STYX Human (26-223)

Serine/Threonine/Tyrosine Interacting Protein (STYX) is a unique and intriguing protein that plays a significant role in cellular signaling pathways. The specific fragment of STYX, spanning amino acids 26 to 223, has been studied extensively for its interactions and functions. This article delves into the background, structure, and significance of this recombinant human protein.

The Serine/Threonine/Tyrosine Interacting Protein (26-223 a.a.) is a fragment of the full-length STYX protein. This fragment is expressed in Escherichia coli and is purified to a high degree of purity, typically greater than 85% . The recombinant protein is tagged with a His tag at the N-terminus, which facilitates its purification and detection in various experimental applications .

STYX is classified as an inactive tyrosine-protein phosphatase. Despite its lack of catalytic activity, it plays a crucial role in cellular signaling by interacting with phosphorylated serine, threonine, and tyrosine residues on target proteins . These interactions are vital for regulating various cellular processes, including cell growth, differentiation, and apoptosis.

The 26-223 amino acid fragment of STYX retains the protein’s ability to interact with phosphorylated residues, making it a valuable tool for studying protein-protein interactions and signaling pathways in a controlled experimental setting .

The recombinant human STYX protein (26-223 a.a.) is widely used in research for several applications:

• SDS-PAGE: The protein’s purity and molecular weight can be analyzed using SDS-PAGE, a common technique for protein separation and characterization .
• Mass Spectrometry (MS): The protein can be used as a standard or reference in mass spectrometry experiments to identify and quantify other proteins in complex mixtures .