Prion Protein

Prion Protein

Prion Protein

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  • View Data Sheet

    Description:

    Prion Protein Human Recombinant

    ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.

    Product # :

    PRO-1400

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    • description
    • source
    • formulation
    • purity
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    Description

    PRNP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (23-230a.a) and having a molecular mass of 25kDa. GOSR2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PRNP protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Prion protein (PRNP) is a ubiquitous membrane glycoprotein whose abnormal self-replicating, misfolded form is widely believed to cause several central nervous system disorders, together known as Transmissible Spongiform Encephalopathies (TSE). PRNP contains a highly unstable region of five tandem octapeptide repeat. Mutations in PRNP protein’s repeat region as well as elsewhere have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru.

    • Synonyms

      ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKKRPKPGGW NTGGSRYPGQ GSPGGNRYPP QGGGGWGQPH GGGWGQPHGG GWGQPHGGGW GQPHGGGWGQ GGGTHSQWNK PSKPKTNMKH MAGAAAAGAV VGGLGGYVLG SAMSRPIIHF GSDYEDRYYR ENMHRYPNQV YYRPMDEYSN QNNFVHDCVN ITIKQHTVTT TTKGENFTET DVKMMERVVE QMCITQYERE SQAYYQRGS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Prnp Human
  • View Data Sheet

    Description:

    Prion Protein 2 Human Recombinant

    Prion protein 2, DOPPEL, DPL, PrPL.

    Product # :

    PRO-018

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    Description

    PRND Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (27-152a.a) and having a molecular mass of 16.9kDa. PRND is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRND protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRND is a membrane glycosylphosphatidylinositol-anchored glycoprotein which exists mainly in testis. PRND is expressed during embryogenesis, although in the central nervous system it is expressed minimally .Mutations in PRND may cause neurological disorders. PRND located on chromosome 20, about 20 kbp downstream of the gene encoding cellular prion protein, to which it is biochemically and structurally analogous.

    • Synonyms

      Prion protein 2, DOPPEL, DPL, PrPL.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSRGIKHRI KWNRKALPST AQITEAQVAE NRPGAFIKQG RKLDIDFGAE GNRYYEANYW QFPDGIHYNG CSEANVTKEA FVTGCINATQ AANQGEFQKP DNKLHQQVLW RLVQELCSLK HCEFWLERG.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Prnd Human

About PRN / Prion Protein:

Prion (PRN) proteins are defined as misfolded proteins that are able to transmit their shape upon normal proteins. Why this happens is currently not known, but they are considered the main characteristic in a range of fatal and sometimes transmissible neurodegenerative diseases.
For instance, prion isoforms of the prion protein have been hypothesized as having an integral cause in the development of mad cow disease, chronic wasting disease in deer, and scrapie in sheep. All of these prion diseases have no effective treatment as of yet, and unfortunately, they always lead to fatal consequences.

PRN Structure
Prions are known to form unfamiliar aggregates of proteins which have been associated with both cell death and tissue damage. The proteins that prions develop from is found throughout the body in both human and animal populations. However, in infectious form, the PrPSc curates a different structure and becomes immune to the protein-processing enzymes.

Prion Protein Types
Types of prion disease can include CJD and its variant, fatal insomnia, and Kuru. Prions can form amyloids, for aforementioned aggregates of proteins, and are linked to certain neurodegenerative diseases in old age, like Alzheimer’s and Parkinson’s.

PRN Function
The normal functioning of the Prion Protein and its physiological function is not entirely understood. It has been found that the activation of myelin repair seems to be caused of Prion proteins in the peripheral nerves.
Those with risk factors of prion disease include those with a family history of it, eating meat infected with ‘mad cow disease’ and exposure to contaminated medical equipment.