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AB753

Recombinant Cow Prion protein PrP

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(3 Publications)

Recombinant Cow Prion protein PrP is a Cow Full Length protein, in the 25 to 244 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, ELISA.

View Alternative Names

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

1 Images
SDS-PAGE - Recombinant Cow Prion protein PrP (AB753)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Cow Prion protein PrP (AB753)

SDS-PAGE of 2 μg PrPc (lane 1).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

SDS-PAGE, ELISA

applications

Biologically active

No

Accession

P10279

Animal free

No

Carrier free

No

Species

Cow

Storage buffer

pH: 4 Constituents: 0.082% Sodium acetate

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESQAYYQRGASHHHHHH","proteinLength":"Full Length","predictedMolecularWeight":"25 kDa","actualMolecularWeight":null,"aminoAcidEnd":244,"aminoAcidStart":25,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P10279","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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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.
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Specifications

Form

Liquid

Additional notes

Expressed in E.coli BL21, solubilized from inclusion bodies in 6 M guanidine-HCl, and purified by Ni(II)-nitriloacetate agarose chromatography, followed by reversed-phase HPLC (C4 column).The rPrPc appears as a single protein band of about 27 kDa in SDS-PAGE (>95% of total protein).

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General info

Function

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).

Sequence similarities

Belongs to the prion family.

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Product protocols

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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
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Publications (3)

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

Journal of animal science 86:3069-78 PubMed18599661

2008

Copper deficiency in the young bovine results in dramatic decreases in brain copper concentration but does not alter brain prion protein biology.

Applications

WB

Species

Unspecified reactive species

L R Legleiter,J W Spears,H C Liu

Journal of animal science 85:2895-903 PubMed17644786

2007

Exposure to low dietary copper or low copper coupled with high dietary manganese for one year does not alter brain prion protein characteristics in the mature cow.

Applications

WB

Species

Unspecified reactive species

L R Legleiter,H C Liu,K E Lloyd,S L Hansen,R S Fry,J W Spears

Biochemical and biophysical research communications 352:884-8 PubMed17157816

2006

Decreased brain copper due to copper deficiency has no effect on bovine prion proteins.

Applications

Unspecified application

Species

Unspecified reactive species

Leon R Legleiter,Jason K Ahola,Terry E Engle,Jerry W Spears
View all publications
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