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The protein encoded by PRNP is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. Additionally we are shipping PRNP Proteins (54) and PRNP Kits (18) and many more products for this protein.
Showing 10 out of 173 products:
Cow (Bovine) Monoclonal PRNP Primary Antibody for EIA, IHC (fro) - ABIN264042
Kascsak, Rubenstein, Merz, Tonna-DeMasi, Fersko, Carp, Wisniewski, Diringer: Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. in Journal of virology 1987
Show all 4 references for ABIN264042
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 references for ABIN180947
Cow (Bovine) Polyclonal PRNP Primary Antibody for EIA, IHC (p) - ABIN319008
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 references for ABIN319008
Human Polyclonal PRNP Primary Antibody for ELISA, WB - ABIN185661
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 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
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) is highly enriched on exosomes from SH-SY5Y cells and that exosomes bind amyloid beta via PrP(C).
The results suggest a role of PrP(C) in proteostasis, dysfunctions of which may be involved in the pathogenesis of neurodegenerative diseases such as TSE and Alzheimer's Disease.
Effects such as the stabilization of the native alpha-fold, dictating the efficiency of the alpha-cleavage, attenuating the fibrillation propensity and yielding the most benign amyloids suggest that the charge design ensures PrPC functions.
Genetic coupling between Prnp and glutamate receptor 5 is responsible for synapse loss in Alzheimer's disease transgenic mouse model.
these results show that multiple gene irregularity in BxPC-3 cells is responsible for the formation of pro-PrP (show C4BPA Antibodies), and binding of pro-PrP (show C4BPA Antibodies) to filamin A (show FLNA Antibodies) contributes to enhanced tumor cell motility.
Overall, these results suggest that PrP(c) contribute the breast cancer invasion and migration via MMP-9 (show MMP9 Antibodies).
We propose that PrP (show C4BPA Antibodies) modulates beta1 integrin adhesion and migration of monocytes through RhoA (show RHOA Antibodies)-induced actin remodeling mediated by cofilin (show CFL1 Antibodies), and through the regulation of ERM (show ETV5 Antibodies)-mediated membrane-cytoskeleton linkage.
We conclude that the V180I mutation in prion protein gene produces a late-developing and slow-developing, less severe form of Creutzfeldt-Jakob disease
The decrease in FK-derived PrPSc levels was mediated, at least in part, by the phosphatidylinositol 3-kinase/MEK (show MAP2K1 Antibodies) signalling pathway.
PRNP polymorphisms at codons 129 and 219 affect the prion disease susceptibility depending on the prion strain; review aims to summarize recent advances in our knowledge about the influence of the PRNP polymorphisms on the prion disease susceptibility
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).
Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster = mouse < rabbit < bovine prion protein
PrP(C) promotes myelin homeostasis through flexible tail-mediated Gpr126 (show GPR126 Antibodies) agonism
Thus, we conclude that 'rigidity' in the b2-a2 loop region of the normal conformer of PrP has less effect on misfolding than other sequence-related effects in this region.
The prion protein is required to form the splenic white pulp structure and for development of normal levels of CD4 (show CD4 Antibodies) and helper-inducer T cells.
PrP(C) is highly enriched on exosomes from N2a cells. Exosomes bind amyloid beta via PrP(C).
Data suggest that expression of shadoo (show SPRN Antibodies) in neuron or hepatocyte cell lines induces same toxic phenotype of drug hypersensitivity as prion protein/PrP(-central region); this effect is counteracted by co-expression of PrP-wild-type.
aged Prnp(ZH3/ZH3) mice developed a chronic demyelinating peripheral neuropathy, confirming the crucial involvement of PrP(C) in peripheral myelin maintenance.
Neuroprotective effect of cellular prion protein (PrPC) is related with activation of alpha7 nicotinic acetylcholine receptor (alpha7nAchR)-mediated autophagy flux.
Kinetics of prp folding and unfolding shows an equilibrium A-state corresponding to a late folding intermediate, which is a monomeric precursor of aggregates suggesting the A-state is a branching point between the folding and aggregation pathways.
the pathogenic mutation T182A causes a drastic reduction in the apparent cooperativity and enthalpy of unfolding of the mouse prion protein under misfolding-prone conditions by converting the protein into a molten globule-like conformation
These findings show that the sialic acid moiety of the glycosylphosphatidylinositol attached to PrP(C) modifies local membrane microenvironments that are important in PrP-mediated cell signaling and PrP(Sc) formation.
single nucleotide polymorphisms (G11A, G615C, G684A, T726G) in the open reading frame of the porcine PRNP gene were found
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
The comparison of the structural stability of prion proteins from the three species rabbit, human and mouse showed that the human and mouse prion protein structures were not affected by the removing the two salt bridges
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.
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.
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 protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)
, prion protein PrP
, Major prion protein
, CARD-containing MAGUK protein 2
, bcl10-interacting maguk protein 2
, card-maguk protein 2
, carma 2
, caspase recruitment domain-containing protein 14
, CD230 antigen
, prion-related protein
, major scrapie-associated fibril protein 1
, prion protein precursor PrP
, prion protein variant a
, prion protein variant b
, prion protein, PrP
, prion protein, structural
, 65-21 protein
, acetylcholine receptor-inducing activity
, major prion protein homolog
, prion-like protein
, glutathione synthetase
, major prion protein preproprotein
, infectious amyloid
, PrP 27-30