Mtrnr2l Activators
Chemical activators of Mtrnr2l can engage in various interactions to enhance the protein's function. Zinc plays a crucial role in maintaining the structural integrity of Mtrnr2l. By binding to the protein, Zinc ions can induce conformational stability, ensuring that Mtrnr2l retains a functional shape that is necessary for its catalytic action. Similarly, Magnesium directly contributes to the protein's conformation and activity. As an essential cofactor, Magnesium ions interact with Mtrnr2l to maintain its structure, enabling the protein to carry out its functions effectively. Manganese(II) sulfate can also serve as a cofactor; the Manganese ions may interact with Mtrnr2l to promote structural changes, thus enhancing its enzymatic activity. Copper(II) sulfate, by facilitating electron transfer through its binding, can further stabilize Mtrnr2l or participate in its catalytic processes. Nickel(II) chloride and Cobalt(II) chloride can mimic these effects, potentially binding to Mtrnr2l and activating the protein by promoting favorable structural configurations.
In addition to the metal ion activators, compounds like Forskolin and Phorbol 12-myristate 13-acetate (PMA) can modulate Mtrnr2l activity through the activation of kinases. Forskolin raises the levels of cAMP within the cell, which in turn activates protein kinase A (PKA). PKA can then phosphorylate Mtrnr2l, leading to a change in its activity state. PMA works through a similar mechanism but targets a different kinase; it activates protein kinase C (PKC), which can also result in the phosphorylation and subsequent activation of Mtrnr2l. Adenosine 5'-triphosphate (ATP) is another critical molecule that supplies the necessary phosphate groups for these phosphorylation events. Sodium orthovanadate can contribute to the activation of Mtrnr2l by inhibiting phosphatases that would otherwise dephosphorylate the protein, thus maintaining its active state. Calcium chloride and Ionomycin, by increasing intracellular calcium levels, can induce further conformational changes that promote the proper folding and function of Mtrnr2l, enabling it to maintain activity within the cellular environment.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc serves as a cofactor for Mtrnr2l, ensuring proper folding and function of the protein. Adequate levels of Zinc can enhance the catalytic activity of Mtrnr2l by stabilizing its structure, thereby directly increasing its functional activity. | ||||||
Manganese(II) sulfate monohydrate | 10034-96-5 | sc-203130 sc-203130A | 100 g 500 g | $41.00 $107.00 | ||
Manganese ions can act as cofactors for many enzymes, including potentially Mtrnr2l. By binding to the protein, Manganese(II) sulfate can activate Mtrnr2l by inducing conformational changes that enhance its enzymatic activity. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $46.00 $122.00 $189.00 | 3 | |
Copper ions can activate proteins by binding to them and facilitating electron transfer, which may enhance the activity of Mtrnr2l by improving its structural stability or by acting directly as a cofactor in its enzymatic function. | ||||||
Nickel(II) chloride | 7718-54-9 | sc-236169 sc-236169A | 100 g 500 g | $68.00 $188.00 | ||
Nickel ions can interact with proteins such as Mtrnr2l, potentially serving as a cofactor and activating the protein by inducing structural changes that promote its activity. | ||||||
Cobalt(II) chloride | 7646-79-9 | sc-252623 sc-252623A | 5 g 100 g | $64.00 $176.00 | 7 | |
Cobalt ions can mimic the effects of other divalent metal ions, potentially binding to Mtrnr2l and activating it by stabilizing its structure or by directly participating in its catalytic processes. | ||||||
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $66.00 $262.00 | 1 | |
Calcium ions are known to play a role in the activation of various proteins by binding to them and inducing conformational changes that lead to activation. Calcium chloride can supply these ions, which may bind to and activate Mtrnr2l by promoting its structural integrity and function. | ||||||
Sodium Orthovanadate | 13721-39-6 | sc-3540 sc-3540B sc-3540A | 5 g 10 g 50 g | $49.00 $57.00 $187.00 | 142 | |
Sodium orthovanadate can inhibit tyrosine phosphatases, which may lead to the activation of signaling pathways that enhance the activity of Mtrnr2l by maintaining its phosphorylated state, a modification that can increase protein activity. | ||||||
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $41.00 $132.00 $214.00 $500.00 $948.00 | 119 | |
PMA activates protein kinase C (PKC), which can phosphorylate a broad range of substrates, possibly including Mtrnr2l. The phosphorylation of Mtrnr2l by PKC can result in its activation. | ||||||
Adenosine 5′-Triphosphate, disodium salt | 987-65-5 | sc-202040 sc-202040A | 1 g 5 g | $39.00 $75.00 | 9 | |
ATP can serve as a substrate for kinases that phosphorylate proteins such as Mtrnr2l, which may lead to its activation by inducing structural changes that enhance its enzymatic activity. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $78.00 $270.00 | 80 | |
Ionomycin is a calcium ionophore that increases intracellular calcium levels, which can activate proteins by inducing conformational changes. This rise in calcium could lead to the activation of Mtrnr2l by promoting its proper folding and functional state. | ||||||