Overview

  • Product name

    Anti-Prion protein PrP antibody [8H4]
    See all Prion protein PrP primary antibodies
  • Description

    Mouse monoclonal [8H4] to Prion protein PrP
  • Host species

    Mouse
  • Tested applications

    Suitable for: IHC-P, WB, IP, ICC, Flow Cyt, Indirect ELISAmore details
  • Species reactivity

    Reacts with: Mouse, Rat, Sheep, Cow, Human, Monkey
  • Immunogen

    Recombinant full length protein corresponding to Mouse Prion protein PrP.

  • Epitope

    The antibody epitope resides within amino acids 145-180 of human Prion protein PrP.
  • Positive control

    • Mouse brain extract

Properties

Applications

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.

Application Abreviews Notes
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.

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

  • 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
    All lanes : 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

    See Abreview

References

This product has been referenced in:

  • Gunther EC  et al. Rescue of Transgenic Alzheimer's Pathophysiology by Polymeric Cellular Prion Protein Antagonists. Cell Rep 26:145-158.e8 (2019). Read more (PubMed: 30605671) »
  • Wiegmans AP  et al. Secreted cellular prion protein binds doxorubicin and correlates with anthracycline resistance in breast cancer. JCI Insight 5:N/A (2019). Read more (PubMed: 30830863) »
See all 7 Publications for this product

Customer reviews and Q&As

1-5 of 5 Abreviews or Q&A

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

Abcam user community

Verified customer

Submitted 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

Abcam user community

Verified customer

Submitted 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

Abcam user community

Verified customer

Submitted Apr 16 2014

Answer

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 information for our monitoring of product quality. I would like to reassure you that this antibody is tested and covered by our guarantee for WB and human samples.

I appreciate the time you have spent in the laboratory and understand your concerns. It is regrettable the results have not been successful. Reviewing the details, I am sorry there very few tips to provide on this occasion to help improve the results. I can suggest you may have regrettably received a bad vial.

I can recommend you may like to consider trying the following options:

1. I can recommend to check the amount of protein loaded and ensure this is just 20 - 30 ug so the gel is not overloaded.

2. I can suggest to try BSA rather than milk to block, changing blocking agents can sometimes help to improve results.

3. Try a lower concentration of antibody to help reduce the non specific binding, try 1:2000. The concentration of secondary antibody may also need to be reduced to help optimize the results.

Alternatively, or if these tips do not work, I am pleased to offer you a free of charge replacement or credit note in compensation.

Thank you for your cooperation. I look forward to hearing from you with details of how you would like to proceed.

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Question
Answer

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 our Abpromise will certainly apply for this assay.

I hope this helps and if I can assist further, please do not hesitate to contact me.

.

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