibodyKURU antibodyMajor prion protein antibodyp27 30 antibodyPRIO_HUMAN antibodyPrion protein antibodyPrion related protein antibodyPRIP antibodyPRNP antibodyPrP antibodyPrP27 30 antibodyPrP27-30 antibodyPrP33-35C antibodyPrPC antibodyPrPSc antibodySinc antibody

  see all

Anti-Prion protein PrP antibody images

• 

  Western blot - Prion protein PrP antibody (ab89750)
  All lanes : Anti-Prion protein PrP antibody (ab89750) at 1/5000 dilution
  
  Lane 1 : Recombinant Prion protein PrP from Cow
  Lane 2 : Recombinant Prion protein PrP from Human
  Lane 3 : Recombinant Prion protein PrP from Sheep
  Lane 4 : Recombinant Prion protein PrP from Deer
  
  Secondary
  HRP-conjugated Goat anti-Mouse IgG/M antibody
  
  Predicted band size : 28 kDa