Mouse Prion Protein (PRNP) Protein
234€ (10 µg)
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name
Mouse Prion Protein (PRNP) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx068666
tested applications
WB, SDS-PAGE
Description
Mouse Prion Protein (PRNP) is a recombinant Mouse protein produced in a Prokaryotic expression system (E. coli).
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Prion Protein (PRNP) |
| Host | E. coli |
| Origin | Mouse |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 26.6 kDa Observed MW (SDS-PAGE): 27 kDa Concentration: Prior to lyophilization: 70 µg/ml Sequence Fragment: Lys23-Ser230 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 97% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized Reconstitute in ddH2O to a concentration of 0.1-0.7 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 0.01% Sarcosyl, 5% Trehalose. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P04925 |
| Alias | Creutzfeldt-Jakob disease,CJD,GSS,PrP,ASCR,KURU,PRIP,PrPc,CD230,Alternative prion protein |
| Background | Protein PRNP |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
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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