Date published: 2025-9-15

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Psg23 Inhibitors

Psg23 inhibitors are a class of small molecules that specifically target the protein Psg23 (Pregnancy-Specific Glycoprotein 23), which is part of the carcinoembryonic antigen (CEA) family. This family is known for its involvement in various cellular processes such as cell adhesion, signaling, and potentially immune modulation. Psg23 itself is a glycoprotein characterized by its domain structure, including immunoglobulin-like folds, which are common in proteins involved in cell-cell communication. Psg23 inhibitors are designed to disrupt the function of this glycoprotein, typically by binding to its active or allosteric sites, thereby inhibiting its natural interactions. Such inhibition can lead to alterations in the cellular pathways in which Psg23 is involved, making these compounds of significant interest for studying Psg23's biological roles and cellular effects. The specific molecular structure of Psg23 inhibitors varies, but they often feature structural motifs that enable selective binding and high affinity for the Psg23 protein.

These inhibitors are typically characterized by their ability to modulate Psg23's activity at the biochemical level, thereby affecting downstream signaling pathways or cellular processes influenced by Psg23. Structural studies of these molecules reveal key interactions, such as hydrogen bonding, van der Waals forces, and hydrophobic interactions, which allow for the high specificity of binding to Psg23. The chemical diversity within this class allows for the exploration of different modes of inhibition, such as competitive, non-competitive, or irreversible binding. Additionally, Psg23 inhibitors can vary widely in their physicochemical properties, including solubility, stability, and molecular weight, making them versatile tools for probing the biological functions of Psg23 in various experimental settings. The specificity and binding dynamics of these inhibitors make them valuable for understanding Psg23's role in normal cellular processes and the molecular mechanisms by which Psg23 contributes to cellular homeostasis and signaling.

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