Bovine Major prion protein(PRNP) ELISA kit

Code CSB-EL018739BO
Size 96T,5×96T,10×96T
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Product Details

Alternative Names
PRNP ELISA Kit; PRP ELISA Kit; Major prion protein ELISA Kit; PrP ELISA Kit; Major scrapie-associated fibril protein 1 ELISA Kit; CD antigen CD230 ELISA Kit
Abbreviation
PRNP
Uniprot No.
Species
Bos taurus (Bovine)
Sample Types
serum, plasma, tissue homogenates, cell lysates
Detection Range
0.01 ng/ml-10 ng/ml
Sensitivity
0.01 ng/ml
Assay Time
1-5h
Sample Volume
50-100ul
Detection Wavelength
450 nm
Research Area
Neuroscience
Assay Principle
quantitative
Measurement
Sandwich
Precision
 
Linearity
 
Recovery
 
Typical Data
 
Troubleshooting
and FAQs
Storage
Store at 2-8°C. Please refer to protocol.
Lead Time
3-5 working days after you place the order, and it takes another 3-5 days for delivery via DHL or FedEx
Description

This Bovine PRNP ELISA Kit was designed for the quantitative measurement of Bovine PRNP protein in serum, plasma, tissue homogenates, cell lysates. It is a Sandwich ELISA kit, its detection range is 0.01 ng/ml-10 ng/ml and the sensitivity is 0.01 ng/ml.

