Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.
Human prion protein (PrP), also known as PRNP, is a ubiquitously expressed GPI-anchored cell surface glycoprotein associating with lipid raft components and functioning as a signaling molecule. PrP plays a role in apoptosis in a cell context-dependent manner, is involved in proliferation of epithelial cells and in distribution of junction-associated proteins in human enterocytes. Conversion of this normal cellular prion protein (PrPc) into an abnormal conformer (PrPSc) is the crucial step associated with triggering the pathogenesis of the prion neurodegenerative disorders, such as the Creutzfeld-Jakob disease (CJD). Whereas PrPc is rich in alpha-helices, the PrPSc form has higher content of beta-sheets and is resistant to proteinase K.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Alternative prion protein; AltPrP; ASCR; BSE; CD230; CD230 antigen; Major prion protein; MGC26679; prion protein, PrP; prion protein, structural; prion-related protein; PrP; PrP27-30; PrP33-35C; TSE
AA960666; AI325101; ALTPRP; ASCR; CD230; CJD; GSS; KURU; p27-30; PRIP; Prn; Prn-i; Prn-p; PRNP; PRP; PrP27-30; PrP33-35C; PrP