ISG15 E1/UBE1L Protein, Human (sf9, His, Strep)

The ISG15 E1/UBE1L protein initiates ubiquitination by adenylating the C-terminal glycine of ubiquitin with ATP to form a thioester bond with its cysteine residue. This produces ubiquitin-E1 thioester and free AMP. ISG15 E1/UBE1L Protein, Human (sf9, His, Strep) is the recombinant human-derived ISG15 E1/UBE1L protein, expressed by Sf9 insect cells , with N-8*His, N-Strep labeled tag. The total length of ISG15 E1/UBE1L Protein, Human (sf9, His, Strep) is 1011 a.a., .

ISG15 E1/UBE1L protein initiates the ubiquitination process by activating ubiquitin through a two-step mechanism. It begins by adenylating the C-terminal glycine residue of ubiquitin with ATP and subsequently forms a thioester bond between this glycine residue and a cysteine residue in E1. This results in the generation of a ubiquitin-E1 thioester and free AMP. In addition to its role in ubiquitin activation, ISG15 E1/UBE1L catalyzes the ISGylation of the influenza A virus NS1 protein, highlighting its involvement in antiviral responses. The protein is actively engaged in protein modification processes, particularly protein ubiquitination, underscoring its significance in regulating cellular pathways through post-translational modifications.

Human

Sf9 insect cells

N-8*His;N-Strep

P41226 (D2-L1012)

7318  [NCBI]

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.