The NSMCE2 Antibody (PAC010939) is a high-quality polyclonal antibody designed for research involving NSMCE2, a key protein involved in DNA repair and genome stability. This antibody, raised in rabbits, exhibits high reactivity with human samples and has been validated for use in Western blot applications. By specifically binding to NSMCE2, this antibody enables accurate detection and analysis of the protein in various cell types, making it an essential tool for studies in molecular biology and cancer research.NSMCE2, also known as EID3 (E1A-like inhibitor of differentiation 3), is a crucial component of the SMC5/6 complex, which plays a vital role in maintaining genomic integrity and regulating DNA damage response pathways.
Dysregulation of NSMCE2 has been linked to various human diseases, including cancer and developmental disorders. Therefore, a thorough understanding of NSMCE2 function is essential for advancing research in these fields and developing targeted therapies for related conditions.By utilizing the NSMCE2 Antibody (PAC010939), researchers can accurately investigate the role of NSMCE2 in DNA repair processes, cell cycle regulation, and genome stability. This antibody provides a reliable tool for studying the molecular mechanisms underlying disease development and progression, ultimately leading to the discovery of novel therapeutic interventions in the fields of genetics, oncology, and biomedicine.
non-SMC element 2, MMS21 homolog (S. cerevisiae);NSMCE2;C8orf36;FLJ32440;MMS21;NSE2 ;
UniProt Protein Function:
NSMCE2: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Acts as a E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TRAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair, and for formation of APBs in ALT cell lines. Required for sister chromatid cohesion during prometaphase and mitotic progression. Belongs to the NSE2 family.Protein type: Ubiquitin ligase; SUMO conjugating system; EC 6.-.-.-; EC 6.3.2.-; LigaseChromosomal Location of Human Ortholog: 8q24.13Cellular Component: PML body; chromosome, telomeric region; nucleusMolecular Function: protein binding; zinc ion binding; SUMO ligase activity; ligase activityBiological Process: mitosis; positive regulation of maintenance of mitotic sister chromatid cohesion; protein sumoylation; cell division; telomere maintenance via recombination; positive regulation of mitotic metaphase/anaphase transition; double-strand break repair via homologous recombination; double-strand break repair via nonhomologous end joining
UniProt Protein Details:
NCBI Summary:
This gene encodes a member of a family of E3 small ubiquitin-related modifier (SUMO) ligases that mediates the attachment of a SUMO protein to proteins involved in nuclear transport, transcription, chromosome segregation and DNA repair. The encoded protein is part of the structural maintenance of chromosomes (SMC) 5/6 complex which plays a key role genome maintenance, facilitating chromosome segregation and suppressing mitotic recombination. A knockout of the orthologous mouse gene is lethal prior to embryonic day 10.5. Naturally occurring mutations in this gene, that abolish the SUMO ligase activity, are associated with primordial dwarfism and extreme insulin resistance. [provided by RefSeq, Mar 2017]
