Recombinant Proteins

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PRNP Human

Prion Protein Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT7001
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PRND Human

Prion Protein 2 Human Recombinant

Recombinant Human PRND, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 149 amino acids (27-152a.a). With a molecular weight of 58.5kDa, it includes a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6902
Source
Escherichia Coli.
Appearance
A clear, sterile solution without any color.
Definition and Classification

Prion proteins are unique infectious agents composed solely of protein material, devoid of nucleic acids. They are responsible for a group of fatal neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). These diseases include Creutzfeldt-Jakob disease in humans, bovine spongiform encephalopathy in cattle, and scrapie in sheep . Prion proteins exist in two forms: the normal cellular prion protein (PrP^C) and the misfolded, disease-causing form (PrP^Sc) .

Biological Properties

Prion proteins are highly conserved across mammalian species, indicating their significant biological roles. They are predominantly expressed in the central and peripheral nervous systems but are also found in other tissues . The cellular prion protein (PrP^C) is anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor and is involved in various cellular processes .

Biological Functions

The primary functions of prion proteins are still under investigation. However, they are known to play roles in:

  • Neuroprotection: PrP^C is involved in protecting neurons from oxidative stress and apoptosis .
  • Cellular Signaling: PrP^C acts as a scaffold protein, facilitating the assembly of signaling modules at the cell surface .
  • Immune Response: Prion proteins are implicated in modulating immune responses and pathogen recognition .
Modes of Action

Prion proteins interact with various molecules and cells through several mechanisms:

  • Binding Partners: PrP^C binds to multiple extracellular and transmembrane ligands, which are essential for its role in signal transduction .
  • Downstream Signaling Cascades: Upon binding to its partners, PrP^C activates downstream signaling pathways that regulate cellular functions such as differentiation, neuroprotection, and immune responses .
Regulatory Mechanisms

The expression and activity of prion proteins are tightly regulated through:

  • Transcriptional Regulation: The Prnp gene, which encodes PrP^C, is regulated by various transcription factors that respond to cellular and environmental cues .
  • Post-Translational Modifications: PrP^C undergoes several post-translational modifications, including glycosylation and the addition of a GPI anchor, which are crucial for its proper localization and function .
Applications

Prion proteins have several applications in biomedical research and therapeutic strategies:

  • Diagnostic Tools: Detection of PrP^Sc is used in diagnosing prion diseases .
  • Therapeutic Strategies: Research is ongoing to develop therapies that target prion proteins to treat prion diseases and other neurodegenerative disorders .
Role in the Life Cycle

Prion proteins play roles throughout the life cycle, from development to aging and disease:

  • Development: PrP^C is involved in neural development and synapse formation .
  • Aging: The misfolding of PrP^C into PrP^Sc is associated with age-related neurodegenerative diseases .
  • Disease: Prion diseases are characterized by the accumulation of PrP^Sc, leading to progressive neuronal damage and death .
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