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Ubiquitination is a tightly controlled three-step multienzyme cascades. A ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3) act in a concerted manner to form a covalent bond between ubiquitin and its substrate protein, and thereby write the ubiquitin code. In detail, this process is initiated by a family of mechanistically and structurally-related E1 enzymes. The E1s serve to activate ubiquitin/UBLs through C-terminal adenylation and thiol transfer and to coordinate the utilization of ubiquitin/UBLs in specific downstream pathways by charging cognate E2 enzymes, which then interact with the downstream ubiquitylation machinery to coordinate modification of the target.
XIAP protein is a multifunctional regulator that controls apoptosis, inflammation, immunity, copper homeostasis, and various signaling pathways. As a caspase inhibitor, it blocks CASP3 and CASP7 substrate access, keeping CASP9 inactive. XIAP Protein, Human (Avi) is the recombinant human-derived XIAP protein, expressed by E. coli , with C-Avi labeled tag. The total length of XIAP Protein, Human (Avi) is 236 a.a., with molecular weight of ~29.1 kDa.
XIAP protein is a multifunctional regulator that controls apoptosis, inflammation, immunity, copper homeostasis, and various signaling pathways. As a caspase inhibitor, it blocks CASP3 and CASP7 substrate access, keeping CASP9 inactive. XIAP Protein, Human (His) is the recombinant human-derived XIAP protein, expressed by E. coli , with N-His labeled tag. The total length of XIAP Protein, Human (His) is 105 a.a., with molecular weight of ~14.8 kDa.
Ubiquitin-like modifier-activating enzyme 1; Protein A1S9; UBA1; A1S9T; UBE1
Human
Sf9 insect cells
The UBA1 protein initiates ubiquitin conjugation, marking proteins for degradation in the ubiquitin-proteasome system. UBA1 Protein, Human (sf9, His-GST) is the recombinant human-derived UBA1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of UBA1 Protein, Human (sf9, His-GST) is 1057 a.a., with molecular weight of ~130 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.
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.
The UBA5 protein activates UFM1 in ufmylation, linking the C-terminal glycine residue of UFM1 to a cysteine residue in E1. UBA5 Protein, Human (His) is the recombinant human-derived UBA5 protein, expressed by E. coli , with N-6*His labeled tag. The total length of UBA5 Protein, Human (His) is 404 a.a., with molecular weight of 14 & 40-60 kDa, respectively.
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.
Tripartite motif-containing protein 5; RING finger protein 88; TRIM5; RNF88
Human
E. coli
The TRIM5 protein is a capsid-specific restriction factor that prevents non-host adapted retroviral infection. TRIM5 acts as a pattern recognition receptor that activates innate immune signaling by triggering E3 ubiquitin ligase activity upon binding to viral capsids. TRIM5 restricts various retroviruses and regulates autophagy. TRIM5 Protein, Human (His) is the recombinant human-derived TRIM5 protein, expressed by E. coli , with N-6*His labeled tag. The total length of TRIM5 Protein, Human (His) is 248 a.a., with molecular weight of ~33.0 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, a vital component of the ubiquitin-proteasome system, functions as an E2 ubiquitin-conjugating enzyme, crucial for attaching ubiquitin to diverse substrates. In vitro, UBE2K catalyzes 'Lys-48'-linked polyubiquitin chains, particularly with or without the BRCA1-BARD1 E3 ligase complex. It participates in the selective degradation of short-lived proteins, including endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. UBE2K exhibits ubiquitination activity towards targets like huntingtin and p53/TP53, and potentially NF-kappa-B. Its role in viral infections involves contributing to MHC class I heavy chain degradation and participating in HPV E7 protein-dependent degradation of RB1. UBE2K Protein, Human (GST) is the recombinant human-derived UBE2K protein, expressed by E. coli, with N-GST labeled tag. The total length of UBE2K Protein, Human (GST) is 200 a.a., with molecular weight of ~45.0 kDa.
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 ~25.0 kDa.
Ubiquitin-associated and SH3 domain-containing protein B;
STS-1; TULA-2; UBASH3B
Human
E. coli
UBASH3B/STS1 protein blocks CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases, leading to the accumulation of activating receptors such as T cell receptors and EGFR on the cell surface. It exhibits tyrosine phosphatase activity against substrates such as EGFR, FAK, SYK and ZAP70. UBASH3B/STS1 Protein, Human (His) is the recombinant human-derived UBASH3B/STS1 protein, expressed by E. coli , with N-His, N-6*His labeled tag. The total length of UBASH3B/STS1 Protein, Human (His) is 268 a.a., with molecular weight of ~30 kDa.
The ITCH/AIP4 protein, a member of the Nedd4 family of ubiquitin ligases, transfers ubiquitin to protein substrates for lysosomal degradation. It regulates cell differentiation and immune responses and is associated with autoimmune disease. Alternative splicing produces multiple isoforms. ITCH/AIP4 is expressed ubiquitously, with notable levels in the testis, esophagus, and 25 other tissues. ITCH/AIP4 Protein, Human (solution) is the recombinant human-derived ITCH/AIP4 protein, expressed by E. coli , with tag free. and with residual Gly-Pro in N-terminal (not related to functional changes) mutation. The total length of ITCH/AIP4 Protein, Human (solution) is 378 a.a., with molecular weight of ~40 kDa.
E3 ubiquitin-protein ligase RNF43; RING finger protein 43; RNF43
Human
HEK293
RNF43 protein is encoded by the RNF43 gene and is a RING-type E3 ubiquitin ligase. It negatively regulates Wnt signaling by increasing ubiquitination of Frizzled receptors, resulting in reduced surface levels of these receptors. RNF43 Protein, Human (HEK293, His) is the recombinant human-derived RNF43 protein, expressed by HEK293 , with C-His labeled tag. The total length of RNF43 Protein, Human (HEK293, His) is 174 a.a., with molecular weight of ~25-38 kDa.
Ubiquitin-associated and SH3 domain-containing protein A; CLIP4; STS-2; TULA-1
Human
E. coli
UBASH3A interferes with CBL-mediated downregulation and degradation of receptor-type tyrosine kinases and promotes the accumulation of activating receptors such as T cell receptors, EGFR and PDGFRB on the cell surface. It exhibits minimal protein tyrosine phosphatase activity and may act as a dominant negative regulator of UBASH3B-dependent dephosphorylation. UBASH3A Protein, Human (His) is the recombinant human-derived UBASH3A protein, expressed by E. coli , with N-His labeled tag. The total length of UBASH3A Protein, Human (His) is 270 a.a., with molecular weight of ~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, a versatile ubiquitin-conjugating enzyme, accepts ubiquitin from the E1 complex, catalyzing its covalent attachment to diverse substrates. Notably, UBE2W uniquely monoubiquitinates N-termini, including ATXN3, MAPT/TAU, POLR2H/RPB8, and STUB1/CHIP, displaying specificity for disordered N-termini. This monoubiquitination is crucial for degrading misfolded chaperone substrates, as UBE2W mediates STUB1/CHIP monoubiquitination, limiting ubiquitin chain length. Activated by UV irradiation, UBE2W collaborates with FANCL, catalyzing monoubiquitination of FANCD2 in the Fanconi anemia complex, a key step in the DNA damage response pathway. Additionally, UBE2W flexibly catalyzes 'Lys-11'-linked polyubiquitination in vitro. UBE2W Protein, Human (His) is the recombinant human-derived UBE2W protein, expressed by E. coli, with N-His labeled tag. The total length of UBE2W Protein, Human (His) is 151 a.a., with molecular weight of ~18 kDa.
