Overview

  • Product name
    Anti-Prion protein PrP antibody [EP1802Y]
    See all Prion protein PrP primary antibodies
  • Description
    Rabbit monoclonal [EP1802Y] to Prion protein PrP
  • Host species
    Rabbit
  • Tested applications
    Suitable for: WB, Flow Cyt, IHC-P, ICC/IFmore details
    Unsuitable for: IP
  • Species reactivity
    Reacts with: Mouse, Rat, Human
  • Immunogen

    Synthetic peptide within Human Prion protein PrP aa 200-300 (C terminal). The exact sequence is proprietary.

  • Positive control
    • Fetal brain lysate; brain glioma tissue.
  • General notes

    Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMab® patents

    We are constantly working hard to ensure we provide our customers with best in class antibodies. As a result of this work we are pleased to now offer this antibody in purified format. We are in the process of updating our datasheets. The purified format is designated 'PUR' on our product labels. If you have any questions regarding this update, please contact our Scientific Support team.

    This product is a recombinant rabbit monoclonal antibody.

Properties

Applications

Our Abpromise guarantee covers the use of ab52604 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 1/5000 - 1/10000. Detects a band of approximately 28 kDa (predicted molecular weight: 28 kDa).
Flow Cyt 1/200.

ab172730 - Rabbit monoclonal IgG, is suitable for use as an isotype control with this antibody.

IHC-P Use at an assay dependent concentration.
ICC/IF 1/100 - 1/250.
  • Application notes
    Is unsuitable for IP.
  • Target

    • 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
      modifications
      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

    Images

    • Anti-Prion protein PrP antibody [EP1802Y] (ab52604) at 1/10000 dilution + fetal brain lysate at 10 µg

      Secondary
      HRP-labelled goat anti-rabbit at 1/2000 dilution

      Predicted band size: 28 kDa

    • Immunohistochemical analysis of brain glioma using ab52604 at a dilution of 1/100-1/250.
    • Overlay histogram showing SH-SY5Y cells stained with ab52604 (red line). The cells were fixed with 4% paraformaldehyde (10 min) and then permeabilized with 0.1% PBS-Tween for 20 min. The cells were then incubated in 1x PBS / 10% normal goat serum / 0.3M glycine to block non-specific protein-protein interactions followed by the antibody (ab52604, 1/100 dilution) for 30 min at 22ºC. The secondary antibody used was DyLight® 488 goat anti-rabbit IgG (H+L) (ab96899) at 1/500 dilution for 30 min at 22ºC. Isotype control antibody (black line) was rabbit IgG (monoclonal) (1µg/1x106 cells) used under the same conditions. Acquisition of >5,000 events was performed. This antibody gave a positive signal in SH-SY5Y cells fixed with 80% methanol (5 min)/permeabilized with 0.1% PBS-Tween for 20 min used under the same conditions.

    References

    This product has been referenced in:
    • Sokolina K  et al. Systematic protein-protein interaction mapping for clinically relevant human GPCRs. Mol Syst Biol 13:918 (2017). IP . Read more (PubMed: 28298427) »
    • Déry MA & LeBlanc AC Luman contributes to brefeldin A-induced prion protein gene expression by interacting with the ERSE26 element. Sci Rep 7:42285 (2017). WB ; Human . Read more (PubMed: 28205568) »
    See all 18 Publications for this product

    Customer reviews and Q&As

    1-5 of 5 Abreviews or Q&A

    Abcam guarantees this product to work in the species/application used in this Abreview.
    Application
    Western blot
    Sample
    Mouse Cell lysate - whole cell (Neuroblasome cells)
    Gel Running Conditions
    Non-reduced Non-Denaturing (Native)
    Loading amount
    100 µg
    Specification
    Neuroblasome cells
    Blocking step
    BSA as blocking agent for 1 hour(s) and 0 minute(s) · Concentration: 5% · Temperature: 20°C

    Imane Ghafir El Idrissi

    Verified customer

    Submitted Feb 12 2016

    Answer

    Thank you for contacting us again regarding our antibodies directed against PrP. I am sorry that I was not in the office and able to deal with your call. I am sorry that it has taken some time to find more information relating to the antibodies we currently have to offer and which may be the most suitable for you. We have a number of antibodies which have been confirmed to recognise both the PrPc and PrPsc forms of the protein. These include: ab6664, ab703 and ab14219. I am unsure as to how you are currently performing your experiments but it seems that the normal protocol is to use proteinase K to destroy any PrPc in your sample and then any protein which is left (PrPsc) can be detected using Western blotting. As discussed over the phone, ab703 seems to be appropriate for your experiments, however I am a little concerned that the results that you have been observing have been highly non-specific and the Western blot for this antibody has shown to give quite broad bands. This antibody is covered by the Abpromise and if you do choose to buy it we would offer you all the support we can to make it perform as expected and if you were to be unhappy with the results youmay be entitled to a free of charge replacement or a refund. I would suggest considering ab52604 as this antibody has shown very clean Western blotting bands with human fetal, mouse and ratbrain. I have attached the image to this email. Although this antibody has not been tested to see if both forms of the protein are recognised, it seems likely that it would, using the same procedure of proteinase K treatment. However, as this has not beenconclusivelyconfirmed I would be willing to offer a testing discount to you. This would involve you buying this antibody, testing it with your samples to assess the specificity and once you have shared the results with us through submitting an Abreview of your results (should only take 5-10 minutes) you would be entitled to a primaryantibody of your choice from our catalogue. More information onthis offer can befound here: https://www.abcam.com/collaboratordiscount If you would be interested in this offer please let me know and I can issue you witha discount code. I am still trying togather more informationregarding theotherantibodiesinourcatalogueand will keep youupdated with any furtherrelevant information. I hope this information has been of help.If you require any further information please let me know.

    Read More

    Answer

    Thanks for the additional information. Here is a link to an HRP-conjugated secondary antibody you could for western blotting with ab703: https://www.abcam.com/Rabbit-IgG-secondary-antibody-ab16284.html I hope this is helpful. Please contact me again if  you have any further questions.

    Read More

    Answer

    Thank you for your enquiry. I would be happy to help you find a secondary antibody for use with ab703. If you could let me know what application you would use the antibody for and what conjugate you would like attached to the secondary (eg. HRP, biotin, what color fluorophore) then I can recommend a product.

    Read More

    Answer

    Thank you for contacting us. The immunogen used for ab52604 was a smaller peptide from human Prion protein, whereas the protein ab753 is recombinant bovine Prion protein. Ab52604 was not tested for bovine and is not guaranteed to react; a better choice for use with ab753 is ab703, which used ab753 as the immunogen and will definately detect it. I hope this information is helpful to you. Please do not hesitate to contact us if you need any more advice or information.  

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