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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.
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.
UBE2D1 Protein, crucial in cellular processes, accepts ubiquitin from the E1 complex, preferentially catalyzing 'Lys-48'-linked polyubiquitination in vitro, showcasing versatility. It mediates selective degradation of short-lived and aberrant proteins and participates in E6/E6-AP-induced p53/TP53 ubiquitination. UBE2D1 facilitates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6, and TRIM63/MURF1. It ubiquitinates STUB1-associated HSP90AB1 in vitro, highlighting involvement in cellular pathways. Lacking inherent specificity for any ubiquitin lysine residue, UBE2D1's dynamic nature in ubiquitin modification processes is notable. Its essential role in viral activation of IRF3 and mediation of CYP3A4 polyubiquitination emphasizes multifaceted contributions to cellular function. 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.
Ubiquitin-conjugating enzyme E2 D3 (UBE2D3) is an E3 ubiquitin protein ligase. 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.
UBE2G2 Protein, a vital ubiquitination component, accepts ubiquitin from the E1 complex, catalyzing its covalent attachment to various proteins, with a preference for 'Lys-48'-linked polyubiquitination. Its specificity in shaping ubiquitin chains underscores its role in cellular processes. Intricately associated with endoplasmic reticulum-associated degradation (ERAD), UBE2G2 maintains cellular homeostasis by regulating protein turnover. Indispensable for sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase, it facilitates subsequent proteasomal degradation. 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.
UBE2I Protein, a key participant in protein sumoylation, accepts ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4, and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex. Teaming up with E3 ligases like RANBP2, CBX4, and ZNF451, UBE2I catalyzes the covalent attachment of these SUMO proteins to target proteins, including critical substrates FOXL2 and KAT5. Its enzymatic activity extends to forming poly-SUMO chains, influencing diverse cellular processes and playing a pivotal role in specific protein modifications, such as sumoylation of p53/TP53 at 'Lys-386' and ERCC6. 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.
UBE2G1 Protein, a crucial ubiquitin-proteasome system player, acts as an E2 ubiquitin-conjugating enzyme, facilitating ubiquitin attachment to diverse protein substrates. In vitro, UBE2G1 demonstrates catalytic competence in 'Lys-48' and 'Lys-63'-linked polyubiquitination reactions. This multifaceted enzyme is implicated in potential roles, including the degradation of muscle-specific proteins, emphasizing its involvement in cellular processes related to protein turnover. Additionally, UBE2G1 mediates the polyubiquitination of CYP3A4, a cytochrome P450 enzyme, underscoring its significance in regulating specific cellular pathways. 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.
UBE2B Protein, a key ubiquitination player, functions as an E2 ubiquitin-conjugating enzyme, accepting ubiquitin from the E1 complex and catalyzing covalent attachment to proteins. Teaming with BRE1 (RNF20 and/or RNF40) E3 enzyme, UBE2B plays a pivotal role in transcriptional regulation by catalyzing histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). This modification tags various epigenetic processes and is essential for H3K4me and H3K79me formation. UBE2B exhibits versatile ubiquitin chain linkages, mediating 'Lys-11', 'Lys-48', and 'Lys-63'-linked polyubiquitination in vitro. It also plays a crucial role in postreplication repair of UV-damaged DNA, forming the UBE2B-RAD18 ubiquitin ligase complex with RAD18 E3 ligase, which mono-ubiquitinates DNA-associated PCNA on 'Lys-164'. The diverse functions of UBE2B suggest potential involvement in neurite outgrowth. 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.
UBE2D4 Protein, a vital ubiquitin-proteasome system component, acts as an E2 ubiquitin-conjugating enzyme, accepting ubiquitin from the E1 complex and catalyzing its covalent attachment to proteins. In vitro, UBE2D4 demonstrates versatility by promoting polyubiquitination with all seven ubiquitin Lys residues, potentially favoring 'Lys-11' and 'Lys-48'-linked polyubiquitination. This dynamic ubiquitin chain range suggests UBE2D4's involvement in diverse cellular processes and regulatory pathways, highlighting its significance in the intricate network of protein degradation and turnover. 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.
UBE2R2 Protein, a key element in the ubiquitin-proteasome system, operates as an E2 ubiquitin-conjugating enzyme. It accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to diverse protein substrates. In vitro, UBE2R2 displays versatile catalytic activity, facilitating both monoubiquitination and 'Lys-48'-linked polyubiquitination reactions. This implies its potential involvement in various cellular processes, including the targeted degradation of proteins, suggesting a role in the regulation of substrates like katenin. 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.
