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|Cat.No.||Product Name||Source||Species||Tag||Molecular Weight|
|BP-700001||NE101: NEDD8 E1||E. coli||Human||His6 and untagged||61 kDa (APPBP1) and 54kDa (UBA3)|
|BP-700002||SU101: SUMO E1||E. coli||Human||His6-tagged SAE1 and untagged SAE2||39 kDa (SAE1) and 73 kDa (SAE2)|
|BP-700003||UB101: UBE1||E. coli||Human||Untagged||118 kDa|
|BP-700004||NEDD8 E1, His-tag||E. coli||Human||His-tag (APPBP1), no tag (Uba3)||61 kDa (APPBP1), 52 kDa (UBA3)|
|BP-700005||UBA6 (UBE1L2), FLAG-tag||Sf9 insect cells||Human||N-terminal FLAG-tag||118 kDa|
|BP-700006||UBE1 (UBA1), FLAG-tag||Sf9 insect cells||Human||N-terminal FLAG-tag||118 kDa|
|BP-700007||UBE2A, His-Tag||E. coli||Human||N-Terminal His-Tag||17 kDa|
|BP-700008||UBE2C, His-Tag||E. coli||Human||N-Terminal His-Tag||21 kDa|
|BP-700009||UBE2D2, His-Tag||E. coli||Xenopus||N-Terminal His-Tag||17 kDa|
|BP-700010||Ubiquitin, His-Avi-Tag, Biotin Labeled||Sf9 insect cells||Human||N-terminal His-Avi-tag, Biotin labeled||12 kDa|
|BP-700011||Ubiquitin, His-Tag||E. coli||Human||C-terminal His-tag||10 kDa|
The main function of ubiquitin is to participate in the selective degradation of most proteins in eukaryotic cells. In addition, it also plays an important role in various cellular life activities, such as signal transduction, immune response, transcriptional translation and so on. Ubiquitin activating enzyme, also known as E1 enzyme, catalyzes the first step of the ubiquitin reaction, which can degrade proteins through proteasomes. It can load the ubiquitin and other protein ubiquitin samples to the target protein.
ATP, is hydrolyzed by ubiquitin activating enzyme to form a high-energy thioester bond between the cysteine (Cys) of its active site and glycine 76 (Gly76) at the C-terminal of ubiquitin, thus activating the-COOH terminal of ubiquitin in preparation for further nucleophilic attack. The covalent bond between ubiquitin or ubiquitin-like proteins and targeted proteins is the main mechanism by which eukaryotes regulate the function of proteins. Many processes such as cell division, immune response and embryonic development are also regulated by post-translational modification of ubiquitin and ubiquitin-like proteins.
There are two E1:Uba1 (also called Ube1) and Uba6 in mammalian cells. Among them, Uba1 is the most well-known, highly conserved in eukaryotic cells, and is mostly found in protein degradation pathways. In the human body, only Uba1 (also known as Ube1) and Uba6 E1 regulate all downstream ubiquitin reactions. Therefore, inhibition of E1 activity can inhibit some downstream tumor-related ubiquitin. For example, Uba1 inhibitors PYR-41 and PYZD-4409 can induce mammalian cell death, but the more precise mechanism is not clear. Although a variety of E1 inhibitors have been found, only MLN4924, an E1 activase inhibitor of ubiquitin-like molecule NEDD8, has really entered the clinical trial. The reason is that E1 inhibitors have poor specificity and properties, and more importantly, it will lead to the accumulation of ubiquitin substrates. Recent studies have shown that Uba1 is at the core of intracellular homeostasis and neurodegenerative diseases, suggesting that it has great potential as a therapeutic target for a series of neurodegenerative diseases.
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