Anti-Prion protein PrP 抗体 [EP1802Y] (ab52604)


  • 製品名Anti-Prion protein PrP antibody [EP1802Y]
    Prion protein PrP 一次抗体 製品一覧
  • 製品の詳細
    Rabbit monoclonal [EP1802Y] to Prion protein PrP
  • アプリケーション適用あり: WB, Flow Cyt, IHC-P, ICC/IFmore details
    適用なし: IP
  • 種交差性
    交差種: Mouse, Rat, Human
  • 免疫原

    A synthetic peptide corresponding to residues near the C-terminus of human Prion protein PrP.

  • ポジティブ・コントロール
    • Fetal brain lysate; brain glioma tissue.
  • 特記事項

    This product is a recombinant rabbit monoclonal antibody.


    Produced using Abcam’s RabMAb® technology. RabMAb® technology is covered by the following U.S. Patents, No. 5,675,063 and/or 7,429,487.



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.

アプリケーション Abreviews 特記事項
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.
  • 追加情報Is unsuitable for IP.
  • ターゲット情報

    • 機能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).
    • 関連疾患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.
    • 配列類似性Belongs to the prion family.
    • ドメイン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.
    • 翻訳後修飾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.
    • 細胞内局在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
    • 参照データベース
    • 別名
      • 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

    Anti-Prion protein PrP antibody [EP1802Y] 画像

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

      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.

    Anti-Prion protein PrP antibody [EP1802Y] (ab52604) 使用論文

    This product has been referenced in:
    • Doolan KM & Colby DW Conformation-dependent epitopes recognized by prion protein antibodies probed using mutational scanning and deep sequencing. J Mol Biol 427:328-40 (2015). Mouse . Read more (PubMed: 25451031) »
    • Rouvinski A  et al. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. J Cell Biol 204:423-41 (2014). Read more (PubMed: 24493590) »

    See all 11 Publications for this product

    Product Wall

    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

    Miss. Imane Ghafir El Idrissi

    Verified customer

    投稿 Feb 12 2016

    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 curr...

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    Thanks for the additional information. Here is a link to an HRP-conjugated secondary antibody you could for western blotting with ab703: I hope this is helpful. Please contact me again if ...

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    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...

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    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...

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