Product nameAnti-Prion protein PrP antibody [1E5 / G6] (HRP)
See all Prion protein PrP primary antibodies
DescriptionMouse monoclonal [1E5 / G6] to Prion protein PrP (HRP)
SpecificityThis antibody detects: Human recombinant prion protein, Bovine recombinant, native and PrPres proteinase K treated prion protein.
Tested applicationsSuitable for: WB, ELISA, IHC-Pmore details
Species reactivityReacts with: Cow, Human
Recombinant bovine prion protein. Immunization was performed according to the protocol described by Hofmann, J. et al.
EpitopeThis antibody has been shown to specifically bind between amino acids 140 - 160 of bovine prion protein, determined by pepscan (Osman, A.A. et al.).
- native bovine prion protein from brain (M. oblongata)
Storage instructionsShipped at 4°C. Store at +4°C.
Storage bufferConstituent: 50% Glycerol
Concentration information loading...
PurityImmunogen affinity purified
Clone number1E5 / G6
Light chain typekappa
- TMB ELISA Substrate (Highest Sensitivity) (ab171522)
- TMB ELISA Substrate (High Sensitivity) (ab171523)
- TMB ELISA Substrate (Fast Kinetic Rate) (ab171524)
- TMB ELISA Substrate (Slow Kinetic Rate) (ab171525)
- TMB ELISA Substrate (Slower Kinetic Rate) (ab171526)
- TMB ELISA Substrate (Slowest Kinetic Rate) (ab171527)
- 450 nm Stop Solution for TMB Substrate (ab171529)
- 650 nm Stop Solution for TMB Substrate (ab171531)
- Immunoassay Blocking Buffer (ab171534)
- Immunoassay Blocking (BSA Free) (ab171535)
Our Abpromise guarantee covers the use of ab3408 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
IHC-P: Use at an assay dependent concentration (please check Abreview).
WB: Use at a concentration of 1 - 10 µg/ml.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
FunctionThe function of PrP is still under debate. 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 (By similarity). Isoform 2 may act as a growth suppressor by arresting the cell cycle at the G0/G1 phase. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro).
Involvement in diseaseNote=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) [MIM:123400]. 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) [MIM:600072]. 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) [MIM:137440]. 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) [MIM:603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.
Defects in PRNP are the cause of kuru (KURU) [MIM:245300]. 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) [MIM:606688]; 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.
Sequence similaritiesBelongs to the prion family.
DomainThe normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization.
Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization.
modificationsThe glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.
Isoform 2 is sumoylated by SUMO1.
Cellular localizationCell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.
- Information by UniProt
- Alternative prion protein; major prion protein antibody
- AltPrP antibody
- ASCR antibody
Anti-Prion protein PrP antibody [1E5 / G6] (HRP) (ab3408) at 1 µg/ml + native bovine prion protein from brain (M. oblongata)
Performed under non-reducing conditions.
Observed band size: 19 kDa why is the actual band size different from the predicted?
Additional bands at: 27 kDa (possible glycosylated form), 30 kDa (possible glycosylated form)
ab3408 (1/100) staining Prion protein PrP (red) in inflammatory cells from peri-infarcted regions of a human brain after ischaemic stroke. Please refer to Abreview for further experimental details.