Anti-Ube1L antibody [EPR4270] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Ube1L also known as ubiquitin-activating enzyme E1-like plays an important role in the ubiquitin-proteasome system by activating ubiquitin molecules. With a molecular mass of approximately 117 kDa Ube1L functions as the initial enzyme in the ubiquitination cascade catalyzing the formation of a thioester bond with ubiquitin. This process is important for the tagging of proteins for degradation. Ube1L exhibits widespread expression in various tissues indicating its importance in diverse cellular activities.

Biological function summary

This protein participates actively in the regulation of protein homeostasis. Ube1L helps to manage protein turnover and maintains protein quality control by marking damaged or unneeded proteins for degradation via the proteasome. Although Ube1L functions primarily as a standalone enzyme it cooperates closely with ubiquitin-conjugating and -ligating enzymes (E2s and E3s) to achieve precise ubiquitination of target proteins. This cooperation is critical for cellular processes like cell cycle regulation and response to stress.

Pathways

Ube1L is a significant element in the ubiquitin-proteasome pathway which is essential for protein degradation and turnover. It also contributes to the regulation of interferon signaling by modifying proteins such as ISG15 a ubiquitin-like protein involved in antiviral response. Related proteins such as UBE2L6 and UBE2E1 serve as E2 conjugating enzymes that interact with Ube1L further influencing these pathways by facilitating the transfer of activated ubiquitin.

Associated diseases and disorders

Ube1L has been implicated in certain types of cancers and viral infections. Alterations in the expression or function of Ube1L can lead to disrupted protein degradation contributing to cancer progression through the accumulation of oncogenic proteins. Ube1L is also connected to proteins like ISG15 and USP18 which are involved in host defense mechanisms against viral infections. Dysregulation in these contexts can result in inadequate antiviral responses or improper regulation of cell proliferation.