Human Prion Protein (PRNP) Protein

Este producto es parte de PRNP - prion protein (Kanno blood group)
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455€ (50 µg)

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935106861
info@markelab.com
name
Human Prion Protein (PRNP) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx655889
tested applications
WB, SDS-PAGE

Description

Human Prion Protein (PRNP) is a recombinant Human protein produced in 293F cells using Eukaryotic expression.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Prion Protein (PRNP)
Host
293F cell
Origin
Human
Conjugation
Unconjugated
Observed MW
Molecular Weight: Calculated MW: 24.3 kDa  Observed MW (SDS-PAGE): 25 kDa
Concentration: Prior to lyophilization: 150 µg/ml
Sequence Fragment: Lys23-Ser230
Tag: N-terminal His tag
Expression
Recombinant
Purity
> 95%
Size 1
50 µg
Size 2
100 µg
Size 3
200 µg
Size 4
500 µg
Size 5
1 mg
Form
Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in 20 mM Tris, 150 mM NaCl, pH 8.0. If a higher concentration is required, the product can be reconstituted directly in 20 mM Tris, 150 mM NaCl, pH 8.0, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 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
P04156
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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