Recombinant human Polyubiquitinated UbE2S protein Reference: RP10164LQ Polyubiquitinated UbE2S (Ubn (K11-linked)-UbE2S) is a polyubiquitinated substrate in which various K11-linked polyUb chains were conjugated on the Ub conjugating enzyme UbE2S. It can be used as a substrate to monitor deubiquitination mediated by deubiquitinating enzymes, or to determine binding of K11-linked polyUb chains by proteins that have Ub interacting domains.
Recombinant human 26S proteasome non-ATPase regulatory subunit 4/S5A/PSMD4... Reference: RP10165LQ S5a is one of the integral Ub receptors of the 26S proteasome. It’s N-terminal vWA domain interacts with Rpn9 and Rpn10 on the 26S proteasome. The C-terminal domain of S5a contains two Ub-interacting motifs (UIMs) that bind Ub and Ub chains. S5a prefers to bind polyUb chains; it also binds proteins containing a Ub-like domain. It may directly recognize ubiquitinated proteins or coordinate with other Ub receptors to target substrates for proteasomal degradation.
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.