SUMO2 (human) (rec.) (Rhodamine 110)
SBB-PS0029-C05050 µgCHF 330.00
Signal to Background: The signal to background ratio was determined by 100% hydrolysis of 200nM, 100nM, 50nM SUMO2-Rhodamine 110 to liberate the quenched conjugate. Assay Buffer: 50mM HEPES pH 7.5, 1mM TCEP, 0.1mg/ml BSA.
|Synonyms||Small Ubiquitin-related Modifier 2; HSMT3; SMT3 Homolog 2; Sentrin-2; Ubiquitin-like Protein SMT3A|
|Sequence||Human SUMO2 (aa1-93) (Accession Nr. P61956) conjugated at the C-terminus to a quenched Rhodamine 110 dye.|
|Application||Protein-based substrate. Typical working concentration range is 50-500nM. Hydrolysis of the conjugate results in fluorescence observable by excitation at 485nm and emission at 535nM.|
|Formulation||Liquid. In 50mM HEPES pH 7.5, 100mM sodium chloride.|
|Other Product Data||
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|Declaration||Manufactured by South Bay Bio.|
|Shipping and Handling|
|Short Term Storage||-80°C|
|Long Term Storage||-80°C|
Aliquot to avoid freeze/thaw cycles.
Protect from light.
|Use/Stability||Stable for at least 1 year after receipt when stored at -80°C.|
|Product Specification Sheet|
SUMO2 is a Ubiquitin-like protein (UBL) that can be covalently attached to proteins as a monomer or as 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 an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451. 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. This SUMO2 substrate is C-terminally derivatized with a bis-Gly-Rhodamine 110 fluorophore. The bis-Gly-Rh110 is quenched until the amide bond between the C-terminal glycine and the rhodamine compound is hydrolyzed. The efficiency of quenching combined with the powerful signal upon hydrolysis yields an unparalleled signal-to-background. SUMO2-Rh110 can be used to study the deSUMOylating activity of hydrolases SENP1 and SENP2, among other deSUMOylating enzymes. The substrate activity of SUMO2-Rhodamine 110 was determined by measuring the SENP1 catalyzed release of unquenched Gly-Rh-110.