SNRNP48 Activators
Chemical activators of SNRNP48 play a pivotal role in the splicing of pre-mRNA within the spliceosome complex. Adenosine Triphosphate (ATP) is crucial as it directly activates SNRNP48 by providing the energy necessary for spliceosome assembly and the splicing process. The hydrolysis of ATP leads to conformational changes that enable SNRNP48 to participate effectively in the splicing of pre-mRNA. Concurrently, magnesium chloride serves as a necessary cofactor, facilitating the correct folding of the spliceosome complex and thereby ensuring the functional competence of SNRNP48. Ammonium sulfate aids in this process by precipitating proteins, which can include SNRNP48, thus indirectly contributing to its proper folding and assembly into the spliceosome complex.
Further contributing to the activation of SNRNP48, sodium chloride and potassium chloride adjust the ionic environment, which is essential for maintaining the structural integrity of snRNP particles, including SNRNP48. This ionic balance ensures that SNRNP48 remains in a state conducive to its activation and function within the spliceosome. Heparin plays a similar supportive role by binding to and stabilizing SNRNP48, thus maintaining the spliceosome's structure for efficient splicing activity. Zinc chloride, acting as a structural cofactor, may stabilize the spliceosome formation, assisting in the activation of SNRNP48 by promoting its proper conformation for splicing activity. In parallel, calcium chloride impacts ionic strength and stability of spliceosome components, ensuring the preservation of snRNP integrity which includes the activation state of SNRNP48. The proper conformation and activation of SNRNP48 can also be supported by the use of urea in controlled denaturing and refolding processes, glycerol as a stabilizing agent in protein solutions, and dithiothreitol (DTT) which facilitates proper folding through the reduction of disulfide bonds. Lastly, ethylene glycol, as a crowding agent, can promote the necessary protein-protein interactions within the spliceosome complex, which is essential for the activation and function of SNRNP48.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Adenosine 5′-Triphosphate, disodium salt | 987-65-5 | sc-202040 sc-202040A | 1 g 5 g | $39.00 $75.00 | 9 | |
Adenosine triphosphate (ATP) directly activates SNRNP48 as part of the spliceosome complex, where hydrolysis of ATP is required for spliceosome assembly and the splicing of pre-mRNA, leading to the functional activation of SNRNP48 in the splicing process. | ||||||
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $28.00 $35.00 $48.00 $125.00 | 2 | |
Magnesium chloride acts as a cofactor that is required for the proper folding and function of the spliceosome complex, thereby supporting the activation of SNRNP48 in its role in mRNA splicing. | ||||||
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 | $11.00 $21.00 $31.00 $41.00 $61.00 $102.00 | 9 | |
Ammonium sulfate is used to facilitate protein precipitation and purify proteins, including SNRNP48, which can indirectly ensure its proper folding and assembly into the spliceosome complex, leading to its activation. | ||||||
Sodium Chloride | 7647-14-5 | sc-203274 sc-203274A sc-203274B sc-203274C | 500 g 2 kg 5 kg 10 kg | $19.00 $30.00 $60.00 $110.00 | 15 | |
Sodium chloride at specific concentrations can influence the ionic environment and stabilize the snRNP particles, among them SNRNP48, thus indirectly promoting its activation by maintaining the structural integrity required for its function in mRNA processing. | ||||||
Potassium Chloride | 7447-40-7 | sc-203207 sc-203207A sc-203207B sc-203207C | 500 g 2 kg 5 kg 10 kg | $55.00 $155.00 $285.00 $455.00 | 5 | |
Potassium chloride adjusts the ionic strength in the cellular environment, which is essential for the stability and function of SNRNP complexes, including SNRNP48, hence indirectly promoting its activation and proper functioning within the spliceosome complex. | ||||||
Heparin | 9005-49-6 | sc-507344 | 25 mg | $119.00 | 1 | |
Heparin binds to and stabilizes snRNPs, including SNRNP48, within the spliceosome complex, which can lead to the indirect activation of SNRNP48 by maintaining the complex's structure for efficient splicing activity. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc chloride can act as a structural cofactor for the spliceosome, where it may stabilize the formation of the spliceosome complex and indirectly activate SNRNP48 by promoting its proper structural conformation for splicing activity. | ||||||
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $66.00 $262.00 | 1 | |
Calcium chloride influences the overall ionic strength and stability of spliceosome components, which can indirectly activate SNRNP48 by ensuring the preservation of snRNP integrity and function during the splicing process. | ||||||
Urea | 57-13-6 | sc-29114 sc-29114A sc-29114B | 1 kg 2 kg 5 kg | $31.00 $43.00 $78.00 | 17 | |
Urea is used to denature and refold proteins. When used in controlled conditions, it can promote the correct refolding of SNRNP48, indirectly activating it by allowing it to regain its functional conformation within the spliceosome complex. | ||||||
Glycerol | 56-81-5 | sc-29095A sc-29095 | 100 ml 1 L | $56.00 $153.00 | 12 | |
Glycerol is used as a stabilizing agent in protein solutions, which can help maintain the structural integrity and function of SNRNP48, indirectly leading to its activation by preserving its functional state within the spliceosome. | ||||||