Rpp21 Activators
Chemical activators of Rpp21 include a variety of substances that facilitate its ribonuclease function by optimizing the protein's physical and chemical environment. Zinc plays a pivotal role in the activation of Rpp21 by binding to its active site. This binding is necessary for the proper folding and catalytic activity of the protein, as zinc ions are known to be essential for the function of many RNA processing enzymes. Similarly, magnesium chloride contributes magnesium ions that serve as crucial cofactors, directly enhancing the catalytic efficiency of Rpp21. These ions are fundamental to the catalytic activity of ribonucleases, ensuring that Rpp21 operates at its optimal enzymatic capacity.
On the other hand, ammonium sulfate and potassium chloride alter the ionic strength and electrostatic interactions within Rpp21, which are critical for its activity. Ammonium sulfate's role is to promote the proper folding and structural stability necessary for the enzyme's function, while potassium chloride modifies the ionic environment to favor a conformation conducive to enzymatic activity. Sodium acetate and glycerol both stabilize the protein structure, with sodium acetate enhancing the cleavage of RNA by neutralizing its phosphate backbone, and glycerol ensuring the enzyme remains in an active conformation through preferential hydration. Tris buffers the solution to maintain a pH that optimizes Rpp21's activity, while ethylene glycol acts as a crowding agent, influencing the folding and activity of the protein. Dithiothreitol keeps Rpp21 in a reduced state by breaking aberrant disulfide bonds, a condition necessary for its function. Urea, in low concentrations, can expose the active site by denaturing obstructive structures, thereby facilitating catalysis. Imidazole, meanwhile, provides ideal ionic conditions and stabilizes charge distribution at the enzyme's active site. Lastly, sodium chloride supports the protein's structural stability and proper electrostatic interactions, essential for the active conformation of Rpp21.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc can activate Rpp21 by binding to its active site, which is known to require divalent metal ions for its enzymatic function. Zinc's presence is essential for the correct folding and function of many RNA processing enzymes, and it can directly activate the ribonuclease activity of Rpp21. | ||||||
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $27.00 $34.00 $47.00 $123.00 | 2 | |
Magnesium chloride provides magnesium ions, which can activate Rpp21 by serving as a cofactor necessary for its ribonuclease function. Magnesium ions are crucial for the catalytic activity of many ribonucleases, and their presence can directly enhance the catalytic efficiency of Rpp21. | ||||||
Ammonium Sulfate | 7783-20-2 | sc-29085A sc-29085 sc-29085B sc-29085C sc-29085D sc-29085E | 500 g 1 kg 2 kg 5 kg 10 kg 22.95 kg | $10.00 $20.00 $30.00 $40.00 $60.00 $100.00 | 9 | |
Ammonium sulfate, by altering the ionic strength of the solution, can activate Rpp21 by promoting proper folding and stabilization of its tertiary structure, which is necessary for its catalytic activity. By doing so, it can enhance the RNA processing capabilities of Rpp21. | ||||||
Potassium Chloride | 7447-40-7 | sc-203207 sc-203207A sc-203207B sc-203207C | 500 g 2 kg 5 kg 10 kg | $25.00 $56.00 $104.00 $183.00 | 5 | |
Potassium chloride can activate Rpp21 by affecting the ionic environment of the protein, which is critical for its ribonuclease activity. The presence of potassium ions can influence the electrostatic interactions within the Rpp21 structure, promoting a conformation that is favorable for its enzymatic activity. | ||||||
Glycerol | 56-81-5 | sc-29095A sc-29095 | 100 ml 1 L | $55.00 $150.00 | 12 | |
Glycerol can activate Rpp21 by stabilizing its structure through preferential hydration, which can enhance the enzymatic activity of the protein by maintaining it in an active conformation. | ||||||
Ethylene glycol | 107-21-1 | sc-257515 sc-257515A | 500 ml 1 L | $83.00 $118.00 | 1 | |
Ethylene glycol can activate Rpp21 by acting as a crowding agent, which can promote the proper folding and enhance the catalytic activity of the protein. Macromolecular crowding is known to influence the rates of enzymatic reactions by favorably altering the conformational states of proteins. | ||||||
Urea | 57-13-6 | sc-29114 sc-29114A sc-29114B | 1 kg 2 kg 5 kg | $30.00 $42.00 $76.00 | 17 | |
Urea at low concentrations can activate Rpp21 by denaturing inhibitory structures that might be masking the active site, thus exposing the active site for catalysis. Low concentrations of urea have been known to assist in protein refolding and the recovery of enzymatic activity by resolving misfolded intermediates. | ||||||
Imidazole | 288-32-4 | sc-204776 sc-204776A sc-204776B sc-204776C | 25 g 100 g 1 kg 5 kg | $26.00 $55.00 $82.00 $336.00 | 2 | |
Imidazole can activate Rpp21 by providing optimal ionic conditions and acting as a mild buffer that can stabilize the charge distribution on the active site of the enzyme, potentially enhancing its ribonuclease activity. | ||||||
Sodium Chloride | 7647-14-5 | sc-203274 sc-203274A sc-203274B sc-203274C | 500 g 2 kg 5 kg 10 kg | $18.00 $23.00 $35.00 $65.00 | 15 | |
Sodium chloride can activate Rpp21 by influencing the ionic strength and stability of the protein's structure. Optimal ionic conditions are crucial for the activity of Rpp21, and the presence of sodium ions can support the proper electrostatic interactions for the active conformation of the protein. | ||||||