Anti-Prion protein PrP 抗体 [8H4] (ab61409)

製品の概要

  • 製品名Anti-Prion protein PrP antibody [8H4]
    Prion protein PrP 一次抗体 製品一覧
  • 製品の詳細
    Mouse monoclonal [8H4] to Prion protein PrP
  • アプリケーション適用あり: IHC-P, WB, IP, ICC, Flow Cyt, Indirect ELISAmore details
  • 種交差性
    交差種: Mouse, Rat, Sheep, Cow, Human, Monkey
  • 免疫原

    Recombinant full length Mouse Prion protein PrP

  • エピトープThe antibody epitope resides within amino acids 145-180 of human Prion protein PrP.
  • ポジティブ・コントロール
    • Mouse brain extract

製品の特性

アプリケーション

Our Abpromise guarantee covers the use of ab61409 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
IHC-P Use at an assay dependent concentration.
WB Use a concentration of 2 - 4 µg/ml. Predicted molecular weight: 28 kDa.
IP Use at an assay dependent concentration.
ICC Use at an assay dependent concentration.
Flow Cyt Use at an assay dependent concentration. ab170192-Mouse monoclonal IgG2b, is suitable for use as an isotype control with this antibody.
Indirect ELISA Use at an assay dependent concentration.

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 [8H4] 画像

  • All lanes : Anti-Prion protein PrP antibody [8H4] (ab61409) at 1/2500 dilution

    Lane 1 : Wild type mouse hippocampus whole tissue lysate
    Lane 2 : Prnp-/- mouse hippocampus whole tissue lysate

    Lysates/proteins at 30 µg per lane.

    Secondary
    HRP-conjugated sheep anti-mouse IgG monoclonal at 1/5000 dilution
    Developed using the ECL technique

    Performed under reducing conditions.

    Predicted band size : 28 kDa
    Observed band size : 25-37 kDa (why is the actual band size different from the predicted?)


    Exposure time : 30 seconds

    This image is courtesy of an anonymous Abreview

    See Abreview

Anti-Prion protein PrP antibody [8H4] (ab61409) 使用論文

This product has been referenced in:
  • Liu T  et al. IGF-1-induced enhancement of PRNP expression depends on the negative regulation of transcription factor FOXO3a. PLoS One 8:e71896 (2013). WB ; Human . Read more (PubMed: 23967259) »

See 1 Publication for this product

Product Wall

Application Western blot
Loading amount 30 µg
Gel Running Conditions Reduced Denaturing (4-12% SDS-PAGE)
Sample Mouse Tissue lysate - whole (hippocampus)
Specification hippocampus
Blocking step Rapid Block as blocking agent for 20 minute(s) · Concentration: 100% · Temperature: 24°C
Username

Abcam user community

Verified customer

投稿 Sep 12 2014

Application Western blot
Loading amount 30 µg
Gel Running Conditions Reduced Denaturing (12)
Sample Human Tissue lysate - whole (CNS tissue)
Specification CNS tissue
Blocking step Milk as blocking agent for 1 hour(s) and 0 minute(s) · Concentration: 5% · Temperature: 25°C
Username

Abcam user community

Verified customer

投稿 Aug 01 2014

Application Western blot
Loading amount 150 µg
Gel Running Conditions Reduced Denaturing (15)
Sample Mouse Tissue lysate - whole (Spinal Cord)
Specification Spinal Cord
Blocking step Milk as blocking agent for 1 hour(s) and 0 minute(s) · Concentration: 5% · Temperature: 25°C
Username

Abcam user community

Verified customer

投稿 Apr 16 2014

Thank you for taking the time to complete our questionnaire and contact us. I am sorry to hear you have had difficulty obtaining satisfactory results from this antibody.

The details you have kindly provided will provide us with vital informa...

Read More

Thank you for your enquiry and your interest in our products.

Currently, we do not have Western blot image for this particular product (ab61409). However, I would like to reassure you and your customer Western blot is a tested application and...

Read More

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"