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AB753

Recombinant Cow Prion protein PrP

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.

別名を表示する

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

精製度

>95% SDS-PAGE

発現系

Escherichia coli

タグ

His tag C-Terminus

アプリケーション

ELISA, SDS-PAGE

applications

生物活性

No

アクセッション番号

P10279

アニマルフリー

No

キャリアフリー

No

種

Cow

バッファー組成

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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配列情報

[{"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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出荷温度及び保存条件

出荷温度
Blue Ice
短期保存温度
-20°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False
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補足情報

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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製品の性状

製品の状態

Liquid

補足情報

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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一般的な情報

機能

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).

配列の類似性

Belongs to the prion family.

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製品プロトコール

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ターゲットの情報

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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文献 (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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組合せ製品

Primary Antibodies

AB52604

Anti-Prion protein PrP antibody [EP1802Y]

BOND RX™ Validated|RabMAb|Recombinant

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Prion protein PrP antibody [EP1802Y] (AB52604)

  • 4
  • 2
Primary Antibodies

AB214337

Anti-Flavivirus NS1 antibody [D/2/D6/B7]

Immunocytochemistry/ Immunofluorescence - Anti-Flavivirus NS1 antibody [D/2/D6/B7] (AB214337)

  • 0
  • 0
Secondary Antibodies

AB150077

Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

Immunocytochemistry/ Immunofluorescence - Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (AB150077)

  • 5
  • 20
Primary Antibodies

AB138210

Anti-ZDHHC7 antibody

Western blot - Anti-ZDHHC7 antibody (AB138210)

  • 1
  • 1

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