ASB13 Human

The ASB13 protein contains six ankyrin repeats and a SOCS box domain . The ankyrin repeats are known for their role in protein-protein interactions, while the SOCS box domain is involved in targeting proteins for degradation. Specifically, the SOCS box couples suppressor of cytokine signaling (SOCS) proteins and their binding partners with the elongin B and C complex, potentially targeting them for ubiquitination and subsequent proteasomal degradation .

ASB13 is believed to function as a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex. This complex mediates the ubiquitination and subsequent proteasomal degradation of target proteins . This process is crucial for maintaining cellular homeostasis and regulating various cellular processes.

Mutations or dysregulation of the ASB13 gene have been associated with certain diseases. For instance, ASB13 has been linked to hematologic cancers and dentatorubral-pallidoluysian atrophy . Its role in these diseases is likely related to its function in protein degradation and cellular regulation.

Recombinant ASB13 is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 301 amino acids, with a molecular mass of 32.4 kDa. It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques . This recombinant form is used in various research applications to study the protein’s function and its role in disease.

Recombinant ASB13 is utilized in various biochemical assays and research studies to understand its function and interactions. It is particularly useful in studying the mechanisms of protein ubiquitination and degradation, as well as its role in disease pathogenesis.