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AB276456

Recombinant Human Prion protein PrP (Fc Chimera)

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Recombinant Human Prion protein PrP (Fc Chimera) is a Human Fragment protein, in the 1 to 229 aa range, expressed in HEK 293 cells, with >90%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.

View Alternative Names

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

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SDS-PAGE - Recombinant Human Prion protein PrP (Fc Chimera) (AB276456)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Prion protein PrP (Fc Chimera) (AB276456)

SDS-PAGE analysis of ab276456

Key facts

Purity

>90% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

Fc tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P04156

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS

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>" } } }
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Sequence info

[{"sequence":"MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRG","proteinLength":"Fragment","predictedMolecularWeight":"49.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":229,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P04156","tags":[{"tag":"Fc","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Ambient - Can Ship with 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

Lyophilized

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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.

Post-translational modifications

The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.

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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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Complementary Products

Primary Antibodies

AB52604

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Primary Antibodies

AB214337

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

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Secondary Antibodies

AB150077

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

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

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Primary Antibodies

AB138210

Anti-ZDHHC7 antibody

Western blot - Anti-ZDHHC7 antibody (AB138210)

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