PRNP Human

Prion Protein Human Recombinant
Cat. No.
BT7001
Source
E.coli.
Synonyms
ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek'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.
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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.

Product Specs

Introduction
Prion protein (PRNP) is a membrane glycoprotein found throughout the body. Its misfolded form is believed to cause a group of central nervous system disorders known as Transmissible Spongiform Encephalopathies (TSE). PRNP has a region of five repeating octapeptide sequences. Mutations in this repeat region and other parts of the PRNP gene are linked to diseases like Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru.
Description
This product is a recombinant human PRNP protein produced in E. coli bacteria. It is a single chain of 229 amino acids (positions 23-230) without glycosylation, resulting in a molecular weight of 25kDa. It includes a 21 amino acid His-tag attached to the N-terminus for purification purposes, which is achieved through proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The PRNP protein is supplied in a solution at a concentration of 0.25mg/ml. The solution is buffered with 20mM Tris-HCl at pH 8.0 and contains 1M Urea and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the product frozen at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Avoid repeatedly freezing and thawing the product.
Purity
The purity of the PRNP protein is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.
Source
E.coli.
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.

Product Science Overview

Introduction

Prion proteins are a unique class of proteins that have garnered significant attention due to their role in neurodegenerative diseases. The term “prion” was first coined by Stanley Prusiner in 1982 to describe “proteinaceous infectious particles” responsible for diseases such as Creutzfeldt-Jakob disease (CJD), scrapie, and kuru . Prion proteins exist in two forms: the normal cellular prion protein (PrP^C) and the disease-causing scrapie prion protein (PrP^Sc).

Structure and Function

The prion protein (PrP) is encoded by the PRNP gene and is primarily expressed in the central and peripheral nervous systems . The normal cellular form, PrP^C, is a cell surface protein that plays a role in various cellular processes, including cell signaling and protection against oxidative stress . However, the exact physiological function of PrP^C remains not fully understood.

Pathogenesis

Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are caused by the conformational conversion of PrP^C into PrP^Sc . This misfolded form is resistant to protease digestion and tends to aggregate, leading to neuronal damage and the characteristic spongiform changes in the brain . The accumulation of PrP^Sc is associated with cell death, inflammation, and neurodegeneration .

Recombinant Prion Protein

Recombinant prion protein (human) is produced using recombinant DNA technology, which involves inserting the human PRNP gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant form is used extensively in research to study the structure, function, and pathogenic mechanisms of prion proteins .

Research and Therapeutic Implications

Research on prion proteins has provided valuable insights into the mechanisms of protein misfolding and aggregation, which are relevant not only to prion diseases but also to other neurodegenerative disorders like Alzheimer’s and Parkinson’s diseases . Understanding the structural features and toxicity of prion proteins can aid in the development of therapeutic strategies to combat these devastating diseases .

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THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
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