Prion Protein (PRNP) Antibody

Este producto es parte de PRNP - prion protein (Kanno blood group)
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273€ (100 µl)

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935106861
info@markelab.com
name
Prion Protein (PRNP) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx101114
tested applications
WB, IHC, IF/ICC

Description

Polyclonal Antibody to Prion Protein (PRNP).

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Primary Antibodies
Immunogen Target
Prion Protein (PRNP)
Host
Rabbit
Reactivity
Mouse
Recommended Dilution
WB: 0.01-2 µg/ml, IHC: 5-20 µg/ml, IF/ICC: 5-20 µg/ml. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Purification
Purified by antigen-specific affinity chromatography, followed by Protein A affinity chromatography.
Size 1
100 µl
Size 2
200 µl
Size 3
1 ml
Form
Liquid
Tested Applications
WB, IHC, IF/ICC
Buffer
0.01 M PBS, pH 7.4, containing 0.05% Proclin-300, 50% glycerol.
Availability
Shipped within 5-7 working days.
Storage
Aliquot and store at -20°C. 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
Antibody anti-PRNP
Status
RUO

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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