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AB703

Anti-Prion protein PrP antibody

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(5 Publications )

Rabbit Polyclonal Prion protein PrP antibody. Suitable for WB and reacts with Mouse samples. Cited in 5 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Cow PRNP.
1 Images
Western blot - Anti-Prion protein PrP antibody (AB703)
  • WB

Unknown

Western blot - Anti-Prion protein PrP antibody (AB703)

Lane 1 : MW standard
Lane 2 : wild-type mice (PrPc)
Lane 3 : CDI/PrPsc (PK-)
Lane 4 : CDI/PrPsc (PK+),
Lane 5 : PrP 0/0 mice
CDI = clinically ill CD-1 mice, PK = digested with Proteinase K.

Lane 1 : MW standard
Lane 2 : wild-type mice (PrPc)
Lane 3 : CDI/PrPsc (PK-)
Lane 4 : CDI/PrPsc (PK+),
Lane 5 : PrP 0/0 mice
CDI = clinically ill CD-1 mice, PK = digested with Proteinase K.

All lanes:

Western blot - Anti-Prion protein PrP antibody (ab703)

Predicted band size: 28 kDa

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This image is courtesy of Dr. M. Glatzel, Institut of Neuropathology, University Hospital of Zürich, Switzerland

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse

Applications

WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Cow PRNP.

P10279

Specificity

Recognises natural PrPc and conformationally changed PrPc (PrPsc). Recognises recombinant protein ,ab753, in western blot and ELISA.

Reactivity data

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Properties and storage information

Form
Liquid
Purity
Whole antiserum
Storage buffer
Preservative: 0.02% Sodium azide Constituents: Whole serum
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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 (PubMed : 12732622, PubMed : 16492732, PubMed : 19242475, PubMed : 19568430).
See full target information Prnp

Alternative Names

CD230, Prn-p, Prp, Prnp, Major prion protein, PrP, PrP27-30, PrP33-35C

Publications (5)

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

BMC cancer 24:1539 PubMed39695426

2024

Prion protein regulates invasiveness in glioblastoma stem cells.

Applications

Unspecified application

Species

Unspecified reactive species

Mariana B Prado,Bárbara P Coelho,Rebeca P Iglesia,Rodrigo N Alves,Jacqueline M Boccacino,Camila F L Fernandes,Maria Isabel Melo-Escobar,Shamini Ayyadhury,Mario C Cruz,Tiago G Santos,Flávio H Beraldo,Jue Fan,Frederico M Ferreira,Helder I Nakaya,Marco A M Prado,Vania F Prado,Martin L Duennwald,Marilene H Lopes

Cell stress & chaperones 26:443-452 PubMed33547632

2021

Functional genomics screen identifies proteostasis targets that modulate prion protein (PrP) stability.

Applications

Unspecified application

Species

Unspecified reactive species

Jennifer Abrams,Taylor Arhar,Sue Ann Mok,Isabelle R Taylor,Martin Kampmann,Jason E Gestwicki

Molecular biology of the cell 26:3313-28 PubMed26224313

2015

The cellular prion protein PrPc is a partner of the Wnt pathway in intestinal epithelial cells.

Applications

IF

Species

Unspecified reactive species

Laura S Besnier,Philippe Cardot,Barbara Da Rocha,Anthony Simon,Damarys Loew,Christophe Klein,Béatrice Riveau,Michel Lacasa,Caroline Clair,Monique Rousset,Sophie Thenet

Age (Dordrecht, Netherlands) 36:151-65 PubMed23867972

2013

Presence of a neo-epitope and absence of amyloid beta and tau protein in degenerative hippocampal granules of aged mice.

Applications

Unspecified application

Species

Unspecified reactive species

Gemma Manich,Jaume del Valle,Itsaso Cabezón,Antoni Camins,Mercè Pallàs,Carme Pelegrí,Jordi Vilaplana

PloS one 3:e3000 PubMed18714380

2008

The cellular prion protein PrP(c) is involved in the proliferation of epithelial cells and in the distribution of junction-associated proteins.

Applications

IP, IP

Species

Mouse, Human

Etienne Morel,Stéphane Fouquet,Carine Strup-Perrot,Cathy Pichol Thievend,Cathy Pichol Thievend,Constance Petit,Damarys Loew,Anne-Marie Faussat,Lucile Yvernault,Martine Pinçon-Raymond,Jean Chambaz,Monique Rousset,Sophie Thenet,Caroline Clair
View all publications

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