Recombinant human SUMO-2 (Q90P) protein Reference: RP10168LQ SUMO (small Ub-related modifier) is a Ub-like protein. Three types of SUMO are most commonly studied, SUMO 1, SUMO 2, and SUMO 3. SUMO 2 and SUMO 3 are almost identical isoforms and thus share many functions. Like Ub, SUMO can be conjugated to its target proteins as a polymeric chain. However, SUMO 1 forms chains inefficiently as compared to SUMO 2 and SUMO 3. SUMO is conjugated to target proteins by the E1 (SAE1/SAE2), E2 (Ube2I or Ubc9), E3 (RanBP2/Nup358, amongst others). Protein sumoylation is involved in many cellular processes including gene transcription. The SUMO2(Q90P) mutant can still form polySUMO2 chains, but these chains are often resistant to desumolyation.
Recombinant human SUMO-3 protein Reference: RP10170LQ SUMO (small Ub-related modifier) is a Ub-like protein. Three types of SUMO are most commonly studied, SUMO 1, SUMO 2, and SUMO 3. SUMO 2 and SUMO 3 are almost identical isoforms and thus share many functions. Like Ub, SUMO can be conjugated to its target proteins as a polymeric chain. However, SUMO 1 forms chains inefficiently as compared to SUMO 2 and SUMO 3. SUMO is conjugated to target proteins by the E1 (SAE1/SAE2), E2 (Ube2I or Ubc9), E3 (RanBP2/Nup358, amongst others). Protein sumoylation is involved in many cellular processes including gene transcription.
Recombinant human Ubiquitin(K0) protein Reference: RP10176LQ All lysine residues in Ub(K0) were substituted with arginine residues, thereby Ub(K0) can only support monoubiquitination, but not polyubiquitination.
Recombinant human Ubiquitin(K11R) protein Reference: RP10177LQ Ubiquitin (Ub) is a 76 amino acid protein widely expressed in the cytoplasmic and nucleus of cells. Ub is posttranslationally conjugated to proteins by the E1, E2, E3 protein ubiquitination cascade. Ub can be conjugated on proteins as monoUb or polyUb chains. Protein ubiquitination plays both proteolytic and nonproteolytic functions. Usually, polyubiquitinated proteins are targeted to the 26S proteasome for proteolysis. Typical concentration to support in vitro ubiquitination is 50-100 μM. In Ub(K11R), lysine 11 was substituted with an arginine, thereby it cannot form lysine 11-linked polyubiquitin chains.
Recombinant human Ubiquitin(K27R) protein Reference: RP10178LQ Ubiquitin (Ub) is a 76 amino acid protein widely expressed in the cytoplasmic and nucleus of cells. Ub is posttranslationally conjugated to proteins by the E1, E2, E3 protein ubiquitination cascade. Ub can be conjugated on proteins as monoUb or polyUb chains. Protein ubiquitination plays both proteolytic and nonproteolytic functions. Usually, polyubiquitinated proteins are targeted to the 26S proteasome for proteolysis. Typical concentration to support in vitro ubiquitination is 50-100 μM. In Ub(K27R), lysine 27 was substituted with an arginine, thereby it cannot form lysine 27-linked polyubiquitin chains.
Recombinant human Ubiquitin(K29R) protein Reference: RP10179LQ Ubiquitin (Ub) is a 76 amino acid protein widely expressed in the cytoplasmic and nucleus of cells. Ub is posttranslationally conjugated to proteins by the E1, E2, E3 protein ubiquitination cascade. Ub can be conjugated on proteins as monoUb or polyUb chains. Protein ubiquitination plays both proteolytic and nonproteolytic functions. Usually, polyubiquitinated proteins are targeted to the 26S proteasome for proteolysis. Typical concentration to support in vitro ubiquitination is 50-100 μM. In Ub(K29R), lysine 29 was substituted with an arginine, thereby it cannot form lysine 29-linked polyubiquitin chains.
Recombinant human Ubiquitin(K63R) protein Reference: RP10182LQ Ubiquitin (Ub) is a 76 amino acid protein widely expressed in the cytoplasmic and nucleus of cells. Ub is posttranslationally conjugated to proteins by the E1, E2, E3 protein ubiquitination cascade. Ub can be conjugated on proteins as monoUb or polyUb chains. Protein ubiquitination plays both proteolytic and nonproteolytic functions. Usually, polyubiquitinated proteins are targeted to the 26S proteasome for proteolysis. Typical concentration to support in vitro ubiquitination is 50-100 μM. In Ub(K63R), lysine 63 was substituted with an arginine, thereby it cannot form lysine 63-linked polyubiquitin chains.
Recombinant human Ubiquitin(S20C) protein Reference: RP10185LQ Ubiquitin (S20C) bears a single amino acid substitution that replaces serine 20 with a cysteine. This substitution has no effect on Ub’s structure and allows label Ub with other groups, such as biotin or fluorescent groups that are conjugated on a thiol reaction group maleimide.
Recombinant human Ubiquitin(1-75) protein Reference: RP10186LQ Ub75 lacks the amino acid glycine 76, which is required to form thioester bond with Ub activating enzyme E1. Therefore, Ub75 can not react with E1, E2 and E3 enzymes; and does not support ubiquitination. It can be used as a negative control in ubiquitination reactions; or to assay binding of Ub with Ub binding proteins or ubiquitination enzymes.
Recombinant human Ubiquitin thioesterase L1/UCHL1 protein Reference: RP10187LQ Deubiquitinating enzymes (DUBs) are proteases that posses the ability to cleave ubiquitin chains or the isopeptide bond that conjugates ubiquitin with a substrate. Human cells have approximately 100 DUBs that play important roles in regulating various cellular events. UCHL1 is one of the four members of the ubiquitin C-terminal hydrolase (UCH) family. It is thought to be mainly involved in cleaving proubiquitin proteins into monomeric ubiquitin.
Recombinant human Ubiquitin thioesterase L3/UCHL3 protein Reference: RP10188LQ Ubiquitin C-terminal hydrolase L3 (UchL3) is a deubiquitinase enzyme (DUB), which performs hydrolysis of the bond at the C terminus of the ubiquitin and trims down the polyubiquitin chain into monomers. UchL3 has been found to also process a ubiquitin-like substrate called NEDD8. It is 52% identical to the amino acid sequence of its related DUB, UchL1, and may share roles in maintaining neurons of the gracile tract in mice.
26S proteasome Reference: RP10189TLQ The 26S proteasome is an approximately 2.5 mDa large complex composed of the 20S proteasome and the 19S regulatory particle (also called PA700 in mammals). The 20S proteasome has 28 subunits that form a barrel – shaped structure arranged as four heptomeric ring of αββα. Three β subunits have peptidase activities that hydrolyze proteins. Either one or both ends of the 20S proteasome can associate with PA700 to form the 26S proteasome. PA700 contains 19 different proteins that have the ability to bind, deubiquitinate and unfold polyubiquitinated proteins with the consumption of ATP hydrolysis. The 26S proteasome degrades polyubiquitinated proteins, which plays essential roles in regulating various cellular events including protein quality control, gene transcription and signal transduction.