UBE2L6 Protein, Human (His)

The UBE2L6 protein plays a key role in cell regulation by catalyzing the covalent attachment of ubiquitin or ISG15 to other proteins. Notably, it plays a role in E6/E6-AP-induced ubiquitination of p53/TP53, a core process in regulating cellular responses to stress and DNA damage. UBE2L6 Protein, Human (His) is the recombinant human-derived UBE2L6 protein, expressed by E. coli , with C-6*His labeled tag. The total length of UBE2L6 Protein, Human (His) is 153 a.a., with molecular weight of ~17.0 kDa.

UBE2L6, also known as ubiquitin-conjugating enzyme E2L6, is a protein that catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins, a process crucial for the regulation of protein stability and function. Specifically, UBE2L6 plays a role in the E6/E6-AP-induced ubiquitination of p53/TP53, a tumor suppressor protein involved in cell cycle regulation and apoptosis. Additionally, UBE2L6 is implicated in promoting ubiquitination and subsequent proteasomal degradation of FLT3, a receptor tyrosine kinase associated with cell proliferation and differentiation. Through these ubiquitination events, UBE2L6 contributes to the targeted degradation of specific proteins, influencing cellular pathways and processes, particularly those related to cell cycle control and signaling cascades.

Human

E. coli

C-6*His

O14933 (M1-S153)

9246  [NCBI]

MMASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPEYPFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPCTKTCQVLEALNVLVNRPNIREPLRMDLADLLTQNPELFRKNAEEFTLRFGVDRPS

Approximately 17.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.