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Neuroscience Neurology process Neurodegenerative disease Prions
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Recombinant Mouse Prion protein PrP (ab74056)

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Western blot - Recombinant Mouse Prion protein PrP  (ab74056)

    Key features and details

    • Expression system: Escherichia coli
    • Purity: > 95% SDS-PAGE
    • Suitable for: SDS-PAGE, WB

    Description

    • Product name

      Recombinant Mouse Prion protein PrP
      See all Prion protein PrP proteins and peptides
    • Purity

      > 95 % SDS-PAGE.
      ab74056 is purified by metal-chelation and ion exchange chromatography, copper refolded. It is solubilized from inclusion bodies in 8 M urea.
    • Expression system

      Escherichia coli
    • Protein length

      Full length protein
    • Animal free

      No
    • Nature

      Recombinant
      • Species

        Mouse

    Associated products

    • Related Products

      • Anti-Prion protein PrP antibody [EP1802Y] (ab52604)
      • Anti-Prion protein PrP antibody [8H4] (ab61409)
      • Anti-Prion protein PrP antibody (ab703)

    Specifications

    Our Abpromise guarantee covers the use of ab74056 in the following tested applications.

    The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

    • Applications

      SDS-PAGE

      Western blot

    • Form

      Liquid
    • Concentration information loading...

    Preparation and Storage

    • Stability and Storage

      Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.

      Constituent: 0.41% Sodium acetate

    General Info

    • Alternative names

      • Alternative prion protein; major prion protein
      • AltPrP
      • ASCR
      • CD230
      • CD230 antigen
      • CJD
      • GSS
      • KURU
      • Major prion protein
      • p27 30
      • PRIO_HUMAN
      • Prion protein
      • Prion related protein
      • PRIP
      • PRNP
      • PrP
      • PrP27 30
      • PrP27-30
      • PrP33-35C
      • PrPC
      • PrPSc
      • Sinc
      see all
    • Function

      The 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 disease

      Note=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 similarities

      Belongs to the prion family.
    • Domain

      The 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.
    • Post-translational
      modifications

      The 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 localization

      Cell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.
    • Target information above from: UniProt accession P04156 The UniProt Consortium
      The Universal Protein Resource (UniProt) in 2010
      Nucleic Acids Res. 38:D142-D148 (2010) .

      Information by UniProt

    Images

    • Western blot - Recombinant Mouse Prion protein PrP  (ab74056)
      Western blot - Recombinant Mouse Prion protein PrP (ab74056)

    Protocols

    To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.

    Click here to view the general protocols

    Datasheets and documents

    • SDS download

    • Datasheet download

      Download

    References (0)

    Publishing research using ab74056? Please let us know so that we can cite the reference in this datasheet.

    ab74056 has not yet been referenced specifically in any publications.

    Customer reviews and Q&As

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    Question

    Could you please confirm the sequence of murine PrP (ab74056)? ie. Does it carry a His tag? If not, does it have an N-terminal methionine?

    Read More

    Abcam community

    Verified customer

    Asked on Jul 15 2013

    Answer



    ab74056 is a recombinant murine PrP (amino acid residues 23-231), with an N-terminal methionine and serine.

    It is expressed from a PCR-amplified ORF segment inserted into a pET23b expression vector, transformed into BL21(DE3)pLysS strain of E.coli, solubilised from inclusion bodies in 8M urea, 20mM Tris HCl, 0.1M sodium phosphate.

    It was then purified by metal-chelation and ion exchange chromatography, copper refolded and dialysed to 50mM sodium acetate.

    Read More

    Elisa Thomas

    Abcam Scientific Support

    Answered on Jul 15 2013

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