E3 Ubiquitin Ligases


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Cat.No.Product NameSourceSpeciesTagMolecular Weight
BP-700052UB301: MuRF1E. coliHumanHis6-SUMO40 kDa
BP-700053UB302: CARP2E. coliHumanHis6-SUMO41 kDa
BP-700054UB303: Praja1E. coliHumanHis6-SUMO71 kDa
BP-700055UB304: E6APE. coliHumanNone101 kDa
BP-700056UB305: MuRF2E. coliHumanHis6-SUMO72.7 kDa (with tag), 60.5 kDa (without tag)
BP-700057UB306: MuRF3E. coliHumanHis6-SUMO52.4 kDa (with tag), 40.3 (without tag)
BP-700058UB307: Hrd1 (Synoviolin)E. coliHumanHis6-SUMOCytoplasmic fragment (236-617): 39.3 kDa (without SUMO tag)
BP-700059UB308: Cbl-b CoreE. coliHumanHis6 + HA48 kDa
BP-700060UB308FL: Cbl-b Full Length
BP-700061UB310: GP78E. coliHumanN-terminal GST tag72 kDa
BP-700062UB312: TRAF6E. coliHumanSUMO70 kDa
BP-700063UB313: MDM2E. coliHumanN-terminal His6-HA-Smt368 kDa
BP-700064UB315: ITCHE. coliHumanHis6-SUMO110 kDa
BP-700065UB316H: WWP2, His6-SUMOE. coliHumanHis6112 kDa
BP-700066UB317: Parkin (non-phosphorylated)E. coliHumanHis6SUMO64 kDa
BP-700067UB317A: Parkin (phosphorylated)E. coliHumanHis6SUMO64 kDa
BP-700068CARP2, SUMO-His-tagsE. coliHumanN-terminal SUMO-His-tags41 kDa
BP-700069CBL, GST-TagE. coliHumanN-terminal GST-Tag71 kDa
BP-700070CBL-B (Y363F), His-tag, Biotin-labeled (Human)E. coliHumanN-terminal His-tag, N-terminal Avi-tag48 kDa
BP-700071CBL-B TR-FRET Assay Kit
BP-700072CBL-B, Avi-His-Tag, Biotin-labeled (Human)E. coliHumanN-terminal Avi-His Tag48 kDa
BP-700073CBL-B, GST-Tag (Human)E. coliHumanN-terminal GST-Tag72 kDa
BP-700074CBL-B, His-Avi-TagE. coliHumanN-terminal His-tag, N-terminal Avi-tag48 kDa
BP-700075CBLC, FLAG-TagHEK293HumanN-terminal FLAG-tag45 kDa
BP-700076Cereblon/DDB1/Cul4A/Rbx1 ComplexHEK293HumanCereblon: N-terminal FLAG-tag; DDB1: N-terminal FLAG-tag; Cul4a: N-terminal His-tag; Rbx1: N-terminal His-tagCereblon: 51 kDa; DDB1: 128 kDa; Cul4a: 87 kDa; Rbx1: 13 kDa
BP-700077CUL2, FLAG-TagHEK 293HumanFLAG-Tag88 kDa
BP-700078CUL3/Rbx1, GST-tagSf9 Insect CellHumanN-terminal GST-tagCUL3: 117 kDa; Rbx1: 12 kDa
BP-700079Elob, FLAG-TagHEK293HumanN-terminal FLAG-tag14 kDa
BP-700080ELOB/ELOC/VHL ComplexHEK293HumanVHL: N-terminal FLAG-tag; ELOB: N-terminal FLAG-tag; ELOC: N-terminal His-tagVHL: 25 kDa; ELOB: 14 kDa; ELOC: 13 kDa
BP-700081Hrd1, SUMO-His-tagsE. coliHumanN-terminal SUMO-His-tags39.3 kDa (without SUMO tag)
BP-700082KCTD13, GST-tagSf9 cellHumanN-terminal GST-tag63 kDa
BP-700083MDM2, GST-tagSf9 insect cellsHumanN-terminal GST-tag82 kDa
BP-700084MuRF1, SUMO-His-tagsE. coliHumanN-terminal SUMO-His-tags40 kDa
BP-700085MuRF2, SUMO-tagE. coliHumanN-terminal SUMO-tag60.5 kDa (without SUMO tag)
BP-700086MuRF3, SUMO-His-tagsE. coliHumanN-terminal SUMO-His-tags40.3 kDa (without SUMO tag)
BP-700087NEDD4, FLAG-tagSf9 insect cellsHumanN-terminal FLAG-tag86 kDa
BP-700088Praja1, SUMO-tagE. coliHumanN-terminal SUMO-tag71 kDa
BP-700089RNF20, His-FLAG-tagsSf9 insect cellsHumanN-terminal His-FLAG-tags115 kDa
BP-700090SMURF1, FLAG-tagSf9 insect cellsHumanN-terminal FLAG-tag70 kDa
BP-700091SMURF2, FLAG-tagSf9 insect cellsHumanN-terminal FLAG-tag72 kDa
BP-700092UBE3A, His-FLAG-tagsSf9 insect cellsHumanN-terminal His-FLAG-tags99.8 kDa
BP-700093UFL1, GST-tagSf9 cellHumanN-terminal GST-tag116 kDa
BP-700094UHRF1, His-FLAG-tagsSf9 insect cellsHumanN-terminal His-FLAG-tags92 kDa
BP-700095VHL/CUL2/ELOB/ELOC/RBX1 ComplexHEK293HumanVHL: N-terminal FLAG-tag; CUL2: N-terminal FLAG-tag; ELOB: N-terminal FLAG-tag; ELOC: N-terminal His-tag; Rbx1: N-terminal His-tagVHL: 25 kDa; CUL2: 88 kDa; ELOB: 14 kDa; ELOC: 13 kDa; Rbx1: 13 kDa
BP-700096WWP1, FLAG-tagSf9 insect cellsHumanN-terminal FLAG-tag106 kDa
BP-700097XIAP, FLAG-tagSf9 insect cellsHumanN-terminal FLAG-tag57 kDa


