• Product name
    Anti-Prion protein PrP antibody
    See all Prion protein PrP primary antibodies
  • Description
    Goat polyclonal to Prion protein PrP
  • Host species
  • Tested applications
    Suitable for: IHC-FoFr, WB, ELISA, Dot blot, IHC-Pmore details
  • Species reactivity
    Reacts with: Mouse, Sheep, Hamster, Cow, Human
  • Immunogen

    Synthetic peptide, corresponding to amino acids 79-97 of Human Prion protein PrP.

  • Positive control
    • CJD brain.
  • General notes
    Prion protein has recently been classified as CD230 at the 7th HLDA workshop.



Our Abpromise guarantee covers the use of ab6664 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
IHC-FoFr Use at an assay dependent dilution. PubMed: 16492732
WB Use at an assay dependent dilution.
ELISA Use at an assay dependent dilution. It has only been tested for direct ELISA but not for Sandwich ELISA.
Dot blot Use at an assay dependent dilution.
IHC-P 1/200. Do not perform antigen retrieval.


  • 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


  • CJD brain section showing stained prion plaque using ab6664 at 1:200


This product has been referenced in:
  • Piccardo P  et al. Dissociation of prion protein amyloid seeding from transmission of a spongiform encephalopathy. J Virol 87:12349-56 (2013). Read more (PubMed: 24027305) »
  • Steele AD  et al. Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc Natl Acad Sci U S A 103:3416-21 (2006). ICC/IF, IHC-FoFr ; Mouse . Read more (PubMed: 16492732) »

See all 2 Publications for this product

Customer reviews and Q&As

Thank you for kindly confirming these details.

As requested, we would be pleased to arrange this free of charge replacement. In order to do this, I am forwarding these details on to our distributors team who will be happy to organize this fo...

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I am sorry to hear the suggestions made have not improved the results on this occasion. I appreciate the time you have spent on these experiments and would be pleased to ...

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Thank you for your reply and for kindly confirming this further information. This enquiry has been forwarded to me as my colleague is currently away from the office.

I appreciate your cooperation and understand your concerns. It is regrettab...

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Thank you for your reply and providing that extra information.

I am happy to send you ab73098 as a free of charge replacement as ab7303 also did not prove successful for you. Your new order number is ****** and currently we are out of stock o...

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Thank you for your reply.

I am sorry that the replacement antibody that we sent did not prove to be successful for you. I know that you mentioned that you tried different antigen retrieval protocols, but did you also try different antibody co...

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Thank you for your reply.

I have processed your request to receive ab7303 as a replacement for ab6664 which did not work in IHC-P. Currently ab7303 is out of stock, but we have an estimated delivery date of 14th February and your new order nu...

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Thank you for your reply.

I am sorry that the O/N incubation did not prove to be successful, I could be as you initially suspected and that it is the formic acid fix that is the problem.

I am happy to send you ab7303 to see if that ...

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Thank you for your reply.

Based on the information you provided and the extensive troubleshooting you have already done using this antibody, I agree that the most probable cause is the formic acid. As the most successful protocols using this ...

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Thank you for contacting Abcam.

I am sorry that you are having problems with ab6664 in IHC-P on human sections. The antibody is covered under our Abpromise for six months and is guaranteed to work in IHC-P on human samples . If we cannot reso...

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ab6664 has been shown to react with mouse PrPc via western blotting. So if detectable levels of this protein are expressed in N2a cells, then we would guarantee that ab6664 will detect it. Thus no testing agreement will be necessary. I hope this...

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