TSEN15 Human
tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.
Description
TSEN15 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids (1-171 a.a.) and having a molecular mass of 20.9kDa.
The TSEN15 is purified by proprietary chromatographic techniques.
Product Specs
tRNA-splicing endonuclease subunit Sen15 (TSEN15) plays a vital role in cell growth and division as a part of the tRNA splicing mechanism. The TSEN15 protein is a subunit of the tRNA splicing endonuclease, responsible for cleaving pre-tRNA at the 5' and 3' splice sites, ultimately releasing the intron.
Recombinant Human TSEN15, expressed in E. coli, is a purified protein with a His tag (20 amino acids) attached to its N-terminus. This single, non-glycosylated polypeptide chain is 191 amino acids long (including amino acids 1-171) with a molecular weight of 20.9 kDa. The protein purification process utilizes proprietary chromatographic methods.
The TSEN15 protein solution is provided at a concentration of 0.5 mg/ml and contains the following components: 20mM Tris-HCl buffer at a pH of 8.0, 2mM DTT, 20% glycerol, and 200mM NaCl.
For short-term storage (2-4 weeks), the TSEN15 solution should be kept refrigerated at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To ensure long-term stability, consider adding a carrier protein (0.1% HSA or BSA) before freezing. Repeated freezing and thawing of the solution should be avoided.
tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.
Product Science Overview
tRNA Splicing Endonuclease 15 (TSEN15) is a crucial subunit of the tRNA splicing endonuclease (TSEN) complex, which plays an essential role in the maturation of transfer RNAs (tRNAs). tRNAs are vital for the translation of mRNA into proteins, a fundamental process in cellular biology. The TSEN complex is responsible for the removal of introns from pre-tRNA transcripts, a critical step in the maturation of tRNAs in eukaryotic cells.
The human TSEN complex is composed of four core subunits: TSEN54, TSEN2, TSEN34, and TSEN15 . Each subunit has a specific function in the splicing process. TSEN15, in particular, is involved in the cleavage of pre-tRNA at the 5’ and 3’ splice sites to release the intron . The complex also co-purifies with the polynucleotide kinase CLP1, although the exact role of CLP1 in tRNA splicing remains unclear .
The TSEN complex catalyzes the removal of introns from pre-tRNA transcripts. TSEN2 and TSEN34 are metal ion-independent nucleases that cleave the 5’ and 3’ splice sites, respectively, generating the 5’ exon with a 2’3’-cyclic phosphate and the 3’ exon with a 5’-hydroxyl group . This process is essential for the proper maturation and functionality of tRNAs, which are necessary for protein synthesis.
Recombinant human TSEN15 protein, fused to a His-tag at the N-terminus, has been successfully expressed in E. coli and purified using conventional chromatography techniques . This recombinant system allows for the production of active TSEN complexes, which are essential for studying the function and regulation of tRNA splicing in vitro.
Mutations in genes encoding the TSEN subunits, including TSEN15, have been linked to neurodegenerative disorders . Understanding the mechanisms underlying these disorders is crucial for developing potential therapeutic strategies. The recombinant production of TSEN15 and other subunits provides valuable tools for investigating the molecular basis of these diseases.