E3 is a large family, more than 600 E3 have been found. There are three main types of ubiquitin ligase E3: HECT (homologous to E6AP C-terminus) domain family, RING (really interesting new gene) domain family, and U-box protein family. The HECT domain acts mainly through the thioester bond necessary for the formation of ubiquitin. The RING domain provides residence sites for E2 and the substrate to catalyze the transfer of ubiquitin to the substrate. The ubiquitin ligase E3 of the U-box family is necessary for post-translational quality control of eukaryotic proteins.


E3 is a ubiquitin ligase, which directly or indirectly catalyzes the transfer of ubiquitin to the target protein (substrate) and forms isopeptide bonds. In general, ubiquitin ligase can make the target protein multi-ubiquitin, that is, adding multiple ubiquitin molecules to form a multi-ubiquitin chain, and the protein with multi-ubiquitin chain can be recognized by proteasome and degraded. However, in some cases, ubiquitin ligase connects only one ubiquitin molecule to the target protein, this single ubiquitin protein will not be degraded by proteasome, but its location or function in cells may be changed. For example, mono-ubiquitin proteins can change their position by binding to other proteins with ubiquitin-binding domains.


Compared with E1 and E2, E3 has attracted more attention, not only because of the large number of E3, but also because E3 can specifically recognize protein substrates, so it can be used as a therapeutic target for a variety of E3-related diseases, including human tumors. E3 is more specific. E3 is full of carcinogenic factors, tumor suppressor factors, and some can be converted into each other under specific conditions. For example, in many human tumors, tumor suppressor Fbw7 is often lost or mutated, so regulating its upstream factor to restore the function of Fbw7 is one of the ways of tumor therapy. Skp2 can achieve its carcinogenic effect by degrading tumor suppressor, making cancer cells proliferate malignant. β-TRCP has two sides, and regulates the degradation of tumor suppressor or carcinogenic factors according to the environment. Drugs targeting E3, such as Serdemetan, LCL161 and AT-406, have entered clinical trials, and IMiDs has been approved by FDA.


  1. Mayer, J., Layfield, R., Ardley, H. C., & Robinson, P. A. (2005). E3 ubiquitin ligases. Essays in biochemistry, 41, 15-30.
  2. Sun, Y. (2003). Targeting E3 ubiquitin ligases for cancer therapy. Cancer biology & therapy, 2(6), 623-629.

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