NSMCE1 Human

NSMCE1 is a protein that consists of 266 amino acids and has a molecular mass of approximately 33 kDa . It is typically produced in E. coli and purified using conventional chromatography techniques . The recombinant form of NSMCE1 often includes a His-tag at the N-terminus to facilitate purification .

The SMC5-SMC6 complex, which includes NSMCE1, is essential for the repair of DNA double-strand breaks. This complex promotes sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to the sites of double-strand breaks . This recruitment is crucial for the accurate repair of DNA and the prevention of genomic instability.

NSMCE1 is also involved in telomere maintenance, particularly in cells that use the alternative lengthening of telomeres (ALT) pathway. In ALT-associated PML bodies (APBs), NSMCE1 mediates the sumoylation of shelterin complex components, leading to the disassembly of the shelterin complex . This process is vital for the maintenance of telomeres and the prevention of chromosomal abnormalities.

In vitro studies have shown that NSMCE1 possesses ubiquitin ligase activity in the presence of NDNL2 . This activity suggests that NSMCE1 may play a role in the regulation of protein degradation and other cellular processes through ubiquitination.

Recombinant NSMCE1 is widely used in research to study its role in DNA repair, telomere maintenance, and protein ubiquitination. It is also used to investigate the mechanisms of genomic stability and the potential therapeutic targets for diseases related to DNA repair deficiencies.

Recombinant NSMCE1 should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain the protein’s stability and functionality .