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Ubiquitin (Ub) or ubiquitin-like proteins (UBLs) carboxyl termini are attached to other proteins, or in some cases lipids, generally through E1-E2-E3 multienzyme cascades. Ubiquitin-conjugating enzymes (E2s) are responsible for transferring Ub/UBLs to substrate proteins and often function with a single or limited number of E3 ligases, although in some cases no E3 is required.
Members of the family of ubiquitin-conjugating enzymes (E2s) are characterized by the presence of a highly conserved ∼150 amino acid residues ubiquitin-conjugating catalytic (UBC) fold. The UBC domains are ~35% conserved among different family members and provide a binding platform for E1s, E3s, and the activated Ub/UBL. Within this domain, a catalytic cysteine is embedded that accepts the activated ATP-activated Ub/UBLs via a covalently thioester bond, prior to interaction with E3 ligases and subsequent substrate conjugation. The majority of Ub/UBLs use particular E2s for conjugation, but in some cases E2s are shared, such as between the ubiquitin and ISG15-conjugation pathways.
The UBE2D1 protein is critical in cellular processes. It accepts ubiquitin from the E1 complex and preferentially catalyzes "Lys-48"-linked polyubiquitination in vitro, demonstrating multifunctionality. It mediates the selective degradation of short-lived and aberrant proteins and is involved in E6/E6-AP-induced ubiquitination of p53/TP53. UBE2D1 Protein, Human (GST) is the recombinant human-derived UBE2D1 protein, expressed by E. coli , with N-GST labeled tag. The total length of UBE2D1 Protein, Human (GST) is 147 a.a., with molecular weight of ~40.0 kDa.
UBE2D3 is able to accept ubiquitin from specific E2 ubiquitin-conjugating enzymes and transfer it to substrates, often promoting its degradation by the proteasome. UBE2D3 Protein, Human is the recombinant human-derived UBE2D3 protein, expressed by E. coli , with tag free. The total length of UBE2D3 Protein, Human is 147 a.a., with molecular weight of ~15.0 kDa.
Ubiquitin/ISG15-Conjugating Enzyme E2 L6; Retinoic Acid-Induced Gene B Protein; RIG-B; UbcH8; Ubiquitin Carrier Protein L6; Ubiquitin-Protein Ligase L6; UBE2L6; UBCH8
Human
E. coli
The UBE2L6 protein plays a key role in cell regulation by catalyzing the covalent attachment of ubiquitin or ISG15 to other proteins. Notably, it plays a role in E6/E6-AP-induced ubiquitination of p53/TP53, a core process in regulating cellular responses to stress and DNA damage. UBE2L6 Protein, Human (His) is the recombinant human-derived UBE2L6 protein, expressed by E. coli , with C-6*His labeled tag. The total length of UBE2L6 Protein, Human (His) is 153 a.a., with molecular weight of ~17.0 kDa.
UBE2A cooperates with the E3 enzyme BRE1 to promote the attachment of ubiquitin to proteins, specifically histone H2B at "Lys-120", forming H2BK120ub1. This modification serves as a tag for transcriptional activation, RNA polymerase II elongation, telomeric silencing, and is critical for the formation of H3K4me and H3K79me. UBE2A Protein, Human (GST-His) is the recombinant human-derived UBE2A protein, expressed by E. coli , with N-6*His, N-GST labeled tag. The total length of UBE2A Protein, Human (GST-His) is 152 a.a., with molecular weight of ~52.0 kDa.
The UBE2G2 protein is an important ubiquitination component that accepts ubiquitin in the E1 complex, catalyzes its covalent attachment to various proteins, and preferentially performs "Lys-48"-linked polyubiquitination. Its specificity in shaping ubiquitin chains emphasizes its role in cellular processes. UBE2G2 Protein, Human (GST) is the recombinant human-derived UBE2G2 protein, expressed by E. coli , with N-GST labeled tag. The total length of UBE2G2 Protein, Human (GST) is 165 a.a., with molecular weight of ~43.0 kDa.
