• Product name
    Anti-Prion protein PrP antibody [7D9]
    See all Prion protein PrP primary antibodies
  • Description
    Mouse monoclonal [7D9] to Prion protein PrP
  • Host species
  • Specificity
    Ab14219 recognises both protease sensitive and protease resistant forms of PrP (after denaturing).
  • Tested applications
    Suitable for: WB, ELISA, IHC-Pmore details
  • Species reactivity
    Reacts with: Mouse, Rat, Sheep, Hamster, Cow, Cat, Human, Deer, Elk
  • Immunogen

    Recombinant fragment, corresponding to amino acids 23-237 of Prion protein PrP.

  • General notes
    Do not store antibody diluted below 50 µg/ml in the absence of protein. Vortex sample prior to removing aliquot (prolonged storage may show aggregation).



Our Abpromise guarantee covers the use of ab14219 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/10000 - 1/20000. Predicted molecular weight: 32 kDa.
ELISA 1/20000 - 1/50000.
IHC-P Use at an assay dependent concentration. Retrieve antigens with 70% Formic acid for 10-30 minutes at room temperature before commencing with IHC staining protocol.


  • Function
    The 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 disease
    Note=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 similarities
    Belongs to the prion family.
  • Domain
    The 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
    The 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 localization
    Cell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.
  • Information by UniProt
  • Database links
  • Alternative names
    • Alternative prion protein; major prion protein antibody
    • AltPrP antibody
    • ASCR antibody
    • CD230 antibody
    • CD230 antigen antibody
    • CJD antibody
    • GSS antibody
    • KURU antibody
    • Major prion protein antibody
    • p27 30 antibody
    • PRIO_HUMAN antibody
    • Prion protein antibody
    • Prion related protein antibody
    • PRIP antibody
    • PRNP antibody
    • PrP antibody
    • PrP27 30 antibody
    • PrP27-30 antibody
    • PrP33-35C antibody
    • PrPC antibody
    • PrPSc antibody
    • Sinc antibody
    see all


  • IHC-P using Ab14219.


This product has been referenced in:
  • Murphy RG  et al. Alkaline hydrolysis of mouse-adapted scrapie for inactivation and disposal of prion-positive material. J Anim Sci 87:1787-93 (2009). WB ; Mouse . Read more (PubMed: 19098230) »
See 1 Publication for this product

Customer reviews and Q&As

1-4 of 4 Abreviews or Q&A


Thank you for your enquiry. The exact epitope recognized by this antibody has not been mapped. The immunogen for the antibody contains amino acids 23-237 of Prion protein PrP, so the epitope will lie within that range, but unfortunately I do not have any more specific information to give you. I hope this information helps, please do not hesitate to contact us if you need any more advice or information.

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Thank you for your enquiry. Following some consultation with the source of this antisera, I can confirm that this antibody was determined to detect both the protease sensitive and protease resistant forms of PrP (after denaturing) by Western blotting. By running gels of sample material with and without digestion, they were able to distinguish the protease resistant and protease sensitive forms. It may be done by ELISA, but the methodology has not been determined. I hope this information helps, please do not hesitate to contact me should you require further assistance.

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Thank you for your enquiry and patience. I was able to obtain the following information regarding these antibodies. Ab13643 - The epitope has not been mapped. The antibody was generated using a synthetic peptide (derived from regions within the PrP molecule thought to be involved in the conversion of normal protein to the Beta isomer) in a specific tertiary formation. This means the antibody, as we've seen so far, is conformationally dependent. Epitope mapping will not provide useful information. Ab14219 - The epitope has not been precisely mapped. The immunogen that was used to generate the antibody was recombinant PrP amino acids 23-237. The epitope is, therefore, within that region, but I cannot narrow it further. Ab23985 - The immunogen used to generate this antibody was a 15 residue synthetic peptide derived from C-terminal domain of Human Prion Protein PrP. Ab705 - This antibody recognizes a conformational epitope. However, we don't have any additional information at this time. Ab706 - This antibody recognizes a conformational epitope. However, we don't have any additional information at this time. If you have any additional questions, please contact us again.

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The epitope has not been precisely mapped. The immunogen that was used to generate the antibody was recombinant PrP amino acids 23-237. The epitope is, therefore, within that region, but I cannot narrow it further.

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