Human PRNP (Major prion protein) ELISA Kit

Este producto es parte de PRNP - prion protein (Kanno blood group)
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935106861
info@markelab.com
name
Human PRNP (Major prion protein) ELISA Kit
category
ELISA Kits
provider
FineTest
reference
EH2469
tested applications
ELISA

Documents del producto

Instrucciones
Descargar
Data sheet

Product specifications

Category
ELISA Kits
Reactivity
Human
Detection Method
Colorimetric
Assay Data
4 hours
Assay Type
Sandwich ELISA, Double Antibody
Test Range
0.313-20ng/ml
Sensitivity
0.188ng/ml
Size 1
96T
Tested Applications
ELISA
Sample Type
Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples
Availability
Shipped within 10-14 working days.
Storage
2-8 °C for 12 months
UniProt ID
P04156
Alias
Creutzfeldt-Jakob disease,CJD,GSS,PrP,ASCR,KURU,PRIP,PrPc,CD230,Alternative prion protein
Background
Elisa kits for PRNP
Status
RUO

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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