Date published: 2025-9-15

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C4ST-3 Activators

Carbohydrate (chondroitin 4) sulfotransferase 3 (C4ST-3) is an enzyme that plays a critical role in the modification of chondroitin sulfate, a key component of the extracellular matrix. The activity of C4ST-3 is pivotal in the sulfation process, which confers specific biological functions on chondroitin sulfate, including its interaction with various proteins and its contribution to the structural integrity of the cellular environment. The expression of C4ST-3 is regulated by a complex network of cellular signals, and its induction is tightly controlled to maintain cellular and tissue homeostasis. Understanding which molecules can induce the expression of C4ST-3 is of significant interest in the field of biochemistry and molecular biology, as these molecules can be crucial for modulating the extracellular matrix's composition and function in various biological contexts.

Several chemical compounds have been identified that can potentially act as activators to induce the expression of C4ST-3. Retinoic acid, for example, is known to play a role in cell differentiation and development and may have a role in promoting C4ST-3 expression to facilitate extracellular matrix maturation. Similarly, Dexamethasone, a glucocorticoid, could influence the expression of C4ST-3 as part of the cellular response to inflammation. Compounds like Forskolin and Phorbol 12-myristate 13-acetate (PMA) exert their effects by activating intracellular signaling cascades that can lead to increased expression of a variety of genes, including those involved in the biosynthesis of sulfated glycosaminoglycans. Moreover, epigenetic modifiers such as Sodium Butyrate and Trichostatin A (TSA), which affect chromatin structure and gene accessibility, could also play a significant role in upregulating C4ST-3 expression by altering the transcriptional landscape. These activators, among others, highlight the diverse array of molecules that can influence the expression of C4ST-3, reflecting the intricate regulation of this enzyme in the context of cellular function and extracellular matrix dynamics.

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