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Sheep (Ovine) Monoclonal PRNP Primary Antibody for IHC (p), ELISA - ABIN2479379
Leonard: Safety of amoxapine. in Lancet (London, England) 1989
Show all 4 Pubmed References
Sheep (Ovine) Monoclonal PRNP Primary Antibody for IHC (p), IHC - ABIN254225
Cook, Bingham, Besier, Bayley, Hawes, Shearer, Yamada, Bergfeld, Williams, Middleton: Atypical scrapie in Australia. in Australian veterinary journal 2016
Human Polyclonal PRNP Primary Antibody for ELISA, WB - ABIN251503
Ballerini, Gourdain, Bachy, Blanchard, Levavasseur, Grégoire, Fontes, Aucouturier, Hivroz, Carnaud: Functional implication of cellular prion protein in antigen-driven interactions between T cells and dendritic cells. in Journal of immunology (Baltimore, Md. : 1950) 2006
Human Monoclonal PRNP Primary Antibody for WB - ABIN349704
Yang, Chen, Pan, Kou, Xu: Glycosylation modification of human prion protein provokes apoptosis in HeLa cells in vitro. in BMB reports 2009
Show all 4 Pubmed References
Sheep (Ovine) Monoclonal PRNP Primary Antibody for EIA, IHC (p) - ABIN180947
Andréoletti, Berthon, Marc, Sarradin, Grosclaude, van Keulen, Schelcher, Elsen, Lantier: Early accumulation of PrP(Sc) in gut-associated lymphoid and nervous tissues of susceptible sheep from a Romanov flock with natural scrapie. in The Journal of general virology 2000
Show all 2 Pubmed References
Human Monoclonal PRNP Primary Antibody for ELISA, WB - ABIN2452080
Sakudo, Nakamura, Ikuta, Onodera: Recent developments in prion disease research: diagnostic tools and in vitro cell culture models. in The Journal of veterinary medical science / the Japanese Society of Veterinary Science 2007
Human Monoclonal PRNP Primary Antibody for ELISA, WB - ABIN2452081
Sakudo, Nakamura, Tsuji, Ikuta: GPI-anchorless human prion protein is secreted and glycosylated but lacks superoxide dismutase activity. in International journal of molecular medicine 2008
Cow (Bovine) Polyclonal PRNP Primary Antibody for IHC (p), ELISA - ABIN2479376
Shinagawa, Munekata, Doi, Takahashi, Goto, Sato: Immunoreactivity of a synthetic pentadecapeptide corresponding to the N-terminal region of the scrapie prion protein. in The Journal of general virology 1986
Show all 2 Pubmed References
Our results indicated, we found that PrP (show C4BPA Antibodies) gene had an IRES-dependent translation initiation mechanism and we successfully identified the IRESs inside of the prion protein gene.
the kinetics of prion replication occur in a prion protein codon 129 genotype-dependent manner, reflecting the genotype-dependent susceptibility to clinical variant Creutzfeldt-Jakob disease found in patients.
the modulation of HOP (show STIP1 Antibodies)-PrP(C) engagement or the decrease of PrP(C) and HOP (show STIP1 Antibodies) expression may represent a potential therapeutic intervention in glioblastoma.
a strong overexpression of PrP(C) is observed in human Merlin (show NF2 Antibodies)-deficient mesothelioma cell line TRA and in human Merlin (show NF2 Antibodies)-deficient meningiomas. PrP(C) contributes to increased proliferation, cell-matrix adhesion and survival in schwannoma cells acting via 37/67 kDa non-integrin laminin receptor (LR/37/67 kDa)
Homozygous state of position 129 in the PRNP is not a risk factor for MSA (show TPO Antibodies). No other variants in the PRNP gene were associated with increased risk for MSA (show TPO Antibodies)
Transgenic Creutzfeldt-Jakob disease (CJD) mice, expressing the mouse PrP (show C4BPA Antibodies) (moPrP) homolog of human PrP (show C4BPA Antibodies) D178N/V129 (moPrP D177N/V128), closely reproduce essential features of CJD. The mutant PrPs (show MSMB Antibodies) expressed in these mice are misfolded but unable to self-replicate. They accumulate in different compartments of the neuronal secretory pathway, impairing the membrane delivery of ion channels essential for neuronal function.
Identified are several nuclear PrP(c) partners, which comprise gamma-catenin (show JUP Antibodies), one of its desmosomal partners, beta-catenin (show CTNNB1 Antibodies) and TCF7L2 (show TCF7L2 Antibodies), the main effectors of the canonical Wnt (show WNT2 Antibodies) pathway, and YAP (show YAP1 Antibodies), one effector of the Hippo pathway.
Rare mutation in PRNP leading to an exchange of amino acid from glutamic acid (E) to alanine (A) at codon 196 (E196A) is associated with Creutzfeldt-Jacob disease.
This article discusses a framework for investigating the extended hypothesis that PrPC may be involved in major depression associated with neurodegenerative conditions, with focus on the Transmissible Spongiform Encephalopathies (TSEs, or Prion Diseases) and Alzheimer's Disease (AlzD).
Expert commentary: Computational approaches provide novel insights into prion-like protein functions, their regulation and their role in disease.
Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND (show PRND Antibodies)) Variation in Domestic Cattle
Misfolded structures, with nonnative beta-strands formed in the flexible N-terminal domain of PRNP were found in acidic pH simulations.
