Human SUMO1/SUMO-1 (His Tag) recombinant protein
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases 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. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.
Small ubiquitin-related modifier 1
Protein short names
SMT3H3; DAP1; MGC103203; SUMO1; SUMO-1; SMT3C; GMP1; OK/SW-CL.43; SMT3; SMTP3; OFC10; SENTRIN; SENP2; PIC1; UBL1
SUMO1; SMT3C; SMT3H3; UBL1; OK/SW-cl.43
A DNA sequence encoding the human SUMO1 (AAH66306.1) (Ser 2-Val 101) was expressed, with a polyhistide tag at the N-terminus.
The recombinant human SUMO1 consisting of 107 amino acids and has a calculated molecular mass of 12.4 kDa. It migrates as an 22 kDa band in SDS-PAGE under reducing conditions as predicted.
> 90 % as determined by SDS-PAGE
Measured by its ability to be proteolytically processed by SENP1.
>50% of 1 μg Recombinant Human (rh) SUMO1 is cleaved by < 10 ng of recombinant human SENP.
Human SUMO1 / SUMO-1 Protein (His Tag) SDS-PAGE
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