SUMO1 (human) (rec.) (Rhodamine 110)
|Synonyms||Small Ubiquitin-related Modifier 1; GAP-modifying Protein 1; SMT3C, SMT3H3, UBL1; Sentrin; Ubiquitin-homology Domain Protein PIC1|
|Sequence||Human SUMO1 (aa1-97) (Accession Nr. P63165) 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||
Click here for a Typical Lot-specific Product Datasheet from the Original Manufacturer
Our product description may differ slightly from the original manufacturers product datasheet.
|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|
SUMO1 is a 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. This SUMO1 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 bis-Gly-Rh110 compound is hydrolyzed to mono-Gly-Rhodamine 110. The efficiency of quenching combined with the powerful signal upon hydrolysis yields a reagent with unparalleled signal-to-background. SUMO1-Rh110 can be used to study the deSUMOylating activity of hydrolases SENP1 and SENP2, or other deSUMOylating enzymes. The substrate activity of SUMO1-Rhodamine 110 was determined by measuring the SENP1 catalyzed release of unquenched mono-Gly-Rh110.