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Small Ubiquitin-like Modifiers Negative Control Peptide Substrate

Chemical

1.53kDa

≥90% (HPLC)

White lyophilized powder.

Soluble in water or other aqueous buffers (5mg/ml).

Lyophilized from a 0.2 μm filtered solution in Acetic Acid.

Multi-species

Manufactured by Boston Biochem

Use: Negative control and contains a scrambled version of the consensus motif sequence. It will not be conjugated to SUMO-1, SUMO-2 or SUMO-3 proteins in the presence of the E1 activating (SAE1/SAE2) and UbcH9 conjugating enzymes. The biotin group allows for sensitive and convenient detection using avidin-linked reagents. Add stock to in vitro or in vivo assays at desired concentration. Recommended concentration range is 50-100μM depending on conditions.

AMBIENT

+4°C

-20°C

Aliquot to avoid freeze/thaw cycles.

Stable for at least 1 year after receipt when stored at -20°C.

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Small ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation. There are four known SUMOs (SUMO1-4). All SUMO proteins share a conserved ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following cleavage of a C-terminal prosegment, the C-terminal glycine residue of SUMO is enzymatically attached to a lysine residue on a target protein. In humans, SUMO is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme. In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p. SUMOylation can occur without the requirement of a specific SUMO ligase (E3), where SUMO is transferred directly from UBE2I/Ubc9 to specific substrates. Unlike SUMO1, which is usually conjugated to proteins as a monomer, SUMO2 and SUMO3 are known to form high molecular weight polymers on proteins. SUMO precursor processing and deconjugation are catalyzed by a family of cysteine proteases known as SUMO-specific proteases (SENPs) and DeSUMOylating Isopeptidase 1.