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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.

대체 명칭 보기

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

1 이미지
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

주요 정보

Purity

>90% SDS-PAGE

Endotoxin 레벨

< 1 EU/µg

발현 시스템

HEK 293 cells

Tags

Fc tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Animal free

No

Carrier free

No

Species

Human

보관 버퍼

pH: 7.4 Constituents: PBS

storage-buffer

Reactivity 정보

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

서열 정보

[{"linker":null,"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"}]}]

특성 및 보관 정보

제형
Lyophilized
배송 시 보관 조건
Ambient - Can Ship with Ice
적절한 단기 보관 조건
-20°C
적절한 장기 보관 조건
-20°C
분주 정보
Upon delivery aliquot
보관 정보
Avoid freeze / thaw cycle
False

추가 정보

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.

일반 정보

기능

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).

서열 유사성

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.

제품 프로토콜

타겟 정보

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

Product promise

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