Prion Protein (PRNP) Antibody
377€ (100 µg)
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name
Prion Protein (PRNP) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx415316
tested applications
WB, IHC, FCM
Description
Major Prion Protein (CD230) Antibody is a Mouse Monoclonal antibody against Major Prion Protein (CD230).
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Prion Protein (PRNP) |
| Host | Mouse |
| Reactivity | Sheep |
| Recommended Dilution | Validated in IHC-P. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Monoclonal |
| Conjugation | Unconjugated |
| Isotype | IgG2a |
| Purification | Purified |
| Size 1 | 100 µg |
| Form | Liquid |
| Tested Applications | WB, IHC, FCM |
| Buffer | PBS. Contains sodium azide. |
| Availability | Shipped within 3-7 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P10279, P23907 |
| Alias | Creutzfeldt-Jakob disease,CJD,GSS,PrP,ASCR,KURU,PRIP,PrPc,CD230,Alternative prion protein |
| Background | Antibody anti-PRNP |
| Status | RUO |
| Note | Concentration: 1.0 mg/ml - |
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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