You are viewing an incomplete version of our website. Please click to reload the website as full version.

Browse our PRNP Proteins (PRNP)

Full name:
Prion Protein Proteins (PRNP)
On www.antibodies-online.com are 54 Prion Protein (PRNP) Proteins from 9 different suppliers available. Additionally we are shipping PRNP Antibodies (201) and PRNP Kits (22) and many more products for this protein. A total of 285 PRNP products are currently listed.
Synonyms:
AA960666, AI325101, AltPrP, ASCR, BIMP2, CARMA2, CD230, CJD, GSS, KURU, MGC84114, p27-30, prion, PRIP, Prn, Prn-i, Prn-p, PRNP, Prp, prp(c), prP27-30, prP33-35C, PrP, PrPC, PrPSc, PSORS2, PSS1, Sinc, SIP
list all proteins Gene Name GeneID UniProt
PRNP 79092 Q9BXL6
PRNP 19122 P04925
Rat PRNP PRNP 24686 P13852

Show all synonyms

PRNP Proteins (PRNP) by Origin

Select your origin of interest

Top referenced PRNP Proteins

  1. Human PRNP Protein expressed in Escherichia coli (E. coli) - ABIN1098792 : Lee, Westaway, Smit, Wang, Seto, Chen, Acharya, Ankener, Baskin, Cooper, Yao, Prusiner, Hood: Complete genomic sequence and analysis of the prion protein gene region from three mammalian species. in Genome research 1998 (PubMed)
    Show all 2 references for ABIN1098792

  2. Human PRNP Protein expressed in Human Cells - ABIN2005013 : Wang, Tian, Fan, Chen, Lv, Sun, Zhao, Zhang, Wang, Shi, Gao, Chen, Shao, Dong: Polo-like kinase 3 (PLK3) mediates the clearance of the accumulated PrP mutants transiently expressed in cultured cells and pathogenic PrP(Sc) in prion infected cell line via protein interaction. in The international journal of biochemistry & cell biology 2015 (PubMed)

More Proteins for PRNP Interaction Partners

Xenopus laevis Prion Protein (PRNP) interaction partners

Horse (Equine) Prion Protein (PRNP) interaction partners

  1. 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.

Human Prion Protein (PRNP) interaction partners

  1. Active compounds do not alter total or cell-surface levels of PrP(C), and do not bind to recombinant PrP (show C4BPA Proteins) in surface plasmon resonance experiments, although at high concentrations they inhibit PrP (show C4BPA Proteins)(Sc)-seeded conversion of recombinant PrP (show C4BPA Proteins) to a misfolded state in an in vitro reaction (RT-QuIC).

  2. data provided molecular details about the interaction between HuPrP and the NCAM (show NCAM1 Proteins) fibronectin (show FN1 Proteins) domain, and revealed a new role of PrP(C) N terminus as a dynamic and functional element responsible for protein-protein interaction.

  3. This work sheds light on the amyloid core structures underlying prion strains and how I138M, I139M, and S143N affect prion protein aggregation kinetics.

  4. Data suggest second and third helices (H2 and H3) of C-terminal region of prion protein serve as Achilles heels of prion protein stability; separation of B1-H1-B2 and H2-H3 domains seems to play a key role, as well. (H1, H2, H3 denote the 3 alpha-helices; B1, B1 denote the 2 beta-sheets. Studies involved molecular dynamic simulations using nuclear magnetic resonance data obtained for N-terminal and C-terminal domains.)

  5. prion protein-derived cell-penetrating peptide cytotoxicity is modulated by pH but independent of amyloid formation

  6. Psoriasis mutations disrupt CARD14 (show CARD14 Proteins) autoinhibition promoting BCL10 (show BCL10 Proteins)-MALT1 (show MALT1 Proteins)-dependent NF-kappaB (show NFKB1 Proteins) activation

  7. effect of familial Creutzfeld-Jacob (show NELF Proteins) disease prion genes on prion protein conformation and secondary structure

  8. The two cases reported here of sporadic Creutzfeldt-Jakob disease belonged to the same family and carried the most common point mutation of the PRNP gene observed in Italy.

  9. The protonation state of histidine 111 regulates the aggregation of the evolutionary most conserved region of the human prion protein.

  10. genetic evidence suggests association of the CARD14 (show CARD14 Proteins) single nucleotide polymorphism rs11652075 and other rare mutations in this gene with psoriasis. To assess whether combined data support the relationship between CARD14 (show CARD14 Proteins) rs11652075 and susceptibility to this disease, we conducted a meta-analysis. Our results demonstrate a significant association between the CARD14 (show CARD14 Proteins) rs11652075 polymorphism and psoriasis.

Cow (Bovine) Prion Protein (PRNP) interaction partners

  1. Misfolded structures, with nonnative beta-strands formed in the flexible N-terminal domain of PRNP were found in acidic pH simulations.

  2. 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 Proteins)) genes, are reported.

  3. 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

  4. 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 Proteins) and RP58 (show ZNF238 Proteins) may contribute to the negative feedback mechanism of PRNP.

  5. allele and haplotype segregation at the polymorphic sites within the promoter (23indel) and intron 1 (12indel) regions of the PRNP

  6. PRNP gene variation in Pakistani cattle and buffaloes.

  7. 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.

  8. 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

  9. these results identify a novel PrP(C)-interacting protein KCTD1 (show KCTD1 Proteins) and suggest a new approach to investigating the unidentified physiological cellular function of PrP(C).

