Testing Data
(MBS6010100 staining of prion plaques from human CJD brain.)
Goat Prion Protein, aa79-97 Polyclonal Antibody | anti-PRNP antibody
Prion Protein, aa79-97, NT (PrP, CD230)
Serum.
Serum.
Dilution: Immunohistochemistry: >1:200 on paraffin embedded, formalin fixed human brain.
Western Blot: > 1:2000
ELISA: > 1:35,000
Optimal dilutions to be determined by researcher.
Testing Data
(MBS6010100 staining of prion plaques from human CJD brain.)
Testing Data
(MBS6010100 staining of prion plaques from human CJD brain.)
NCBI and Uniprot Product Information
NCBI Description
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. [provided by RefSeq, Oct 2012]
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
Chromosomal Location of Human Ortholog: 20p13
Cellular Component: Golgi apparatus; mitochondrial outer membrane; cell surface; extrinsic to membrane; endoplasmic reticulum; cytoplasm; plasma membrane; integral to membrane; nucleus; lipid raft
Molecular Function: tubulin binding; ATP-dependent protein binding; identical protein binding; protein binding; copper ion binding; microtubule binding; chaperone binding
Biological Process: axon guidance; cellular copper ion homeostasis; metabolic process; 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; regulation of protein localization; learning and/or memory; response to cadmium ion; negative regulation of interleukin-17 production; negative regulation of protein amino acid phosphorylation; negative regulation of interferon-gamma production; response to oxidative stress; cell cycle arrest; protein homooligomerization; negative regulation of apoptosis
Disease: Gerstmann-straussler Disease; Huntington Disease-like 1; Kuru, Susceptibility To; Fatal Familial Insomnia; Creutzfeldt-jakob Disease; Spongiform Encephalopathy With Neuropsychiatric Features
Research Articles on PRNP
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Product Notes
The PRNP prnp (Catalog #AAA6010100) is an Antibody produced from Goat and is intended for research purposes only. The product is available for immediate purchase. The Prion Protein, aa79-97, NT (PrP, CD230) reacts with Bovine, Drosophila, Hamster, Human, Mouse, Sheep and may cross-react with other species as described in the data sheet. AAA Biotech's Prion Protein, aa79-97 can be used in a range of immunoassay formats including, but not limited to, ELISA (EL/EIA), Western Blot (WB), Immunohistochemistry (IHC). Suitable for use in Immunohistochemistry, Western Blot, ELISA. Other application not tested. Dilution: Immunohistochemistry: >1:200 on paraffin embedded, formalin fixed human brain. Western Blot: > 1:2000 ELISA: > 1:35,000 Optimal dilutions to be determined by researcher. 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, aa79-97, 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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