Recombinant Mouse Glypican-1/GPC1 Protein (HEK293)，His

Transthyretin (TTR) is a tetrameric protein primarily produced in the liver and is crucial for the transport of thyroxine and retinol-binding protein. It plays a significant role in maintaining thyroid hormone balance and vitamin A metabolism in the human body. However, mutations in the TTR gene can lead to various amyloid diseases, such as familial amyloidotic polyneuropathy and senile systemic amyloidosis, which are characterized by the deposition of misfolded TTR. The study of recombinant TTR proteins has gained momentum due to their potential therapeutic applications, including the development of small molecules that stabilize the tetrameric form of TTR and prevent its misfolding. Moreover, recombinant TTR can be utilized to explore the mechanisms of amyloidogenesis, investigate structure-function relationships, and enhance our understanding of TTR-related pathologies. Current research is focused on elucidating the protein’s folding pathways, identifying stabilizing ligands, and evaluating their implications in drug design. The advancement of recombinant DNA technology has facilitated the expression and purification of TTR in various model systems, enabling high-throughput screening of compounds that may mitigate the aggregation propensity of TTR. With ongoing studies, recombinant TTR represents a promising avenue for effective therapeutic strategies aimed at combating TTR-related diseases and improving patient outcomes.