Genetic characterization of PRNP promoter indel variations and the polymorphism of open reading frames (ORFs) of PRNP and bovine prion-like Shadoo (SPRN (show SPRN Antibodies)) genes, are reported.
data showed a differential timing of PrPC expression during early bovine development; the cell-specific expression of PrPC in bovine embryos was revealed to included the developing brain and spinal cord, peripheral nervous system, liver, and mesonephros
The results indicate that certain negative feedback response elements are located in the 5' flanking region and intron1 of the PRNP gene, suggesting that regulation by transcription factors such as Sp1 (show SP1 Antibodies) and RP58 (show ZNF238 Antibodies) may contribute to the negative feedback mechanism of PRNP.
allele and haplotype segregation at the polymorphic sites within the promoter (23indel) and intron 1 (12indel) regions of the PRNP
PRNP gene variation in Pakistani cattle and buffaloes.
A significant relation between the investigated PRNP indel polymorphisms (23 and 12 bp indels), and susceptibility of Polish Holstein-Friesian cattle to classical bovine spongiform encephalopathy, is reported.
fibrils formed by the rabbit protein contain less beta-sheet structure and more alpha-helix structure than those formed by the proteins from human and cow
these results identify a novel PrP(C)-interacting protein KCTD1 (show KCTD1 Antibodies) and suggest a new approach to investigating the unidentified physiological cellular function of PrP(C).
single nucleotide polymorphisms (G11A, G615C, G684A, T726G) in the open reading frame of the porcine PRNP gene were found
Data show the presence of PrP(Sc) in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.
PrP(c) is expressed in all digestive regions of the rat, monkey, and cow; PrP(c) expressing cells appeared scattered throughout the epithelium of fundic and pyloric glands as well as in intestinal villi and crypts.
study found 8 amino acid residues in rec (show ZDHHC2 Antibodies)-PrP that are probably involved in its low susceptibility to misfolding into a protease-resistant isoform; 3 of those residues (S107, M108, and I202) appear to have a stronger influence
fibrils formed by the rabbit protein contain less beta-sheet structure and more alpha-helix structure than those formed by the proteins from human and cow; strong inhibition of fibrillization of the rabbit PrP by the crowded physiological environment and the absence of such a protease-resistant fragment for the rabbit protein could be why rabbits are resistant to prion diseases
Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster = mouse < rabbit < bovine prion protein
amyloid and oxidative stress-related disease proteins like prion protein are increased in expression and form localized accumulations in diabetic muscle in this rabbit model of diabetes.
The salt bridge between D177 and R163 greatly contributes to the structural stability of rabbit prion protein.
Results describe a single amino acid exchange within the loop, D167S, between mouse and horse prion protein (PrP) which is unique to the PrP sequences of equine species.
PrP(C) controls the expression of the epidermal growth factor receptor (EGFR (show EGFR Antibodies)) downstream from Notch (show NOTCH1 Antibodies).
the PRNP octapeptide repeat domain was necessary to promote exosome secretion and to impair the formation of the CAV1-dependent ATG12-ATG5 cytoplasmic complex that drives autophagosome formation.
Transgenic Creutzfeldt-Jakob disease (CJD) mice, expressing the mouse PrP (moPrP) homolog of human PrP D178N/V129 (moPrP D177N/V128), closely reproduce essential features of CJD. The mutant PrPs (show MSMB Antibodies) expressed in these mice are misfolded but unable to self-replicate. They accumulate in different compartments of the neuronal secretory pathway, impairing the membrane delivery of ion channels essential for neuronal function.
Association of human and mouse P-tau with amyloid PrPSc did not diminish survival time following prion infection in these mice. By analogy, human P-tau may not affect prion disease progression in humans.
results suggest that PrP(C) recognizes structural features common to both Abeta (show APP Antibodies) oligomers and fibril ends and that this interaction could contribute to the neurotoxic effect of Abeta (show APP Antibodies) aggregates.
a simple purification strategy for single tryptophan, single cysteine-containing mutant variants of the mouse prion protein is presented, with yields comparable to that of the wild type protein.
The study presented here further elucidates our understanding of the soluble oligomeric amyloid-beta-Abetao-binding cellular prion protein (PrP(C)) signaling pathway in a familial form of Alzheimer's disease (AD) by implicating PrP(C) as a potential therapeutic target for AD.
The retention of prion protein in the endoplasmic reticulum prevents neuroblastoma (show ARHGEF16 Antibodies) cells from proteasome inhibition-induced cytotoxicity.
Data, including data from studies using knockout/transgenic mice, suggest that PrPC is involved in development of insulin (show INS Antibodies) resistance and obesity; PrPC knockout mice fed high-fat diet present all the symptoms associated with insulin (show INS Antibodies) resistance (hyperglycemia, hyperinsulinemia, and obesity); transgenic mice overexpressing PrPC fed high-fat diet exhibit normal insulin (show INS Antibodies) sensitivity and reduced weight gain.
PrP aggresomes are cytosolic overflow deposition centers for the endoplasmic reticulum quality control mechanisms.
Findings indicate the molecular mechanisms of prion pathogenesis and strain diversity.
Data indicate that prion protein PrP dimers were funneled into a thermodynamically stable misfolded state along a single pathway containing several intermediates.
Here, we report that the degree of PrP(Sc) protease resistance is highly dependent on the concentration of salt in the solution.
Localization of fully posttranslationally modified Syrian golden hamster glycosylated PrPC is confirmed in the plasma membrane together with the posttranslational glycosylation pattern.
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.
, major prion protein
, prion-related protein
, prion protein, PrP
, prion protein, structural
, major scrapie-associated fibril protein 1
, prion protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)
, prion protein PrP
, prion protein precursor PrP
, prion protein variant a
, prion protein variant b
, 65-21 protein
, acetylcholine receptor-inducing activity
, major prion protein homolog
, prion-like protein
, prion protein
, infectious amyloid
, Major prion protein
, major prion protein preproprotein
, PrP 27-30