Prion Protein (PRNP) Antibody Pair

Product specifications

Antibody Pairs

Prion Protein (PRNP)

Human

Detection Antibody Biotinilated

Sandwich

Dilute the Capture Antibody 125-fold with Coating Buffer.  Dilute the Biotin-Conjugated Detection Antibody 200-fold with Detection Antibody Diluent.  Optimal dilutions/concentrations should be determined by the end user.

5 × 96 tests

10 × 96 tests

Standard: Lyophilized--Liquid (Capture Antibody and Detection Antibody)

Reconstitute the standard with Standard Diluent. The volume, and therefore standard concentration, should be determined by the end user.

ELISA

The Capture and Detection Antibody both contain 0.1% sodium azide.

Please enquire.

Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.

No

Creutzfeldt-Jakob disease,CJD,GSS,PrP,ASCR,KURU,PRIP,PrPc,CD230,Alternative prion protein

Antibody Pair for PRNP

RUO

This antibody pair contains ( 5 x 96 det):    Detection:  50 µg  Capture:  200 µg  Standard:  2 µg

This product is for research use only.

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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