Mouse Prion Protein (PRNP) Protein

Este producto es parte de PRNP - prion protein (Kanno blood group)
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234€ (10 µg)

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935106861
info@markelab.com
name
Mouse Prion Protein (PRNP) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx068666
tested applications
WB, SDS-PAGE

Description

Mouse Prion Protein (PRNP) is a recombinant Mouse protein produced in a Prokaryotic expression system (E. coli).

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Prion Protein (PRNP)
Host
E. coli
Origin
Mouse
Conjugation
Unconjugated
Observed MW
Molecular Weight: Calculated MW: 26.6 kDa  Observed MW (SDS-PAGE): 27 kDa

Concentration: Prior to lyophilization: 70 µg/ml

Sequence Fragment: Lys23-Ser230

Tag: N-terminal His tag
Expression
Recombinant
Purity
> 97%
Size 1
10 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
500 µg
Form
Lyophilized Reconstitute in ddH2O to a concentration of 0.1-0.7 mg/ml. Do not vortex.
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 0.01% Sarcosyl, 5% Trehalose.
Availability
Shipped within 5-7 working days.
Storage
Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
P04925
Alias
Creutzfeldt-Jakob disease,CJD,GSS,PrP,ASCR,KURU,PRIP,PrPc,CD230,Alternative prion protein
Background
Protein PRNP
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

The PRNP gene, encoding the prion protein (PrP), plays a critical role in both neurobiology and disease. This gene is located on chromosome 20 in humans and encodes the cellular prion protein, PrP^C. Prion proteins are unique in their ability to exist in multiple conformations, including a pathological form, PrP^Sc, associated with prion diseases. Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are neurodegenerative disorders marked by rapidly progressive neuronal loss and a spongiform appearance in brain tissue. TSEs include diseases such as Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Sträussler-Scheinker syndrome (GSS), and kuru. The prion protein (PrP) is primarily expressed in the central nervous system (CNS), especially in neurons, but it is also found in other tissues. While the physiological function of PrP^C remains partially understood, it is thought to be involved in cellular processes like cell signaling, protection against oxidative stress, and synaptic function. Its pathological form, PrP^Sc, is formed by a misfolded conformation of PrP^C that becomes self-propagating, causing other normal PrP^C molecules to misfold. This cascade leads to the accumulation of toxic aggregates and extensive neuronal damage, a hallmark of prion diseases.

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