Anticorps Recombinant de lapin anti-Prion protein PrP/CD230

Prion protein PrP/CD230 Recombinant Antibody for WB, ELISA

Hôte / Isotype

Lapin / IgG

Réactivité testée

Humain

Applications

WB, ELISA

Conjugaison

Non conjugué

CloneNo.

243104D11

N° de cat : 85611-4-RR

Synonymes

Prion protein PrP, PRNP, PrP, Alternative prion protein, AltPrP

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Galerie de données de validation

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  WB analysis of fetal human brain using 85611-4-RR

  fetal human brain tissue was subjected to SDS PAGE followed by western blot with 85611-4-RR (PRNP antibody) at dilution of 1:10000 incubated at room temperature for 1.5 hours.

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Applications testées

• Résultats positifs en WB: tissu cérébral humain fœtal,

Dilution recommandée

• Western Blot (WB): WB : 1:5000-1:50000

It is recommended that this reagent should be titrated in each testing system to obtain optimal results.

Sample-dependent, check data in validation data gallery

Informations sur le produit

85611-4-RR cible Prion protein PrP/CD230 dans les applications de WB, ELISA et montre une réactivité avec des échantillons Humain

• Réactivité: Humain
• Hôte / Isotype: Lapin / IgG
• Clonalité: Recombinant
• Type: Anticorps
• Immunogène: Prion protein PrP/CD230 Protéine recombinante Eg3359
• Nom complet: prion protein
• Poids moléculaire observé: 20-35 kDa
• Numéro d’acquisition GenBank: BC012844
• Symbole du gène: PrP
• Identification du gène (NCBI): 5621
• Conjugaison: Non conjugué
• Forme: Liquide
• Méthode de purification: Purification par protéine A
• Tampon de stockage: PBS with 0.02% sodium azide and 50% glycerol
• Conditions de stockage: Stocker à -20°C. Stable pendant un an après l'expédition. L'aliquotage n'est pas nécessaire pour le stockage à -20^oC Les 20ul contiennent 0,1% de BSA.

Informations générales

Prion protein (PRNP) is a ubiquitous membrane glycoprotein whose abnormal self-replicating, misfolded form is widely believed to cause several central nervous system disorders, collectively known as Transmissible Spongiform Encephalopathies (TSE). Prion diseases are TSEs, attributed to conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer that accumulates in the brain. The two isoforms, PrPC and PrPS, have the same primary amino acid sequence and only differ in conformation. While PrPC is composed of 42% α-helix and only 3% β-sheet, PrPSc is composed of 30% α-helix and 43% β-sheet. PrPC converts to its pathogenic isoform when the region corresponding to the residues 108-144 fold into β-sheets. PrPC is very soluble in detergents and easily digested by proteases while the PrPSc is insoluble in detergents and resistant to protease digestion. Prion diseases exist in infectious, sporadic, and genetic forms.

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