Major Prion Protein (PRNP) Antibody

Este producto es parte de PRNP - prion protein (Kanno blood group)
Major Prion Protein (PRNP) Antibody
455€ (0.1 mg)

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Name
Major Prion Protein (PRNP) Antibody
Category
Primary Antibodies
Provider
Abbexa
Reference
abx140599
Tested Applications
WB

Description

Major Prion Protein (PRNP) Antibody is a Mouse Monoclonal Antibody against Major Prion Protein (PRNP).

Documentos del producto

Instrucciones
Data sheet
Descargar

Especificaciones del producto

Category
Primary Antibodies
Immunogen Target
Target: Major Prion Protein (PRNP)
Immunogen: Recombinant human prion protein.
Host
Mouse
Reactivity
Human
Assay Type
Concentration: 1 mg/ml
Recommended Dilution
Optimal dilutions/concentrations should be determined by the end user.
Clonality
Monoclonal
Conjugation
Unconjugated
Isotype
IgG2a
Clone ID
J790
Purification
Purified by Protein A affinity chromatography.
Size 1
0.1 mg
Tested Applications
WB
Buffer
PBS solution with 15 mM sodium azide.
Availability
Shipped within 5-12 working days.
Storage
Store at 2-8°C. Do not freeze.
Dry Ice
No
UniProt ID
P04156
Gene ID
5621
OMIM
176640
Alias
Creutzfeldt-Jakob disease,CJD,GSS,PrP,ASCR,KURU,PRIP,PrPc,CD230,Alternative prion protein
Background
Antibody anti-PRNP
Status
RUO
Note
THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.

Background

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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