SENP2 Protein, Human

The SENP2 protein is crucial in the SUMO pathway and has the dual function of maturing and uncoupling SUMO. It hydrolyzes the α-linked peptide bond in the SUMO propeptide, converting it to the mature form. SENP2 Protein, Human is the recombinant human-derived SENP2 protein, expressed by E. coli , with tag free. The total length of SENP2 Protein, Human is 227 a.a., with molecular weight of ~29.0 kDa.

SENP2 protein plays a pivotal role in the SUMO pathway, exerting dual functions crucial for the maturation and deconjugation of small ubiquitin-like modifiers (SUMOs). Firstly, it hydrolyzes an alpha-linked peptide bond at the C-terminal end of SUMO propeptides (SUMO1, SUMO2, and SUMO3), facilitating their conversion into mature forms. Secondly, SENP2 contributes to the deconjugation process by cleaving the epsilon-linked peptide bond between the C-terminal glycine of mature SUMO and the lysine epsilon-amino group of target proteins. This dual enzymatic activity enables SENP2 to finely regulate SUMOylation dynamics and impact various cellular processes. Beyond its canonical functions, SENP2 has been implicated in modulating the Wnt pathway, influencing CTNNB1 levels, and actively participating in adipogenesis by desumoylating and stabilizing CEBPB. Additionally, SENP2 emerges as a key player in antiviral responses, contributing to the regulation of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection. The interactions of SENP2 with SUMO isoforms, as well as its binding to proteins like NUP153 and MTA1, further underscore its intricate involvement in cellular processes and signaling pathways.

Human

E. coli

Tag Free

Q9HC62 (D363-L589)

59343  [NCBI]

DDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWSLVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL

Approximately 29.0 kDa

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

<1 EU/μg, determined by LAL method.