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anti-Human PRNP Antikörper:
anti-Rat (Rattus) PRNP Antikörper:
anti-Mouse (Murine) PRNP Antikörper:
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Sheep (Ovine) Monoclonal PRNP Primary Antibody für IHC (p), ELISA - ABIN2479379
Leonard: Safety of amoxapine. in Lancet (London, England) 1989
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Sheep (Ovine) Monoclonal PRNP Primary Antibody für 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
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Human Polyclonal PRNP Primary Antibody für 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
Sheep (Ovine) Monoclonal PRNP Primary Antibody für IHC (p), IHC - ABIN254225
Cook, Bingham, Besier, Bayley, Hawes, Shearer, Yamada, Bergfeld, Williams, Middleton: Atypical scrapie in Australia. in Australian veterinary journal 2016
Human Monoclonal PRNP Primary Antibody für WB - ABIN349704
Yang, Chen, Pan, Kou, Xu: Glycosylation modification of human prion protein provokes apoptosis in HeLa cells in vitro. in BMB reports 2009
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Cow (Bovine) Polyclonal PRNP Primary Antibody für 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
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Human Monoclonal PRNP Primary Antibody für 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 für 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
Here, we provide an overview of the increasingly multifaceted picture of prion protein proteolysis and shed light on physiological and pathological roles associated with these cleavages.
the coordination bonds between the Methionine-Lysine-Histidine (Ac-MKH-NHMe) tripeptide model associated with the fifth metal binding site, which triggers the beta-sheet formation of human prion protein and the divalent metal cations such as Mn(2+), Cu(2+) and Zn(2+) were studied.
Importantly, flies expressing human PrP (zeige C4BPA Antikörper) showing a robust eye phenotype will allow performing genetic screens to uncover novel mechanisms mediating PrP (zeige C4BPA Antikörper) neurotoxicity.
Our results indicated, we found that PrP (zeige C4BPA Antikörper) 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 (zeige STIP1 Antikörper)-PrP(C) engagement or the decrease of PrP(C) and HOP (zeige STIP1 Antikörper) expression may represent a potential therapeutic intervention in glioblastoma.
a strong overexpression of PrP(C) is observed in human Merlin (zeige NF2 Antikörper)-deficient mesothelioma cell line TRA and in human Merlin (zeige NF2 Antikörper)-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 (zeige TPO Antikörper). No other variants in the PRNP gene were associated with increased risk for MSA (zeige TPO Antikörper)
Transgenic Creutzfeldt-Jakob disease (CJD) mice, expressing the mouse PrP (zeige C4BPA Antikörper) (moPrP) homolog of human PrP (zeige C4BPA Antikörper) D178N/V129 (moPrP D177N/V128), closely reproduce essential features of CJD. The mutant PrPs (zeige MSMB Antikörper) 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 (zeige JUP Antikörper), one of its desmosomal partners, beta-catenin (zeige CTNNB1 Antikörper) and TCF7L2 (zeige TCF7L2 Antikörper), the main effectors of the canonical Wnt (zeige WNT2 Antikörper) pathway, and YAP (zeige YAP1 Antikörper), one effector of the Hippo pathway.
Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND (zeige PRND Antikörper)) 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 (zeige SPRN Antikörper)) 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 (zeige SP1 Antikörper) and RP58 (zeige ZNF238 Antikörper) 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 (zeige KCTD1 Antikörper) 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 (zeige ZDHHC2 Antikörper)-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) takes part in the cell apparatus controlling Ca(2 (zeige CA2 Antikörper)+) homeostasis, and that PrP(C) is involved in protecting neurons from toxic Ca(2 (zeige CA2 Antikörper)+) overloads.
both gain-of-function and loss-of-function pathogenic mechanisms may be associated with N-terminal domains and may therefore contribute to neurotoxicity in prion disease.
PrP(C) controls the expression of the epidermal growth factor receptor (EGFR (zeige EGFR Antikörper)) downstream from Notch (zeige NOTCH1 Antikörper).
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 (zeige MSMB Antikörper) 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 (zeige APP Antikörper) oligomers and fibril ends and that this interaction could contribute to the neurotoxic effect of Abeta (zeige APP Antikörper) 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 (zeige ARHGEF16 Antikörper) cells from proteasome inhibition-induced cytotoxicity.
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