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Target Background

Function
(From Uniprot)
Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.
Gene References into Functions
  1. Data suggest that the E211K prion protein provides the opportunity for future analysis of physiological changes over time. PMID: 29262866
  2. Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle PMID: 27224046
  3. the data indicate a four-rung beta-solenoid structure as a key feature for the architecture of infectious mammalian prions. PMID: 27606840
  4. Insights into Chronic Wasting Disease and Bovine Spongiform Encephalopathy Species Barriers by Use of Real-Time Conversion PMID: 26157118
  5. Misfolded structures, with nonnative beta-strands formed in the flexible N-terminal domain of PRNP were found in acidic pH simulations. PMID: 24970211
  6. This work demonstrates that this isolate is transmissible, has a BSE-H phenotype when transmitted to cattle with the K211 polymorphism, and has molecular features that distinguish it from other cases of BSE-H described in the literature. PMID: 22715405
  7. Genetic characterization of PRNP promoter indel variations and the polymorphism of open reading frames (ORFs) of PRNP and bovine prion-like Shadoo (SPRN) genes, are reported. PMID: 22723200
  8. 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 PMID: 22674901
  9. The centripetal spread of bovine spongiform encephalopathy prions along the autonomic nervous system to the central nervous system, starting already halfway in the incubation time, is reported. PMID: 22781833
  10. 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 and RP58 may contribute to the negative feedback mechanism of PRNP. PMID: 22412936
  11. allele and haplotype segregation at the polymorphic sites within the promoter (23indel) and intron 1 (12indel) regions of the PRNP PMID: 22258312
  12. PRNP gene variation in Pakistani cattle and buffaloes. PMID: 22634099
  13. The Japanese and Canadian L-type bovine spongiform encephalopathy prions are identical to those from the European cases. PMID: 22453183
  14. 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. PMID: 22170597
  15. 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 PMID: 21943430
  16. these results identify a novel PrP(C)-interacting protein KCTD1 and suggest a new approach to investigating the unidentified physiological cellular function of PrP(C). PMID: 22138399
  17. Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster PMID: 21800884
  18. The polymorphisms of PRNP gene, including SNP in exon 3, 23-bp indel in promoter region, 12-bp indel in intron 1 in 2 Chinese indigenous cattle breeds of northeast China, were investigated. PMID: 21120616
  19. The del/del genotype or at least its del allele may modulate the expression of PRNP at the 23-bp locus in the medulla oblongata of the cattle breeds studied. PMID: 21611160
  20. PRNP haplotype is associated with classical bovine spongiform encephalopathy incidence in European Holstein cattle. PMID: 20862290
  21. The present study demonstrated that vector-based siRNA expression systems is an efficient approach to knockdown the PRNP gene expression in bovine fibroblast cells. PMID: 19821149
  22. The interaction of the molecular chaperone Hsc70 (HSPA8) with recombinant PrP was investigated. PMID: 20434583
  23. Role the of regulatory domains within intron 1 was defied in regulating the promoter activity of the bovine prion protein gene. PMID: 20553871
  24. unusual conformational plasticity of prion protein PMID: 20380155
  25. PRNP polymorphisms in native Chinese cattle are reportd. PMID: 20140032
  26. Study found a significant correlation between promoter indel polymorphisms and PRNP-mRNA expression; also report a novel difference in PRNP expression between Japanese Black and Japanese Brown cattle breeds. PMID: 19917050
  27. existence of two 2'-fluoro-RNA aptamer binding sites within the PrP molecule PMID: 12902353
  28. a 23-bp insertion/deletion polymorphism in the putative PRNP promoter region shows a significant association with bovine spongiform encephalopathy susceptibility in our animals. PMID: 14727152
  29. Transgenic mice expressing bovine PrP (boTg mice) bearing an additional octapeptide insertion to the wild type (seven octapeptide repeats instead of six) showed an altered course of bovine spongiform encephalopathy (BSE) infection PMID: 14999066
  30. PRNP shows no direct CAGA box correspondence with the APP superfamily members. PMID: 15208260
  31. evaluated the patterns of nucleotide variation associated with PRNP exon 3 for 36 breeds of domestic cattle PMID: 15477588
  32. A functional promoter analysis of the different bovine PRNP promoter alleles by reporter gene assays in vitro and PRNP mRNA levels in calves with different PRNP genotypes in vivo are reported. PMID: 16141216
  33. the genomic structure of three genes, PRNP, PRND, and RASSF2, within the syntenic region of the bovine genome is highly conserved in order and orientation. PMID: 16460908
  34. J protein family serves as a 'folding catalyst' for prion protein and implicates Rdj2 as a factor in the protection against prion diseases PMID: 16774738
  35. 10 single nucleotide polymorphisms (SNPs) were discovered in the coding region of the Caracu PRNP gene. PMID: 16965405
  36. DNA variants in the PRNP gene are associated with genetic disposition to bovine spongiform encephalopathy. PMID: 16978176
  37. results demonstrate a substantial genetic PRNP associated component for BSE susceptibility in cattle PMID: 17014722
  38. data indicate that bovine spongiform encephalopathy agent can be altered by crossing a species barrier, raising concerns about the virulence of this new prion towards other species, including humans. PMID: 17079295
  39. The number of polymorphisms in the prion gene region of U.S. cattle is nearly four times greater than previously described; these polymorphisms define PRNP haplotypes that may influence BSE susceptibility in cattle PMID: 17092337
  40. Immunohistochemical characterization of cell types expressing the cellular prion protein in the small intestine was studied and compared to the mouse. PMID: 17165097
  41. identified the deletion/insertion polymorphism of the prion protein gene (PRNP) within the promoter sequence (23 bp), intron 1 (12 bp) and 3' untranslated region (14 bp) PMID: 17272863
  42. These results advocate that certain polymorphisms such as specific protein 1 binding site polymorphisms in the bovine PRNP promoter region in Japanese Black cattle could influence promoter activity. PMID: 17283444
  43. Genotype and allele frequencies of the 23 bp indel polymorphism in Korean Holsteins cattle. PMID: 17426768
  44. polymorphisms in the PRNP promoter region have an influence on susceptibility to BSE PMID: 17437640
  45. Levels of the protein for PrP are higher in theca cells of dominant compared to subordinate follicles. PMID: 17595008
  46. Results describe the expression of the prion protein gene (PRNP) and cellular prion protein (PrPc) in cattle and sheep fetuses and maternal tissues during pregnancy. PMID: 17605301
  47. no association between genotype and resistance to atypical bovine spongiform encephalopathy or experimentally inoculated transmissible spongiform encephalopathies. PMID: 17709775
  48. PrP(C) specifically binds tetraspanin-7 through the region corresponding to bovine PrP(154-182) containing alpha-helix 1. PMID: 17981143
  49. The results suggest that Octapeptide repeat region of PrP(C) is required for the early step of efficient PrP(Sc) production. PMID: 17981146
  50. Polymorphisms of Two Indels at the PRNP Gene in Three Beef Cattle Herds PMID: 18064562

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Involvement in disease
Variations in PRNP are responsible of transmissible bovine spongiform encephalopathies (BSE), a class of neurodegenerative diseases that affect various mammals. These diseases are caused by abnormally folded prion proteins. BSE can be subdivided into at least three groups: classical, H-type and L-type, with the latter 2 collectively referred to as atypical BSE. Susceptibility or resistance to a BSE disease can be influenced by at least 3 factors related to the host prion protein: protein expression levels, number of octapeptide repeats, and specific polymorphisms. In cattle, as in humans, BSEs can occur as infectious, spontaneous and genetic diseases.
Subcellular Location
Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus.
Protein Families
Prion family
Database Links
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