Recombinant Human SUMO2 (N-6His)

产品介绍

{"gui_ge":"10ug","biao_da_su_zhu":"E.coli","biao_qian":"N-6His","fen_zi_liang":"13 KDa","biao_guan_fen_zi_liang":"17 KDa, reducing conditions","xing_tai":"Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.","chun_du":"Greater than 95% as determined by reducing SDS-PAGE.","nei_du_su_shui_ping":"Less than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.","rong_jie_fang_fa":"Always centrifuge tubes before opening.Do not mix by vortex or pipetting.\nIt is not recommended to reconstitute to a concentration less than 100μg\/ml.\nDissolve the lyophilized protein in distilled water.\nPlease aliquot the reconstituted solution to minimize freeze-thaw cycles. ","chu_cun_fang_fa":"Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.\nReconstituted protein solution can be stored at 4-7°C for 2-7 days.\nAliquots of reconstituted samples are stable at < -20°C for 3 months.","yun_shu_tiao_jian":"The product is shipped at ambient temperature.\nUpon receipt, store it immediately at the temperature listed below.","bei_jing_shuo_ming":"Small Ubiquitin-Related Modifier 2 (SUMO2) is an Ubiquitin-like protein that belongs to the ubiquitin family with SUMO subfamily. It is a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. SUMO2 can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptidebond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins."}