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AB2882

Anti-Prion protein PrP antibody [7B6 / D2]

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(1 Publication)

Mouse Monoclonal Prion protein PrP antibody. Suitable for WB and reacts with Cow samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Cow PRNP.

View Alternative Names

CD230, PRP, PRNP, Major prion protein, PrP, Major scrapie-associated fibril protein 1

1 Images
Western blot - Anti-Prion protein PrP antibody [7B6 / D2] (AB2882)
  • WB

Unknown

Western blot - Anti-Prion protein PrP antibody [7B6 / D2] (AB2882)

Native bovine prion protein from brain (M. oblonggata) was seperated by SDS-PAGE under reducing conditions and blotted on nitrocellulose membrange. NC membrange was incubated by 1 µg/ml of ab2882. Bound antibody was detected using horseradish peroxidase conjugated goat anti-mouse IgG/M antibody and H2O2/TMB substrate solution. ab2882 reacted specifically with bands of PrPc.

All lanes:

Western blot - Anti-Prion protein PrP antibody [7B6 / D2] (ab2882)

Predicted band size: 28 kDa

false

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

7B6 / D2

Isotype

IgG1

Light chain type

kappa

Carrier free

No

Reacts with

Cow

Applications

WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Cow PRNP. The exact immunogen used to generate this antibody is proprietary information.

P10279

Epitope

This antibody has been shown to specifically bind between amino acids 123 - 136 and 140 - 160 of bovine prion protein, determined by pepscan (Osman, A.A. et al.).

Specificity

This antibody detects: Human recombinant prion protein. Bovine recombinant, native and PrPres proteinase K treated prion protein.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Cow": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
Preservative: 0.02% Sodium azide
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 (1)

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

Analytical chemistry 80:2141-8 PubMed18271602

2008

Prion protein detection using nanomechanical resonator arrays and secondary mass labeling.

Applications

ELISA

Species

Unspecified reactive species

Madhukar Varshney,Philip S Waggoner,Christine P Tan,Keith Aubin,Richard A Montagna,Harold G Craighead
View all publications

Product promise

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