Category: Proteins & Peptides

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Reference: RP10156LQ

Non-cleavable linear Ub6 was a derivative of 6xHis-non-cleavable linear Ub6 by removal of the N-terminal 6xHis and 3xHA tags using TEV digestion. The G76V substitution was introduced in the first five Ub moieties and the last Ub has G76.

Reference: RP10158LQ

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. OTUB1 is a member of the ovarian tumor domain family. It is recognized as a K48 ubiquitin chain-specific DUB and can inhibit E2 enzymes, especially Ubc13 (also known as Ube2N), which is known to synthesize K63-linked ubiquitin chains. OTUB1 may also deubiquitinate TRAF3 and -6. This would negatively regulate virus-triggered type I IFN induction.

Reference: RP10159LQ

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. OTUB2 is a member of the ovarian tumor domain family. Not much is known about the biological function of this enzyme, but it may deubiquitinate TRAF3 and -6. This would negatively regulate virus-triggered type I IFN induction.

Reference: RP10160LQ

OTUD2 belongs to the OTU (ovarian tumour) family of deubiquitinating enzymes. OTUD2 cleaves K-11, 27, 29 0r 33-linked polyubiquitin chains. It could be involved in regulating endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins.

Reference: RP10161LQ

OTUD6B belongs to the OTU (ovarian tumour) family of deubiquitinating enzymes. Functions of this enzyme are not clear. In vitro, purified OTUD6B has not activity for cleavage of various di-Ub chains.

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.

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.

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.

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.

Reference: RP10176LQ

All lysine residues in Ub(K0) were substituted with arginine residues, thereby Ub(K0) can only support monoubiquitination, but not polyubiquitination.

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.