UBE2H Protein, a crucial participant in cellular ubiquitination, transfers ubiquitin from the E1 complex to various proteins, including MAEA of the CTLH E3 ubiquitin-protein ligase complex. Versatile in vitro, UBE2H catalyzes both 'Lys-11'- and 'Lys-48'-linked polyubiquitination, showcasing its involvement in diverse ubiquitin-related processes. Notably, it demonstrates the capability to ubiquitinate histone H2A in vitro. UBE2H Protein, Human (GST) is the recombinant human-derived UBE2H protein, expressed by E. coli, with N-GST labeled tag. The total length of UBE2H Protein, Human (GST) is 183 a.a., with molecular weight of ~50.0 kDa.
The UBE2I protein is a key player in protein sumoylation, accepting the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex. UBE2I cooperates with E3 ligases such as RANBP2, CBX4, and ZNF451 to catalyze the covalent attachment of these SUMO proteins to target proteins, including key substrates FOXL2 and KAT5. UBE2I Protein, Human (GST) is the recombinant human-derived UBE2I protein, expressed by E. coli , with N-GST labeled tag. The total length of UBE2I Protein, Human (GST) is 158 a.a., with molecular weight of ~40.0 kDa.
UBE2K protein is an important component of the ubiquitin-proteasome system and functions as an E2 ubiquitin-conjugating enzyme, which is critical for attaching ubiquitin to different substrates. In vitro, UBE2K catalyzes "Lys-48" linked polyubiquitin chains, specifically in the presence or absence of the BRCA1-BARD1 E3 ligase complex. UBE2K Protein, Human (GST) is the recombinant human-derived UBE2K protein, expressed by E. coli , with N-GST labeled tag.
NEDD8-conjugating enzyme Ubc12; NEDD8 carrier protein; NEDD8 protein ligase; Ubiquitin-conjugating enzyme E2 M; UBC12; UBE2M;
Human
E. coli
UBE2M Protein is a crucial mediator in the ubiquitin-like protein NEDD8 conjugation pathway. It accepts NEDD8 from the UBA3-NAE1 E1 complex, covalently attaching it to target proteins like CUL1, CUL2, CUL3, and CUL4, particularly interacting with the E3 ubiquitin ligase RBX1. This specificity in neddylating specific targets suggests a pivotal role in regulating cellular processes, notably contributing to cell proliferation. UBE2M Protein, Human is the recombinant human-derived UBE2M protein, expressed by E. coli , with tag free. The total length of UBE2M Protein, Human is 183 a.a., with molecular weight of 19-25.0 kDa.
UBE2T Protein, an essential ubiquitination component, serves as an E2 ubiquitin-conjugating enzyme, accepting ubiquitin from the E1 complex and catalyzing its covalent attachment to proteins. This multifaceted enzyme catalyzes monoubiquitination, crucial in MMC-induced DNA repair processes. Its significance is highlighted by specific association with the Fanconi anemia complex, collaborating with FANCL for FANCD2 monoubiquitination in the DNA damage response pathway. Beyond DNA repair, UBE2T mediates monoubiquitination of FANCL and FANCI and potentially contributes to BRCA1 ubiquitination and degradation. In vitro, UBE2T promotes various polyubiquitination types, showcasing involvement in diverse ubiquitin-dependent processes. UBE2T Protein, Human (His) is the recombinant human-derived UBE2T protein, expressed by E. coli, with N-6*His labeled tag. The total length of UBE2T Protein, Human (His) is 197 a.a., with molecular weight of 25-30 kDa.
The UBE2G1 protein is an important participant in the ubiquitin-proteasome system, acting as an E2 ubiquitin-conjugating enzyme to promote the attachment of ubiquitin to different protein substrates. In vitro, UBE2G1 exhibits catalytic ability in “Lys-48” and “Lys-63” linked polyubiquitination reactions. UBE2G1 Protein, Human is the recombinant human-derived UBE2G1 protein, expressed by E. coli , with tag free. The total length of UBE2G1 Protein, Human is 170 a.a., with molecular weight of ~19.5 kDa.
UBE2W protein is a multifunctional ubiquitin-conjugating enzyme that accepts ubiquitin in the E1 complex and catalyzes its covalent attachment to different substrates. Notably, UBE2W uniquely monoubiquitylates the N-terminus, including ATXN3, MAPT/TAU, POLR2H/RPB8, and STUB1/CHIP, showing specificity for disordered N-termini. UBE2W Protein, Human (His) is the recombinant human-derived UBE2W protein, expressed by E. coli , with N-His labeled tag.
