Western Blot (WB)
(Anti-PRNP antibody, MBS175399, Western blottingAll lanes: Anti PRNP (MBS175399) at 0.5ug/mlLane 1: Rat Brain Tissue Lysate at 50ugLane 2: Rat Brain Tissue Lysate at 50ugPredicted bind size: 28KDObserved bind size: 28KD)
Rabbit anti-Mouse, Rat Prion protein PrP Polyclonal Antibody | anti-PRNP antibody
Anti-Prion protein PrP antibody
Western Blot (WB)
(Anti-PRNP antibody, MBS175399, Western blottingAll lanes: Anti PRNP (MBS175399) at 0.5ug/mlLane 1: Rat Brain Tissue Lysate at 50ugLane 2: Rat Brain Tissue Lysate at 50ugPredicted bind size: 28KDObserved bind size: 28KD)
Western Blot (WB)
(Anti-PRNP antibody, MBS175399, Western blottingAll lanes: Anti PRNP (MBS175399) at 0.5ug/mlLane 1: Rat Brain Tissue Lysate at 50ugLane 2: Rat Brain Tissue Lysate at 50ugPredicted bind size: 28KDObserved bind size: 28KD)
Immunohistochemistry (IHC)
(Anti-PRNP antibody, MBS175399, IHC(P)IHC(P): Rat Brain Tissue )
Immunohistochemistry (IHC)
(Anti-PRNP antibody, MBS175399, IHC(P)IHC(P): Rat Brain Tissue )
Background: PRNP(prion protein), also known as CD230 and PRP, is a protein that in humans is encoded by the PRNP gene. The major prion protein is expressed in the brain and several other tissues. Expression is most predominant in the nervous system but occurs in many other tissues throughout the body. Puckett et al.(1991)identified a RFLP with a high degree of heterozygosity in the 5-prime region of the PRNP gene, which might serve as a useful marker for the pter-p12 region of chromosome 20. PRNP is associated with a variety of cognitive deficiencies and neurodegenerative diseases such as Creutzfeldt-Jakob disease, bovine spongiform encephalopathy, and kuru. PRNP is highly conserved through mammals, lending credence to application of conclusions from test animals such as mice. Comparison between primates is especially similar, ranging from 92.9-99.6% similarity in amino acid sequences.
NCBI and Uniprot Product Information
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: Microtubule-binding; Membrane protein, GPI anchor
Cellular Component: Golgi apparatus; mitochondrial outer membrane; cell surface; membrane; cell; endoplasmic reticulum; cytoplasm; plasma membrane; lipid raft
Molecular Function: tubulin binding; ATP-dependent protein binding; identical protein binding; protein binding; copper ion binding; metal ion binding; chaperone binding; microtubule binding
Biological Process: cellular copper ion homeostasis; negative regulation of activated T cell proliferation; negative regulation of transcription factor activity; negative regulation of T cell receptor signaling pathway; negative regulation of interleukin-2 production; learning and/or memory; response to cadmium ion; regulation of protein localization; negative regulation of interleukin-17 production; response to copper ion; negative regulation of protein amino acid phosphorylation; negative regulation of interferon-gamma production; nucleobase, nucleoside, nucleotide and nucleic acid metabolic process; response to oxidative stress; protein homooligomerization; negative regulation of apoptosis
Research Articles on PRNP
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Product Notes
The PRNP prnp (Catalog #AAA175399) is an Antibody produced from Rabbit and is intended for research purposes only. The product is available for immediate purchase. The Anti-Prion protein PrP antibody reacts with Mouse, Rat and may cross-react with other species as described in the data sheet. AAA Biotech's Prion protein PrP can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), Immunohistochemistry (IHC) Paraffin. Researchers should empirically determine the suitability of the PRNP prnp for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "Prion protein PrP, Polyclonal Antibody" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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