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Neuroscience Neurology process Neurodegenerative disease Prions
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Recombinant Cow Prion protein PrP (ab753)

  • Datasheet
  • SDS
Submit a review Q&A (9)References (3)

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SDS-PAGE - Recombinant Cow Prion protein PrP (ab753)

    Key features and details

    • Expression system: Escherichia coli
    • Tags: His tag C-Terminus
    • Suitable for: SDS-PAGE, ELISA

    Description

    • Product name

      Recombinant Cow Prion protein PrP
      See all Prion protein PrP proteins and peptides
    • Expression system

      Escherichia coli
    • Accession

      P10279
    • Protein length

      Full length protein
    • Animal free

      No
    • Nature

      Recombinant
      • Species

        Cow
      • Sequence

        MKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHV AGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVY YRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQ MCITQYQRESQAYYQRGASHHHHHH
      • Predicted molecular weight

        25 kDa including tags
      • Amino acids

        25 to 244
      • Tags

        His tag C-Terminus

    Specifications

    Our Abpromise guarantee covers the use of ab753 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

      ELISA

    • Form

      Liquid
    • Concentration information loading...

    Preparation and Storage

    • Stability and Storage

      Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

      pH: 4.00
      Constituent: 0.082% 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

    • SDS-PAGE - Recombinant Cow Prion protein PrP (ab753)
      SDS-PAGE - Recombinant Cow Prion protein PrP (ab753)

      SDS-PAGE of 2 µg PrPc (lane 1).

    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 (3)

    Publishing research using ab753? Please let us know so that we can cite the reference in this datasheet.

    ab753 has been referenced in 3 publications.

    • Legleiter LR  et al. Copper deficiency in the young bovine results in dramatic decreases in brain copper concentration but does not alter brain prion protein biology. J Anim Sci 86:3069-78 (2008). WB . PubMed: 18599661
    • Legleiter LR  et al. Decreased brain copper due to copper deficiency has no effect on bovine prion proteins. Biochem Biophys Res Commun 352:884-8 (2007). PubMed: 17157816
    • Legleiter LR  et al. Exposure to low dietary copper or low copper coupled with high dietary manganese for one year does not alter brain prion protein characteristics in the mature cow. J Anim Sci 85:2895-903 (2007). WB . PubMed: 17644786

    Customer reviews and Q&As

    Show All Reviews Q&A
    Submit a review Submit a question

    1-9 of 9 Abreviews or Q&A

    Question

    looking for human prion protein
    the proteins we list do not state which species they were derived from

    Read More

    Abcam community

    Verified customer

    Asked on Jul 19 2013

    Answer

    Ab753: is derived from cattle
    Ab74200: is derived from sheep ARR genotype
    Ab90464: is derived from sheep
    Ab90482: is derived from hamster
    Ab90483: is derived from hamster
    ab140567: is a human prion protein
    Thus, it is ab140567 that would be suitable for you.
    I will also make sure that we update our datasheets with this crucial information.

    Read More

    Sybille Rex

    Abcam Scientific Support

    Answered on Jul 19 2013

    Question

    Please confirm if the prion protein ab753 is infectious?

    Read More

    Abcam community

    Verified customer

    Asked on Mar 06 2012

    Answer

    Thank you for your enquiry.

    I can confirm thatto our knowledge Prion protein PrP ab753 is not infectious. It is a recombinant prion protein HIS tagged, not glycosylated and the product will be completely digested by Proteinase K.

    As far as I am aware, it is the mutated forms of the prion protein that are infectious, such as cPrP.

    I hope this will be helpful to you. If you have any further questions, please do not hesitate to contact us.

    Read More

    Abcam Scientific Support

    Answered on Mar 06 2012

    Question

        Hi thanks for your prompt response. The application is western blotting. the conjugate I am not surebut highly likely is going to be HRP. But your advice on this is welcomed.

    Read More

    Abcam community

    Verified customer

    Asked on Dec 06 2011

    Answer

    Thanks for the additional information. Here is a link to an HRP-conjugated secondary antibody you could for western blotting with ab703: https://www.abcam.com/Rabbit-IgG-secondary-antibody-ab16284.html I hope this is helpful. Please contact me again if  you have any further questions.

    Read More

    Abcam Scientific Support

    Answered on Dec 06 2011

    Question

      Hello Thanks for your previous advice. Could you please also advice me what is the best secondry antibody to detect primary anti-body ab703.

    Read More

    Abcam community

    Verified customer

    Asked on Dec 05 2011

    Answer

    Thank you for your enquiry. I would be happy to help you find a secondary antibody for use with ab703. If you could let me know what application you would use the antibody for and what conjugate you would like attached to the secondary (eg. HRP, biotin, what color fluorophore) then I can recommend a product.

    Read More

    Abcam Scientific Support

    Answered on Dec 05 2011

    Question

      Dear Sir/Madam I would like to order your prion like protein (ab753). However, I need a primary antibody to detect it. Can you please confirm that your antibody (ab52604) is able to detect that prion like protein. I look forward to hearing from you.

    Read More

    Abcam community

    Verified customer

    Asked on Nov 17 2011

    Answer

    Thank you for contacting us. The immunogen used for ab52604 was a smaller peptide from human Prion protein, whereas the protein ab753 is recombinant bovine Prion protein. Ab52604 was not tested for bovine and is not guaranteed to react; a better choice for use with ab753 is ab703, which used ab753 as the immunogen and will definately detect it. I hope this information is helpful to you. Please do not hesitate to contact us if you need any more advice or information.  

    Read More

    Abcam Scientific Support

    Answered on Nov 17 2011

    Question

    For both ab1391 and ab753, what is the conformation of the protein? For ab753, it states to reconstitute in 10 mM sodium acetate buffer or in water (comes lyophilized); is it now as a liquid?

    Read More

    Abcam community

    Verified customer

    Asked on May 17 2004

    Answer

    Thank you for your enquiry. Ab753 is a protein solution in 10 mM sodium acetate buffer; it used to come in lyophilized form but now comes reconstituted in 10 mM sodium acetate buffer. Ab1391 is a protein solution in 50 mM sodium acetate buffer. This is all the information that the originator was able to give me. If you have any more questions, please contact us again.

    Read More

    Abcam Scientific Support

    Answered on May 19 2004

    Question

    First of all, thank you for the information. I would be pleased if you could say me the composition of the buffer used for peptide reconstitution. We are doing adsortion studies with the peptide, and in those tissue sections where we add the peptide diaminobenzidine precipitates (this doesn''t happen in the positive control without peptide). We think it might be due to the composition of the buffer. Could be possible to buy the protein lyophilised?

    Read More

    Abcam community

    Verified customer

    Asked on May 10 2004

    Answer

    Thank you for your enquiry. As described in the data sheet, the buffer is 10 mM sodium acetate buffer pH 4.0. Sorry, we don't produced rb-PrP as lyophilised protein.

    Read More

    Abcam Scientific Support

    Answered on May 11 2004

    Question

    Does the bovine prion recombinant protein ab753 needs special facilities to be handled? (L2, L3 ...)

    Read More

    Abcam community

    Verified customer

    Asked on Oct 13 2003

    Answer

    The antibody does not require any special handling facilities.

    Read More

    Asdf Edo

    Abcam Scientific Support

    Answered on Oct 13 2003

    Question

    Is the His tag at the amino or carboxy terminus of the recombinant PrP protein?

    Read More

    Abcam community

    Verified customer

    Asked on Jul 02 2003

    Answer

    His tag is at the carboxy terminus of the recombinant bovine PrP.

    Read More

    Abcam Scientific Support

    Answered on Jul 02 2003

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