Human PRNP (Major prion protein) ELISA Kit

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name
Human PRNP (Major prion protein) ELISA Kit
category
ELISA Kits
provider
FineTest
reference
EH2469
tested applications
ELISA
Documents del producto
Instrucciones
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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