LSM12 Human

LSM12 is characterized by the presence of the Sm sequence motif, which consists of two regions separated by a linker of variable length that folds into a loop . This motif is essential for the formation of stable heteromeric complexes that are part of the tri-snRNP particles . These particles are significant for the splicing process, ensuring the accurate removal of introns and the joining of exons to form mature mRNA .

The recombinant form of LSM12 is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-195 a.a.) with a molecular mass of 24.1 kDa . It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques .

LSM12 plays a critical role in the splicing of pre-mRNA, a process essential for the proper expression of genes . By associating with U6 snRNA, LSM12 helps maintain the stability and function of the spliceosome . This association is vital for the accurate and efficient removal of introns, which is necessary for the production of functional mRNA and, consequently, the synthesis of proteins .

The recombinant form of LSM12 is widely used in research to study the mechanisms of RNA splicing and the role of snRNPs in gene expression . It is also utilized in structural studies to understand the interactions between LSM12 and other components of the spliceosome . Additionally, LSM12 can be used in assays to investigate the effects of mutations or modifications on its function and stability .

The LSM12 protein solution is formulated in a buffer containing 20mM Tris-HCl (pH 7.5), 0.1M NaCl, 10% glycerol, and 1mM DTT . It should be stored at 4°C if used within 2-4 weeks or frozen at -20°C for longer periods . For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA) to prevent degradation . Multiple freeze-thaw cycles should be avoided to maintain the protein’s integrity .