The UBE2F protein accepts NEDD8 from the UBA3-NAE1 E1 complex and covalently links it to various target proteins in the ubiquitin-like NEDD8 conjugation pathway. The RBX2-UBE2F complex specifically interacts with the E3 ubiquitin ligase RBX2, but not RBX1, for the neddylation of specific targets, especially CUL5. UBE2F Protein, Human (His, Solution) is the recombinant human-derived UBE2F, expressed by E. coli , with N-6*His labeled tag. ,
The UbcH5b/UBE2D2 protein is an important cellular mediator that accepts ubiquitin from the E1 complex and catalyzes multifunctional “Lys-48”-linked polyubiquitination on target proteins. In addition to its catalytic role, it also concentrates and selectively degrades short-lived proteins and contributes to E6/E6-AP-induced ubiquitination of p53/TP53. UbcH5b/UBE2D2 Protein, Human is the recombinant human-derived UbcH5b/UBE2D2 protein, expressed by E. coli , with tag free. The total length of UbcH5b/UBE2D2 Protein, Human is 147 a.a., with molecular weight of ~16 kDa.
UbcH7/UBE2L3 is a unique ubiquitin-conjugating E2 enzyme that cooperates with HECT-type and RBR family E3 ligases and lacks intrinsic E3-independent reactivity with lysine. It uniquely works with RBR family E3 enzymes such as PRKN, RNF31 and ARIH1, acting like a RING-HECT hybrid. UbcH7/UBE2L3 Protein, Human is the recombinant human-derived UbcH7/UBE2L3 protein, expressed by E. coli , with tag free.
The UBE2B protein is a key ubiquitination factor that acts as an E2 ubiquitin-conjugating enzyme, accepting ubiquitin from the E1 complex and catalyzing covalent attachment to proteins. UBE2B works in conjunction with the BRE1 (RNF20 and/or RNF40) E3 enzyme and plays a key role in transcriptional regulation by catalyzing the monoubiquitination of histone H2B at "Lys-120" (H2BK120ub1). UBE2B Protein, Human (HEK293, His) is the recombinant human-derived UBE2B protein, expressed by HEK293 , with C-6*His labeled tag. The total length of UBE2B Protein, Human (HEK293, His) is 152 a.a., with molecular weight of ~17.0 kDa.
ATG3 Protein, Human is a recombinant human Ubiquitin-like-conjugating Enzyme ATG3 expressed in E. coli. ATG3, the E2 ubiquitin-conjugating enzyme for the LC3 lipidation process, is essential for autophagy.
The UBE2D4 protein is an important ubiquitin-proteasome system component that acts as an E2 ubiquitin-conjugating enzyme, accepting ubiquitin from the E1 complex and catalyzing its covalent attachment to proteins. In vitro, UBE2D4 exhibits multifunctionality by promoting polyubiquitination of all seven ubiquitin Lys residues, possibly favoring polyubiquitination of “Lys-11” and “Lys-48” linkages. UBE2D4 Protein, Human (GST) is the recombinant human-derived UBE2D4 protein, expressed by E. coli , with N-GST labeled tag. The total length of UBE2D4 Protein, Human (GST) is 147 a.a., with molecular weight of ~40.0 kDa.
The UBE2J2 protein plays a crucial role in cellular processes by catalyzing the covalent attachment of ubiquitin to other proteins. Its function is involved in the selective degradation of misfolded membrane proteins extending into the endoplasmic reticulum (ERAD), as suggested by the similarity of related processes. UBE2J2 Protein, Human (GST) is the recombinant human-derived UBE2J2 protein, expressed by E. coli , with N-GST labeled tag.
The UBE2R2 protein is a key element of the ubiquitin-proteasome system and functions as an E2 ubiquitin-conjugating enzyme. It accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to a variety of protein substrates. UBE2R2 Protein, Human (His) is the recombinant human-derived UBE2R2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of UBE2R2 Protein, Human (His) is 238 a.a., with molecular weight of ~37.0 kDa.
