Date published: 2025-9-15

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copine 7 Activators

A23187 directly augments the cellular calcium levels, creating an environment conducive to copine 7 activation by facilitating its association with cellular membranes. Thapsigargin and Cyclopiazonic Acid, by inhibiting the calcium pumps of the endoplasmic reticulum, also engender a rise in cytosolic calcium, thereby indirectly initiating copine 7's activity. Further nuanced control of copine 7 is exerted through the modulation of calcium signaling pathways. Ionmycin serves as a vehicle to transport calcium ions across biological membranes, elevating the ion concentration to activate copine 7. Conversely, BAPTA-AM provides a buffering effect, subtly modulating the calcium landscape within the cell, impacting copine 7's state of activation.

The phosphorylation state within the cell is another determinant for copine 7 activation, with several activators targeting this process. Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C, a key player in phosphorylation signaling that could modify the activity and regulation of copine 7. Calyculin A and Okadaic Acid, phosphatase inhibitors, disrupt the delicate balance of phosphorylation within the cell, potentially affecting the proteins in copine 7's regulatory network. Similarly, Dibutyryl-cAMP, a cAMP analog, exerts its effects by activating protein kinase A, which can cascade down to pathways involving copine 7. Other activators such as KN-93, Nimodipine, and Ryanodine offer insights into the intricacies of copine 7 regulation through their targeted actions on kinases and calcium channels. KN-93's inhibition of calcium/calmodulin-dependent protein kinase II alters the signaling milieu, which could modulate copine 7 activation. Nimodipine, by blocking specific calcium channels, and Ryanodine, by modulating calcium release from the sarcoplasmic reticulum, further contribute to the elaborate regulation of calcium dynamics, thereby influencing copine 7 activity.

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