Date published: 2025-9-13

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AI464131 Activators

Chemical activators of the myogenesis regulating glycosidase (putative) can employ a variety of mechanisms to enhance its activity. Forskolin directly stimulates adenylate cyclase, which catalyzes the conversion of ATP to cyclic AMP (cAMP). The rise in cAMP levels results in the activation of protein kinase A (PKA), a kinase that plays a crucial role in phosphorylating proteins that may interact with or directly modify the myogenesis regulating glycosidase (putative), promoting its enzymatic function. Similarly, IBMX elevates intracellular cAMP concentrations by inhibiting phosphodiesterases that degrade cAMP, which also leads to PKA activation and subsequent phosphorylation of proteins associated with the glycosidase. Piceatannol disrupts the action of Syk kinases, altering the phosphorylation states of proteins that modulate the glycosidase's activity, while sodium fluoride acts by inhibiting phosphatases, thereby maintaining a higher level of phosphorylation within the cell, which can indirectly facilitate the glycosidase's activity.

Further activation mechanisms involve okadaic acid and cantharidin, both inhibitors of protein phosphatases PP1 and PP2A. The inhibition of these phosphatases prevents the dephosphorylation of proteins, ensuring that the phosphorylation state remains high, which can lead to activation of the myogenesis regulating glycosidase (putative). Anisomycin activates stress-activated protein kinases (SAPKs), which may phosphorylate and activate proteins associated with the glycosidase. A23187, by increasing intracellular calcium levels, can activate calcium-dependent protein kinases that potentially phosphorylate the glycosidase or its associated proteins. Phorbol 12-myristate 13-acetate (PMA) stimulates protein kinase C (PKC), which is known to phosphorylate a wide array of proteins, possibly including those interacting with the glycosidase. Retinoic acid modulates gene expression and might activate signaling pathways that lead to the activation of the glycosidase. Lastly, zinc chloride and manganese (II) chloride can enhance the glycosidase's activity by serving as cofactors that stabilize the enzyme's structure or by activating kinases that phosphorylate proteins which regulate the activity of the glycosidase.

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