ZNF550 can influence the functionality of this protein through various biochemical interactions and signaling pathways. Zinc ions are fundamental for the structural integrity of ZNF550, as they bind directly to the zinc finger domains, which are crucial for the protein's DNA-binding activity. This direct binding can lead to the proper folding and functional activation of ZNF550, allowing it to interact with DNA as intended. Similarly, magnesium ions contribute to the activation of ZNF550 by maintaining the structural stability of the protein, thus enhancing its DNA-binding capabilities. Other metal ions like nickel, cobalt, and copper can substitute for zinc in the protein's finger motifs. This substitution can induce a conformational change in ZNF550 that may activate its DNA-binding activity. Even cadmium, which often plays an inhibitory role, can under certain conditions mimic the activation usually provided by zinc, inducing a DNA-binding-competent conformation.
Sodium orthovanadate acts as a phosphatase inhibitor and can lead to the accumulation of phosphorylated ZNF550, which is the active form of the protein. Forskolin, known to elevate intracellular cAMP levels, indirectly can activate ZNF550 through the activation of protein kinase A (PKA). PKA can phosphorylate ZNF550, resulting in its activation. Ionomycin, by increasing intracellular calcium levels, can lead to the activation of calmodulin-dependent kinases, which may phosphorylate and thus activate ZNF550. Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), which may also target ZNF550 for phosphorylation, altering its conformation and enhancing its activity. The addition of epidermal growth factor (EGF) activates its receptor and the downstream MAPK/ERK signaling pathway, which might include the phosphorylation of ZNF550, leading to its activation. Lastly, dibutyryl-cAMP, a stable cAMP analog, can activate PKA, which, in turn, is capable of phosphorylating ZNF550, ensuring its functional activation within the cellular context. These chemical interactions collectively contribute to the active state of ZNF550 by promoting changes that favor its DNA-binding function and overall cellular role.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc ions can activate ZNF550 by binding directly to the zinc finger domains of the protein, which are known to require zinc for proper folding and function, leading to the activation of its DNA-binding activity. | ||||||
Cobalt(II) chloride | 7646-79-9 | sc-252623 sc-252623A | 5 g 100 g | $63.00 $173.00 | 7 | |
Cobalt ions can replace zinc in zinc finger domains, which may activate ZNF550 by inducing a conformational change that promotes DNA binding activity. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $45.00 $120.00 $185.00 | 3 | |
Copper ions can bind to zinc finger proteins like ZNF550, potentially activating the protein by changing its conformation to a DNA-binding-competent state. | ||||||
Cadmium chloride, anhydrous | 10108-64-2 | sc-252533 sc-252533A sc-252533B | 10 g 50 g 500 g | $55.00 $179.00 $345.00 | 1 | |
Cadmium can bind to zinc fingers, and although it is often inhibitory, certain conditions might allow cadmium to mimic zinc's activatory role in ZNF550, inducing a conformation that activates DNA binding. | ||||||
Sodium Orthovanadate | 13721-39-6 | sc-3540 sc-3540B sc-3540A | 5 g 10 g 50 g | $45.00 $56.00 $183.00 | 142 | |
Sodium orthovanadate is a phosphatase inhibitor and could activate ZNF550 by inhibiting phosphatases that dephosphorylate the protein, which can lead to an increase in the phosphorylated, and active, form of ZNF550. | ||||||
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $76.00 $150.00 $725.00 $1385.00 $2050.00 | 73 | |
Forskolin activates adenylate cyclase, increasing cAMP levels, which could lead to the activation of PKA; PKA phosphorylates various proteins, potentially including ZNF550, resulting in its activation. | ||||||
Ionomycin, free acid | 56092-81-0 | sc-263405 sc-263405A | 1 mg 5 mg | $94.00 $259.00 | 2 | |
Ionomycin increases intracellular calcium levels which can activate calmodulin-dependent kinases; these kinases could phosphorylate and activate ZNF550. | ||||||
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $40.00 $129.00 $210.00 $490.00 $929.00 | 119 | |
PMA activates protein kinase C (PKC) which may phosphorylate ZNF550, leading to its functional activation due to change in protein conformation or interaction with other molecules. | ||||||
Dibutyryl-cAMP | 16980-89-5 | sc-201567 sc-201567A sc-201567B sc-201567C | 20 mg 100 mg 500 mg 10 g | $45.00 $130.00 $480.00 $4450.00 | 74 | |
Dibutyryl-cAMP, a cAMP analog, activates PKA; the activated PKA may then phosphorylate ZNF550, leading to its functional activation within the cell. | ||||||