Recombinant Human Prion protein PrP (Fc Chimera) is a Human Fragment protein, in the 1 to 229 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Key facts
- Purity
- >90% SDS-PAGE
- Endotoxin level
- < 1 EU/µg
- Expression system
- HEK 293 cells
- Tags
- Fc tag C-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
M A N L G C W M L V L F V A T W S D L G L C K K R P K P G G W N T G G S R Y P G Q G S P G G N R Y P P Q G G G G W G Q P H G G G W G Q P H G G G W G Q P H G G G W G Q P H G G G W G Q G G G T H S Q W N K P S K P K T N M K H M A G A A A A G A V V G G L G G Y M L G S A M S R P I I H F G S D Y E D R Y Y R E N M H R Y P N Q V Y Y R P M D E Y S N Q N N F V H D C V N I T I K Q H T V T T T T K G E N F T E T D V K M M E R V V E Q M C I T Q Y E R E S Q A Y Y Q R G
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
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).
Alternative names
CD230, ALTPRP, PRIP, PRP, PRNP, Major prion protein, PrP, ASCR, PrP27-30, PrP33-35C
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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, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
Key facts
- Purity
- >90% SDS-PAGE
- Endotoxin level
- < 1 EU/µg
- Expression system
- HEK 293 cells
- Tags
- Fc tag C-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- P04156-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 7.4
Constituents: 100% PBS
Sequence info
Amino acid sequence
- M A N L G C W M L V L F V A T W S D L G L C K K R P K P G G W N T G G S R Y P G Q G S P G G N R Y P P Q G G G G W G Q P H G G G W G Q P H G G G W G Q P H G G G W G Q P H G G G W G Q G G G T H S Q W N K P S K P K T N M K H M A G A A A A G A V V G G L G G Y M L G S A M S R P I I H F G S D Y E D R Y Y R E N M H R Y P N Q V Y Y R P M D E Y S N Q N N F V H D C V N I T I K Q H T V T T T T K G E N F T E T D V K M M E R V V E Q M C I T Q Y E R E S Q A Y Y Q R G
- Accession
- P04156
- Protein length
- Fragment
- Predicted molecular weight
- 49.7 kDa
- Amino acids
- 1 to 229
- Nature
- Recombinant
- Tags
- Fc tag C-Terminus
Specifications
- Form
- Lyophilized
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.
Storage
- 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
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
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.
- Associated diseases and disorders
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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SDS-PAGE - Recombinant Human Prion protein PrP (Fc Chimera) (ab276456)
SDS-PAGE analysis of ab276456
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