UBE2L3 Human His
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
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Description
The UBE2L3 protein contains 6xHis tag and is purified by proprietary chromatographic techniques.
Product Specs
DNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAEN
WKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFT
KKYGEKRPVD.
Product Science Overview
Ubiquitin-Conjugating Enzyme E2L 3, also known as UBE2L3, is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme plays a crucial role in the ubiquitination process, which is an essential cellular mechanism for targeting abnormal or short-lived proteins for degradation. The human recombinant version of this enzyme, tagged with a His tag, is widely used in research to study its function and interactions.
UBE2L3 is characterized by its ability to accept ubiquitin from the E1 ubiquitin-activating enzyme and transfer it to target proteins in conjunction with E3 ubiquitin ligases. The enzyme specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases, but does not function with most RING-containing E3 ubiquitin-protein ligases due to its lack of intrinsic E3-independent reactivity with lysine . In vitro, UBE2L3 catalyzes ‘Lys-11’-linked polyubiquitination, which is involved in the selective degradation of short-lived and abnormal proteins .
The modification of proteins with ubiquitin is a critical cellular process that regulates various aspects of cell biology, including protein degradation, cell cycle progression, and DNA repair. UBE2L3 has been demonstrated to participate in the ubiquitination of key regulatory proteins such as p53, c-Fos, and the NF-kB precursor p105 . This highlights its importance in maintaining cellular homeostasis and responding to cellular stress.
The human recombinant UBE2L3, tagged with a His tag, is produced in Escherichia coli and purified to a high degree of purity. The His tag facilitates the purification process and allows for easy detection and quantification of the protein in various assays. This recombinant protein is used in research to study the enzyme’s function, interactions, and role in ubiquitination pathways .
Recombinant UBE2L3 is utilized in various experimental setups, including in vitro ubiquitination assays, protein-protein interaction studies, and structural analysis. Its role in the ubiquitination of specific substrates makes it a valuable tool for understanding the molecular mechanisms underlying protein degradation and regulation. Additionally, studying UBE2L3 can provide insights into the development of therapeutic strategies for diseases associated with dysregulated ubiquitination, such as cancer and neurodegenerative disorders .
