Major prion protein Recombinant Protein | Prnp recombinant protein

Recombinant Rat Major prion protein

Cat. Num. AAA1207676

• Gene Names: Prnp; PrP; Prn
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Major prion protein; Recombinant Rat Major prion protein; CD230; Prnp recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 29-231. Full-Length of the Mature Protein
• Sequence: GGWNTGGSRYPGQGSPGGNRYPPQSGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWSQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMLHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for Prnp recombinant protein

May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. 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 Cu2+ or ZN2+ for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.

References

Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats.Gomi H., Ikeda T., Kunieda T., Itohara S., Prusiner S.B., Yamanouchi K.Neurosci. Lett. 166:171-174(1994) Three-exon structure of the gene encoding the rat prion protein and its expression in tissues.Saeki K., Matsumoto Y., Hirota Y., Matsumoto Y., Onodera T.Virus Genes 12:15-20(1996) Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein.Wopfner F., Weidenhofer G., Schneider R., von Brunn A., Gilch S., Schwarz T.F., Werner T., Schatzl H.M.J. Mol. Biol. 289:1163-1178(1999) Cloning of rat 'prion-related protein' cDNA.Liao Y.-C., Tokes Z., Lim E., Lackey A., Woo C.H., Button J.D., Clawson G.A.Lab. Invest. 57:370-374(1987) Lubec G., Kang S.U., Lubec S.Submitted (SEP-2007) to UniProtKB

NCBI and Uniprot Product Information

• NCBI GI #: 6981410
• NCBI GeneID: 24686
• NCBI Accession #: NP_036763.1
• NCBI GenBank Nucleotide #: NM_012631.2
• UniProt Accession #: P13852; Q549H6
• Molecular Weight: 24.3 kDa
• NCBI Official Full Name: major prion protein
• NCBI Official Synonym Full Names: prion protein
• NCBI Official Symbol: Prnp
• NCBI Official Synonym Symbols: PrP; Prn
• NCBI Protein Information: major prion protein
• UniProt Protein Name: Major prion protein
• Protein Family: Major prion protein
• UniProt Gene Name: Prnp
• UniProt Synonym Gene Names: Prn; Prp; PrP
• UniProt Entry Name: PRIO_RAT

NCBI Description

conformational conversion of gene product prion protein (PrP) associated with Prion diseases, fatal neurodegenerative disorders in man and animal [RGD, Feb 2006]

Uniprot Description

PRNP: May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. 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. PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs. Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD). CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness. Defects in PRNP are the cause of fatal familial insomnia (FFI). FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia. Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD). GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births. Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1). HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features. Defects in PRNP are the cause of kuru (KURU). Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset. Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF); an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms. Belongs to the prion family. 2 isoforms of the human protein are produced by alternative initiation.

Protein type: Membrane protein, GPI anchor; Microtubule-binding

Cellular Component: anchored to plasma membrane; cell surface; cytoplasm; endoplasmic reticulum; Golgi apparatus; lipid raft; membrane; mitochondrial outer membrane; plasma membrane

Molecular Function: ATP-dependent protein binding; chaperone binding; copper ion binding; identical protein binding; lamin binding; microtubule binding; tubulin binding

Biological Process: learning and/or memory; negative regulation of activated T cell proliferation; negative regulation of apoptosis; negative regulation of interferon-gamma production; negative regulation of interleukin-17 production; negative regulation of interleukin-2 production; negative regulation of protein amino acid phosphorylation; negative regulation of T cell receptor signaling pathway; negative regulation of transcription factor activity; protein homooligomerization; regulation of protein localization; response to cadmium ion; response to copper ion; response to oxidative stress