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AB61409

Anti-Prion protein PrP antibody [8H4]

3

(3 Reviews)

|

(17 Publications)

Anti-Prion protein PrP antibody [8H4] (ab61409) is a mouse monoclonal antibody detecting Prion protein PrP in Western Blot, Flow Cytometry, IP, IHC-P, ELISA. Suitable for Cow, Human, Monkey, Mouse, Rat, Sheep.

- Over 10 publications
- Trusted since 2007

View Alternative Names

CD230, ALTPRP, PRIP, PRP, PRNP, Major prion protein, PrP, ASCR, PrP27-30, PrP33-35C

2 Images
Western blot - Anti-Prion protein PrP antibody [8H4] (AB61409)
  • WB

AbReview45016****

Western blot - Anti-Prion protein PrP antibody [8H4] (AB61409)

All lanes:

Western blot - Anti-Prion protein PrP antibody [8H4] (ab61409) at 1/2500 dilution

Lane 1:

Wild type mouse hippocampus whole tissue lysate at 30 µg

Lane 2:

Prnp-/- mouse hippocampus whole tissue lysate at 30 µg

Secondary

All lanes:

HRP-conjugated sheep anti-mouse IgG monoclonal at 1/5000 dilution

Predicted band size: 28 kDa

Observed band size: 25-37 kDa

true

Exposure time: 30s

This image is courtesy of an anonymous Abreview

Western blot - Anti-Prion protein PrP antibody [8H4] (AB61409)
  • WB

Supplier Data

Western blot - Anti-Prion protein PrP antibody [8H4] (AB61409)

All lanes:

Western blot - Anti-Prion protein PrP antibody [8H4] (ab61409) at 4 µg/mL

All lanes:

Mouse brain extract

Secondary

All lanes:

Goat Anti-Mouse IgG-Peroxidase

Predicted band size: 28 kDa

false

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

8H4

Isotype

IgG2b

Carrier free

No

Reacts with

Mouse, Sheep, Monkey, Human, Cow, Rat

Applications

IHC-P, I-ELISA, IP, WB, ICC, Flow Cyt

applications

Immunogen

Recombinant Full Length Protein corresponding to Mouse Prnp.

P04925

Epitope

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

Reactivity data

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Mouse monoclonal IgG2b, is suitable for use as an isotype control with this antibody.</p>", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "<p></p>", "IELISA-species-checked": "guaranteed", "IELISA-species-dilution-info": "", "IELISA-species-notes": "<p></p>" }, "Sheep": { "WB-species-checked": "guaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>", "ICC-species-checked": "guaranteed", "ICC-species-dilution-info": "", "ICC-species-notes": "<p></p>", "IP-species-checked": "guaranteed", "IP-species-dilution-info": "", "IP-species-notes": "<p></p>", "FlowCyt-species-checked": "guaranteed", "FlowCyt-species-dilution-info": "", "FlowCyt-species-notes": "<p><a href='/en-us/products/primary-antibodies/mouse-igg2b-kappa-monoclonal-7e10g10-isotype-control-ab170192'>ab170192</a> - Mouse monoclonal IgG2b, is suitable for use as an isotype control with this antibody.</p>", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "<p></p>", "IELISA-species-checked": "guaranteed", "IELISA-species-dilution-info": "", "IELISA-species-notes": "<p></p>" } } }

Product details

What is this antibody validated in?
Anti-Prion protein PrP antibody [8H4] (ab61409) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Flow Cytometry (Flow Cyt), Immunoprecipitation (IP), Immunohistochemistry (IHC-P), ELISA in Cow, Human, Monkey, Mouse, Rat, Sheep samples.

Trusted by the scientific community
Anti-Prion protein PrP [8H4] (ab61409) was first used in a scientific publication in 2007 and has been cited over 10 times in peer-reviewed journals.

Properties and storage information

Form
Liquid
Purity
IgG fraction
Purification notes
Purified Immunoglobulin
Storage buffer
pH: 7.4 Preservative: 0.097% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Prion protein also known as PrP or major prion protein plays a mechanical role in the normal functioning of brain cells. It is a glycoprotein with a flexible structure and has an approximate mass of 35-36 kDa. PrP expression is high in nervous tissue. It is present in neurons and glial cells but also surfaces in other tissues like heart and kidney. Alternate names like p-pr-p and f89 refer to specific conformations or studies related to its structure.
Biological function summary

Prion protein assists in maintaining normal cell activities. Researchers do not fully understand its exact biological role but it might be involved in copper ion uptake and protection against oxidative stress. PrP can form complexes with other cellular proteins some of which help in routing signals inside the cell. Additionally prion protein may have synaptic functions related to neurodevelopment and neuroprotection.

Pathways

Prion protein links to both neuroprotective and neurodegenerative pathways. It participates in signaling pathways that protect neurons from apoptosis. This protein associates closely with copper-dependent pathways possibly related to its capacity to bind copper ions which affects oxidative stress responses. Prion protein also interacts with proteins like synapsin to modulate synaptic transmission.

Prion protein is directly related to prion diseases such as Creutzfeldt-Jakob disease and kuru. These diseases arise from misfolded forms of PrP which aggregate and cause neurodegeneration. The misfolded form referred to as PrP^Sc can induce normal PrP to misfold propagating disease. Dopamine receptor proteins and synaptic proteins can indirectly interact or be affected in these disorders highlighting a complex network of affected neural functions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
See full target information PRNP

Publications (17)

Recent publications for all applications. Explore the full list and refine your search

Nature medicine 31:1319-1328 PubMed39810005

2025

In vivo base editing extends lifespan of a humanized mouse model of prion disease.