  10. Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster prion protein

Mouse (Murine) Prion Protein (PRNP) interaction partners

  1. data provided molecular details about the interaction between HuPrP and the NCAM (show NCAM1 Proteins) fibronectin (show FN1 Proteins) domain, and revealed a new role of PrP(C) N terminus as a dynamic and functional element responsible for protein-protein interaction.

  2. These results suggest that PrP(C)-mGluR5 (show GRM5 Proteins) form a functional response unit by which multiple ligands can trigger signaling. We propose that trafficking of PrP(C)-mGluR5 (show GRM5 Proteins) may modulate signaling intensity by different PrP(C) ligands.

  3. prion protein-derived cell-penetrating peptide cytotoxicity is modulated by pH but independent of amyloid formation

  4. this work suggests that the sialylation status of GPIs within PrP(Sc) is regulated in a cell-, tissue-, or host-specific manner and is likely to be determined by the specifics of GPI (show GPI Proteins) biosynthesis.

  5. These results are consistent with the hypothesis that the sialylated GPI (show GPI Proteins) anchor attached to PrP(C) acts as a synapse homing signal.

  6. This study further distinguishes two separate Abetao-dependent signaling cascades, one dependent on extracellular Ca(2 (show CA2 Proteins)+) and Fyn (show FYN Proteins) kinase activation and the other dependent on the release of Ca(2 (show CA2 Proteins)+) from intracellular stores. Thus, Abetao triggers multiple distinct PrP(C)-mGluR5 (show GRM5 Proteins)-dependent events implicated in neurodegeneration and dementia.

  7. present our observations made during systematic experiments with the CC9 system targeting the endogenous Prnp locus, to either modify sequences or to boost PrP expression using CC9-based synergistic activation mediators

  8. Though astrocytes are capable of secreting PrP, this is an inefficient method of transferring prion infectivity. Efficient transfer required co-culturing and direct cell contact. Astrocytes form numerous intercellular connections including tunneling nanotubes, containing PrP(Sc), often colocalized with endolysosomal vesicles, which may constitute the major mechanism of transfer.

  9. PrP(C) promotes myelin homeostasis through flexible tail-mediated Gpr126 (show GPR126 Proteins) agonism

  10. 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.

Pig (Porcine) Prion Protein (PRNP) interaction partners

  1. single nucleotide polymorphisms (G11A, G615C, G684A, T726G) in the open reading frame of the porcine PRNP gene were found

Rabbit Prion Protein (PRNP) interaction partners

  1. 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

  2. Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster prion protein

  3. 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

  4. 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.

  5. The salt bridge between D177 and R163 greatly contributes to the structural stability of rabbit prion protein.

Rhesus Monkey Prion Protein (PRNP) interaction partners

  1. Data show the presence of PrP(Sc) in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.

  2. 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.

Golden Syrian Hamster Prion Protein (PRNP) interaction partners

  1. Findings indicate the molecular mechanisms of prion pathogenesis and strain diversity.

  2. Data indicate that prion protein PrP dimers were funneled into a thermodynamically stable misfolded state along a single pathway containing several intermediates.

  3. Here, we report that the degree of PrP(Sc) protease resistance is highly dependent on the concentration of salt in the solution.

  4. Localization of fully posttranslationally modified Syrian golden hamster glycosylated PrPC is confirmed in the plasma membrane together with the posttranslational glycosylation pattern.

PRNP Protein Profile

Protein Summary

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.

Alternative names and synonyms associated with PRNP

  • prion protein (prnp)
  • prion protein (PRNP)
  • caspase recruitment domain family, member 14 (CARD14)
  • prion protein (Prnp)
  • prion protein (PRP)
  • AA960666 protein
  • AI325101 protein
  • AltPrP protein
  • ASCR protein
  • BIMP2 protein
  • CARMA2 protein
  • CD230 protein
  • CJD protein
  • GSS protein
  • KURU protein
  • MGC84114 protein
  • p27-30 protein
  • prion protein
  • PRIP protein
  • Prn protein
  • Prn-i protein
  • Prn-p protein
  • PRNP protein
  • Prp protein
  • prp(c) protein
  • prP27-30 protein
  • prP33-35C protein
  • PrP protein
  • PrPC protein
  • PrPSc protein
  • PSORS2 protein
  • PSS1 protein
  • Sinc protein
  • SIP protein

Protein level used designations for Prion Protein Proteins (PRNP)

prion protein , 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 , ARIA , PR-LP , acetylcholine receptor-inducing activity , major prion protein homolog , prion-like protein , prion-like-protein , prP27-30 , prP33-35C , glutathione synthetase , major prion protein preproprotein , prP , infectious amyloid , PrP 27-30

GENE ID SPECIES
444620 Xenopus laevis
554189 Monodelphis domestica
100065904 Equus caballus
100173712 Pongo abelii
100499575 Ailuropoda melanoleuca
79092 Homo sapiens
5621 Homo sapiens
281427 Bos taurus
493887 Ovis aries
19122 Mus musculus
24686 Rattus norvegicus
494014 Sus scrofa
493886 Felis catus
396452 Gallus gallus
485783 Canis lupus familiaris
100008658 Oryctolagus cuniculus
100345744 Oryctolagus cuniculus
717859 Macaca mulatta
458076 Pan troglodytes
101829062 Mesocricetus auratus
Selected quality suppliers for PRNP Proteins (PRNP)
Did you look for something else?