Browse our PRNP Proteins (PRNP)

Full name:
Prion Protein Proteins (PRNP)
On are 54 Prion Protein (PRNP) Proteins from 9 different suppliers available. Additionally we are shipping PRNP Antibodies (210) and PRNP Kits (26) and many more products for this protein. A total of 298 PRNP products are currently listed.
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

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PRNP Proteins (PRNP) by Origin

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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 1098792

  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. these data indicate that the disruption of the PrP(C)-HOP (show STIP1 Proteins) complex could be a potential therapeutic target for modulating the migratory and invasive cellular properties that lead to metastatic Colorectal cancer (CRC (show CALR Proteins)).

  2. computational approach to elucidate in details the aggregation propensity of PrP (show C4BPA Proteins) protein systems including wild type, wild type treated at different [Ca2 (show CA2 Proteins)+] or E200K mutant; models for the self-assembly of either the E200K mutated or Ca2 (show CA2 Proteins)+-bound PrPC were sketched and discussed

  3. MALT1 (show MALT1 Proteins) deficiency or pharmacological inhibition of MALT1 (show MALT1 Proteins) catalytic activity inhibits pathogenic mutant CARD14 (show CARD14 Proteins)-induced cytokine and chemokine (show CCL1 Proteins) expression in human primary keratinocytes.

  4. The results have unraveled a novel molecular pathway driven by interactions between prion protein (PrP) and Notch1 (show NOTCH1 Proteins) in the progression of pancreatic ductal adenocarcinoma (PDAC), supporting a critical tumor-promoting role of Notch1 (show NOTCH1 Proteins) in PrP (show C4BPA Proteins)-expressing PDAC tumors.

  5. CARD14 (show CARD14 Proteins)/MALT1 (show MALT1 Proteins)-mediated signaling in keratinocytes has a role in psoriasis [review]

  6. The results indicate that the common CARD14 (show CARD14 Proteins) p.Arg820Trp variant might have a significant effect on the response to anti-TNF (show TNF Proteins) therapies among patients with psoriasis. In addition, rare CARD14 (show CARD14 Proteins) missense variants could also predispose to a better response.

  7. The present findings unveil particular neuropathological and neuroinflammatory profiles in Fatal familial insomnia(FFI) and novel characteristics of natural prion protein in FFI, altered PrPres and Scrapie PrP (show C4BPA Proteins) (abnormal and pathogenic PrP (show C4BPA Proteins)) patterns and region-dependent putative capacity of PrP (show C4BPA Proteins) seeding

  8. Our findings, combined with the published literature, suggest that Pityriasis Rubra Pilaris Type V, both familial and sporadic, can be caused by CARD14 (show CARD14 Proteins) mutations.

  9. Distinctive properties of plaque-type dura mater graft-associated Creutzfeldt-Jakob disease PrPSc proteins in cell-protein misfolding cyclic amplification.

  10. Molecular insights obtained through MD (molecular dynamics) simulations suggested that each bispidine-based peptidomimetic differently engages a conserved Tyr (show TYR Proteins) 169 residue at the alpha2-beta2 loop of HuPrP and affects the stability of alpha2 and alpha3 helices.

Cow (Bovine) Prion Protein (PRNP) interaction partners

  1. Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND (show PRND Proteins)) Variation in Domestic Cattle

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

  3. 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.

  4. 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

  5. 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.

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

  7. PRNP gene variation in Pakistani cattle and buffaloes.

  8. 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.

  9. 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

  10. 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).

Mouse (Murine) Prion Protein (PRNP) interaction partners

  1. The retention of prion protein in the endoplasmic reticulum prevents neuroblastoma (show ARHGEF16 Proteins) cells from proteasome inhibition-induced cytotoxicity.

  2. Data, including data from studies using knockout/transgenic mice, suggest that PrPC is involved in development of insulin (show INS Proteins) resistance and obesity; PrPC knockout mice fed high-fat diet present all the symptoms associated with insulin (show INS Proteins) resistance (hyperglycemia, hyperinsulinemia, and obesity); transgenic mice overexpressing PrPC fed high-fat diet exhibit normal insulin (show INS Proteins) sensitivity and reduced weight gain.

  3. PrP aggresomes are cytosolic overflow deposition centers for the endoplasmic reticulum quality control mechanisms.

  4. recombinant PrP functions as a signaling molecule, and its homophilic interaction with membrane-anchored PrP(C) might promote neurite outgrowth and facilitate growth cone guidance.

  5. Results suggest that prion protein PrPC combined with galectin-3 (show LGALS3 Proteins) and -6 can act as a receptor for murine leukemia virus (MuLV).

  6. using a transgenic model we could not provide evidence to support the hypothesis that PrPC regulates amyloid-beta production

  7. PrP deficiency caused a loss or enhancement of NCAM1 (show NCAM1 Proteins) polysialylation, dependent on the cell model used.

  8. ion channel formation may be a possible mechanism of PrP-mediated neurodegeneration by the transmembrane forms of PrP

  9. 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.

  10. 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.

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

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
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