Applications

Unspecified application

Species

Unspecified reactive species

Meirui An,Jessie R Davis,Jonathan M Levy,Fiona E Serack,John W Harvey,Pamela P Brauer,Catherine P Pirtle,Kiara N Berríos,Gregory A Newby,Wei-Hsi Yeh,Nikita Kamath,Meredith Mortberg,Yuan Lian,Michael Howard,Kendrick DeSouza-Lenz,Kenia Guzman,Aaron Thai,Samantha Graffam,Vanessa Laversenne,Alissa A Coffey,Jeannine Frei,Sarah E Pierce,Jiri G Safar,Benjamin E Deverman,Eric Vallabh Minikel,Sonia M Vallabh,David R Liu

Science (New York, N.Y.) 384:ado7082 PubMed38935715

2024

Brainwide silencing of prion protein by AAV-mediated delivery of an engineered compact epigenetic editor.

Applications

Unspecified application

Species

Unspecified reactive species

Edwin N Neumann,Tessa M Bertozzi,Elaine Wu,Fiona Serack,John W Harvey,Pamela P Brauer,Catherine P Pirtle,Alissa Coffey,Michael Howard,Nikita Kamath,Kenney Lenz,Kenia Guzman,Michael H Raymond,Ahmad S Khalil,Benjamin E Deverman,Eric Vallabh Minikel,Sonia M Vallabh,Jonathan S Weissman

Nature communications 14:8131 PubMed38065962

2023

Excess PrP inhibits muscle cell differentiation via miRNA-enhanced liquid-liquid phase separation implicated in myopathy.

Applications

Unspecified application

Species

Unspecified reactive species

Jing Tao,Yanping Zeng,Bin Dai,Yin Liu,Xiaohan Pan,Li-Qiang Wang,Jie Chen,Yu Zhou,Zuneng Lu,Liwei Xie,Yi Liang

Alzheimer's research & therapy 15:201 PubMed37968719

2023

Neuronal transcriptome, tau and synapse loss in Alzheimer's knock-in mice require prion protein.

Applications

Unspecified application

Species

Unspecified reactive species

Austin Stoner,Li Fu,LaShae Nicholson,Chao Zheng,Takuya Toyonaga,Joshua Spurrier,Will Laird,Zhengxin Cai,Stephen M Strittmatter

Science signaling 15:eabm3720 PubMed36378750

2022

M muscarinic receptor activation reduces the molecular pathology and slows the progression of prion-mediated neurodegenerative disease.

Applications

Unspecified application

Species

Unspecified reactive species

Louis Dwomoh,Mario Rossi,Miriam Scarpa,Elham Khajehali,Colin Molloy,Pawel Herzyk,Shailesh N Mistry,Andrew R Bottrill,Patrick M Sexton,Arthur Christopoulos,Jeffrey Conn,Craig W Lindsley,Sophie J Bradley,Andrew B Tobin

JCI insight 7: PubMed35133987

2022

Regional variability and genotypic and pharmacodynamic effects on PrP concentration in the CNS.

Applications

Unspecified application

Species

Unspecified reactive species

Meredith A Mortberg,Hien T Zhao,Andrew G Reidenbach,Juliana E Gentile,Eric Kuhn,Jill O'Moore,Patrick M Dooley,Theresa R Connors,Curt Mazur,Shona W Allen,Bianca A Trombetta,Alison McManus,Matthew R Moore,Jiewu Liu,Deborah E Cabin,Holly B Kordasiewicz,Joel Mathews,Steven E Arnold,Sonia M Vallabh,Eric Vallabh Minikel

International journal of molecular sciences 22: PubMed34445708

2021

Concussion/Mild Traumatic Brain Injury (TBI) Induces Brain Insulin Resistance: A Positron Emission Tomography (PET) Scanning Study.

Applications

Unspecified application

Species

Unspecified reactive species

Sathiya Sekar,Raja Solomon Viswas,Hajar Miranzadeh Mahabadi,Elahe Alizadeh,Humphrey Fonge,Changiz Taghibiglou

Molecular brain 14:89 PubMed34099009

2021

Cannabinoid receptors distribution in mouse cortical plasma membrane compartments.

Applications

Unspecified application

Species

Unspecified reactive species

Hajar Miranzadeh Mahabadi,Haseeb Bhatti,Robert B Laprairie,Changiz Taghibiglou

PloS one 14:e0218509 PubMed31206560

2019

Epitope mapping of the protease resistant products of RT-QuIC does not allow the discrimination of sCJD subtypes.

Applications

Unspecified application

Species

Unspecified reactive species

Gabriele Piconi,Alexander H Peden,Marcelo A Barria,Alison J E Green

Transfusion 59:2429-2435 PubMed31020675

2019

Integrative genome analysis identified the KANNO blood group antigen as prion protein.

Applications

Unspecified application

Species

Unspecified reactive species

Yosuke Omae,Shoichi Ito,Mayumi Takeuchi,Kazumi Isa,Kenichi Ogasawara,Kinuyo Kawabata,Akira Oda,Sayaka Kaito,Hatsue Tsuneyama,Makoto Uchikawa,Ikuo Wada,Hitoshi Ohto,Katsushi Tokunaga
View all publications

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