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Key Specifications Table
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H, Ht | ELISA, IHC, IH(P), IP, WB | M | Purified | Monoclonal Antibody |
| Description | |
|---|---|
| Catalogue Number | MAB1562 |
| Brand Family | Chemicon® |
| Trade Name |
|
| Description | Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4 |
| Alternate Names |
|
| Background Information | Prions are thought to cause a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and the Creutzfeldt-Jakob disease (CJD) in humans. All thus-far hypothesized prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and thought to be fatal. Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing cell death and tissue damage. This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult. |
| Product Information | |
|---|---|
| Format | Purified |
| Control |
|
| Presentation | Purified mouse monoclonal IgG2a in buffer containing PBS and no preservative. |
| Quality Level | MQ100 |
| Applications | |
|---|---|
| Application | This Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4 is validated for use in ELISA, IH, IH(P), IP, WB for the detection of Prion Protein. |
| Key Applications |
|
| Application Notes | Immunohistochemistry(paraffin): Representative images from a previous lot. Optimal Staining With Citrate Buffer, pH 6.0, Epitope Retrieval: Human Brain Immunohistochemistry (Kitamoto et al., 1987): 1:100-1:1,000 *See protocol below. Epitope must be re-exposed in fixed tissue by pretreatment of tissue using one of the following procedures: a. formic acid for 10 minutes at room temperature (Kitamoto et al., 1987) b. hydrolytic autoclaving (Kitamoto et al., 1991) c. microwaving (BioGenex, San Ramon, CA) Western Blot: (Kascsak, R.J., 1991; Kascsak, R.J., 1987): 1:10,000-1:100,000 dilution of a previous lot was used. Immunoprecipitation: (Kascsak, R.J., 1991; Kascsak, R.J., 1987): 1:10-1:100 dilution of a previous lot was used. ELISA: (Kascsak, R.J., 1991; Kascsak, R.J., 1987): Optimal working dilutions must be determined by end user. |
| Biological Information | |
|---|---|
| Epitope | a.a. 109-112 |
| Clone | 3F4 |
| Host | Mouse |
| Specificity | Prion protein, amino acid residues 109-112 of human, hamster and feline. Does not react with PrP from any other mammalian species. MAB1562 is reactive to native and denatured forms of PrP. Tissue or cells which have been fixed requires that the epitope be re-exposed (see below). Recognizes both protease sensitive and protease resistant forms of PrP. |
| Isotype | IgG2a |
| Species Reactivity |
|
| Antibody Type | Monoclonal Antibody |
| Entrez Gene Number |
|
| Entrez Gene Summary | 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. Alternative splicing results in multiple transcript variants encoding the same protein. |
| Gene Symbol |
|
| Purification Method | Protein A Purfied |
| UniProt Number |
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| UniProt Summary | FUNCTION: SwissProt: P04156 # The physiological function of PrP is not known. SIZE: 253 amino acids; 27661 Da SUBUNIT: PrP has a tendency to aggregate yielding polymers called rods. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. PTM: The glycosylation pattern (the amount of mono-, di- and non- glycosylated forms or glycoforms) seems to differ in normal and CJD prion. DISEASE: SwissProt: P04156 # 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 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 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 [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 prion disease with protracted course [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. SIMILARITY:SwissProt: P04156 ## Belongs to the prion family. |
| Molecular Weight | 12.3 kDa |
| Product Usage Statements | |
|---|---|
| Quality Assurance | Immunohistochemistry(paraffin): Prion Protein (cat. # MAB1562) staining pattern/morphology in normal brain. Tissue was pretreated with Citrate, pH 6.0. This lot of antibody was diluted to 1:500, using IHC-Select® Detection with HRP-DAB. Immunoreactivity is seen predominantly as cell body staining of neurons. Optimal Staining With Citrate Buffer, pH 6.0, Epitope Retrieval: Human Brain |
| Usage Statement |
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| Storage and Shipping Information | |
|---|---|
| Storage Conditions | Stable for 1 year at -20ºC from date of receipt. |
| Packaging Information | |
|---|---|
| Material Size | 100 µg |