Human PRNP blocking peptide (CDBP2383)

Synthetic Human PRNP blocking peptide for Apuri, BL, ELISA

Product Overview
Blocking/Immunizing peptide for anti-Prion Protein (143-153) antibody
Prion Protein (143-153)
Species Reactivity
Human, Mouse, Dog, Rat
Application Notes
For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not for human or animal consumption.
Lyophilized powder
100 μg
Shipped at ambient temperature, store at -20°C.
UniProt ID
Antigen Description
The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. An overlapping open reading frame has been found for this gene that encodes a smaller, structurally unrelated protein, AltPrp. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2012]
ATP-dependent protein binding; chaperone binding; copper ion binding; copper ion binding; identical protein binding; microtubule binding; protein binding; tubulin binding;
PRNP; prion protein; CJD; GSS; PrP; ASCR; KURU; PRIP; PrPc; CD230; AltPrP; p27-30; PrP27-30; PrP33-35C; major prion protein; CD230 antigen; prion-related protein;


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Investigation of the prion protein gene (PRNP) polymorphisms in Anatolian, Murrah, and crossbred water buffaloes (Bubalus bubalis)


Authors: Yaman, Yalcin; Karadag, Orhan; Un, Cemal

Bovine spongiform encephalopathy (BSE) of the cattle is the outstanding disease among other transmissible spongiform encephalopathy (TSEs). It can be transmitted from the cattle to a human and causes a new variant of the Creutzfeldt-Jakob disease (CJD). It is known that prion protein coding gene (PRNP) plays a major role in the TSE susceptibility or resistance in some species. Recent researches demonstrated that the insertion (in) and deletion (del) polymorphisms within promoter and intron 1 region of the PRNP related to BSE susceptibility in cattle. In contrast to cattle, BSE has never been reported in water buffalo; hence, PRNP polymorphisms may be an explanation for buffalo resistance to BSE. The aim of this study was to evaluate allele, genotype, and haplotype frequencies of the PRNP promoter and intron 1 insertion/deletion (indel) polymorphism in healthy Anatolian, Murrah, and Murrah x Anatolian crossbred buffaloes. According to our findings, there were no deletion alleles at two mentioned loci. All studied buffaloes were monomorphic and have carried in/in haplotypes which are considered as the most resistant genotype to BSE.

Early pathology in sleep studies of patients with familial Creutzfeldt-Jakob disease


Authors: Givaty, Gili; Maggio, Nicola; Cohen, Oren S.; Blatt, Ilan; Chapman, Joab

In this study, we aimed to assess sleep function in patients with recent-onset familial Creutzfeldt-Jakob disease (fCJD). The largest cluster of fCJD patients is found in Jews of Libyan origin, linked to the prion protein gene (PRNP) E200K mutation. The high index of suspicion in these patients often leads to early diagnosis, with complaints of insomnia being a very common presenting symptom of the disease. The study included 10 fCJD patients diagnosed by clinical manifestations, magnetic resonance imaging (MRI) scan of the brain, elevated tau protein in the cerebrospinal fluid (CSF) and positive PRNP E200K mutation. Standard polysomnography was performed after a brief interview confirming the presence of sleep disturbances. All patients showed a pathological sleep pattern according to all scoring evaluation settings. The sleep stages were characterized by (i) disappearance of sleep spindles; (ii) outbursts of periodic sharp waves and shallowing of sleep consisting in increased Stage 2 and wake periods during the night, as well as decrease of slow-wave sleep and rapid eye movement (REM) sleep. Recordings of respiratory functions reported irregular breathing with central and obstructive apnea and hypopnea. The typical hypotonia occurring during the night and atonia during REM sleep were replaced by hyperactive sleep consisting of multiple jerks, movements and parasomnia (mainly talking) throughout the night. In conclusion, we report unique pathological sleep patterns in early fCJD associated with the E200K mutation. Specific respiratory disturbances and lack of atonia could possibly serve as new, early diagnostic tools in the disease.

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