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Major prion protein

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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 a 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) (By similarity). 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 (By similarity).

Below are the list of possible Major prion protein products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

Major prion protein

 Major prion protein ELISA Kit
 Major prion protein Recombinant
 Major prion protein Antibody
Also known as Major prion protein (PrP) (ASCR) (PrP27-30) (PrP33-35C) (CD antigen CD230).
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
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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

Chromosomal Location of Human Ortholog: 20p13

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

Molecular Function: copper ion binding; identical protein binding; microtubule binding; protein binding; tubulin binding

Biological Process: metabolic process; negative regulation of activated T cell proliferation; 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; response to oxidative stress

Disease: Creutzfeldt-jakob Disease; Fatal Familial Insomnia; Gerstmann-straussler Disease; Huntington Disease-like 1; Kuru, Susceptibility To; Spongiform Encephalopathy With Neuropsychiatric Features
 PRNP ELISA Kit
 PRNP Recombinant
 PRNP Antibody
 ALTPRP ELISA Kit
 ALTPRP Recombinant
 ALTPRP Antibody
 PRIP ELISA Kit
 PRIP Recombinant
 PRIP Antibody
 PRP ELISA Kit
 PRP Recombinant
 PRP Antibody
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Major prion protein 1

 Major prion protein 1 ELISA Kit
 Major prion protein 1 Recombinant
 Major prion protein 1 Antibody
Also known as Major prion protein 1 (PrP) (Major scrapie-associated fibril protein 1) (CD antigen CD230).
Its primary physiological function is unclear. Has cytoprotective activity against internal
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or environmental stresses. 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 ().
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Major prion protein 2

 Major prion protein 2 ELISA Kit
 Major prion protein 2 Recombinant
 Major prion protein 2 Antibody
Also known as Major prion protein 2 (PrP) (Major scrapie-associated fibril protein 2) (CD antigen CD230).
Its primary physiological function is unclear. Has cytoprotective activity against internal
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or environmental stresses. 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 ().
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Major prion protein homolog

 Major prion protein homolog ELISA Kit
 Major prion protein homolog Recombinant
 Major prion protein homolog Antibody
Also known as Major prion protein homolog (65-21 protein) (Acetylcholine receptor-inducing activity) (ARIA) (PR-LP).
This gene encodes a membrane glycosylphosphatidylinositol-anchored glycoprotein found in the central nervous system. In human and other vertebrates, the homologous protein is associated with neurodegenerative diseases that result from improper protein metabolism. [provided by Ref
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Seq, Nov 2012]
 PRNP ELISA Kit
 PRNP Recombinant
 PRNP Antibody
 PRN-P ELISA Kit
 PRN-P Recombinant
 PRN-P Antibody
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