Recombinant human K48-Ub4 protein Reference: RP10144LQ Ub chains are formed by conjugating the C-terminal glycine residue of Ub onto any of seven internal lysine residues or the amino group of the previous Ub. Ub chains are classified by the lysine residue used to link Ubs; different Ub chain topologies can result in different signals. For instance, Ub chains linked through lysine 6, 11, 27, 29, 33 and 48 are capable of targeting proteins for proteasomal degradation; in contrast, Ub chains linked through lysine 63 or the N-terminal amino group (linear Ub chains) often play important nonproteolytic functions including regulation of kinase activation and protein translation. All Ub chain products are produced by using of human wild type Ub reacting with specific E2s.
Recombinant human K63-Ub(2-12) protein Reference: RP10146LQ Ub chains are formed by conjugating the C-terminal glycine residue of Ub onto any of seven internal lysine residues or the amino group of the previous Ub. Ub chains are classified by the lysine residue used to link Ubs; different Ub chain topologies can result in different signals. For instance, Ub chains linked through lysine 6, 11, 27, 29, 33 and 48 are capable of targeting proteins for proteasomal degradation; in contrast, Ub chains linked through lysine 63 or the N-terminal amino group (linear Ub chains) often play important nonproteolytic functions including regulation of kinase activation and protein translation. All Ub chain products are produced by using of human wild type Ub reacting with specific E2s.
Recombinant human K63-Ub2 protein Reference: RP10147LQ Ub chains are formed by conjugating the C-terminal glycine residue of Ub onto any of seven internal lysine residues or the amino group of the previous Ub. Ub chains are classified by the lysine residue used to link Ubs; different Ub chain topologies can result in different signals. For instance, Ub chains linked through lysine 6, 11, 27, 29, 33 and 48 are capable of targeting proteins for proteasomal degradation; in contrast, Ub chains linked through lysine 63 or the N-terminal amino group (linear Ub chains) often play important nonproteolytic functions including regulation of kinase activation and protein translation. All Ub chain products are produced by using of human wild type Ub reacting with specific E2s.
Recombinant human Linear Ub2 protein Reference: RP10152LQ The linear ubiquitin chains are formed by conjugating the N-terminal methionine residue of one ubiquitin with the C-teminal glycine residue of another ubiquitin. This product is expressed in E. coli as a fusion protein.
Recombinant human Non-cleavable Linear Ub6 protein 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.
Recombinant human Non-cleavable SUMO-2 Chain (2-6) protein Reference: RP10157LQ Non-cleavable SUMO2 chains are made of the SUMO2(Q90P) mutant, this substitution makes the formed polySUMO chains to be resistant to SENP proteases.
Recombinant human Ubiquitin thioesterase OTUB1 protein 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.
Recombinant human Ubiquitin thioesterase OTUB2 protein 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.
Recombinant human Ubiquitin thioesterase OTU1 protein 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.
Recombinant human Deubiquitinase OTUD6B protein 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.
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.