Human UBCH8 / UBE2L6 Protein (His Tag)
RIG-B,UBCH8
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Catalog Number | P12641-H07E |
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Organism Species | Human |
Host | E. coli |
Synonyms | RIG-B,UBCH8 |
Molecular Weight | The recombinant human UBE2L6 consisting of 168 amino acids and has a calculated molecular mass of 19.6KDa. It migrates as an 18 kDa band in SDS-PAGE under reducing conditions as predicted. |
predicted N | Met |
SDS-PAGE | |
Purity | > 96 % as determined by SDS-PAGE |
Protein Construction | A DNA sequence encoding the human UBE2L6 isoform 1 (O14933-1) (Met 1-Ser 153) was expressed, with a polyhistide tag at the N-terminus. |
Bio-activity | |
Research Area | Epigenetics |Histone Modifying Enzymes |Ubiquitylation |Ubiquitin like Modifiers |
Formulation | Lyophilized from sterile 20mM Tris, 0.1% Brij35, pH 8.5 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
Background | UBCH8, also known as UBE2L6, belongs to the ubiquitin-conjugating enzyme family. The family of ubiquitin-conjugating (E2) enzymes is characterized by the presence of a highly conserved ubiquitin-conjugating (UBC) domain. These domains accommodate the ATP-activated ubiquitin (Ub) or ubiquitin-like (UBL) protein via a covalently linked thioester onto its active-site residue. E2 enzymes act via selective protein-protein interactions with the E1 and E3 enzymes and connect activation to covalent modification. By doing so, E2s differentiate effects on downstream substrates, either with a single Ub/UBL molecule or as a chain. UBCH8 is highly similar in primary structure to the enzyme encoded by the UBE2L3 gene. It catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. UBCH8 functions in the E6/E6-AP-induced ubiquitination of p53/TP53 and promotes ubiquitination and subsequent proteasomal degradation of FLT3. At protein level, it is present in natural killer cells. |
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