USP37 Protein, Human (Sf9)

The USP37 protein is a multifunctional deubiquitinase that regulates critical cellular processes. During the G1/S transition, it deubiquitinates cyclin A, promotes S phase entry, and enhances activity through Ser-628 phosphorylation. USP37 Protein, Human (Sf9) is the recombinant human-derived USP37 protein, expressed by Sf9 insect cells , with tag free. The total length of USP37 Protein, Human (Sf9) is 978 a.a., .

The USP37 Protein, as delineated in this description, serves as a versatile deubiquitinase with significant roles in various cellular processes, including cell cycle regulation, DNA replication, and DNA damage response. During the G1/S transition, USP37 antagonizes the anaphase-promoting complex (APC/C) by mediating the deubiquitination of cyclin-A (CCNA1 and CCNA2), facilitating S phase entry. Phosphorylation at Ser-628 during G1/S phase enhances its deubiquitinase activity, preventing the degradation of cyclin-A. USP37 further contributes to DNA replication by stabilizing the licensing factor CDT1 and promoting the efficiency and fidelity of replication by deubiquitinating checkpoint kinase 1/CHK1. It sustains the DNA damage response by deubiquitinating and stabilizing the ATP-dependent DNA helicase BLM in the context of DNA double-strand breaks. Additionally, USP37 plays a role in promoting cell migration by deubiquitinating and stabilizing the epithelial-mesenchymal transition (EMT)-inducing transcription factor SNAI. Its involvement in the regulation of mitotic spindle assembly and mitotic progression is highlighted by its association with chromatin-associated WAPL, stabilizing it through deubiquitination. The multifaceted functions of USP37 underscore its importance in coordinating critical cellular events.

Human

Sf9 insect cells

Tag Free

Q86T82 (S2-L979)

57695

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.