NEURL2 Human

The recombinant human NEURL2 protein is typically produced in E. coli and is fused to a His-tag at the N-terminus for purification purposes. The protein consists of 285 amino acids and has a molecular weight of approximately 34.1 kDa . The amino acid sequence of the recombinant protein includes a series of histidine residues that facilitate its purification through affinity chromatography .

NEURL2 is a probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex. This complex mediates the ubiquitination of proteins, a process that tags them for degradation by the proteasome . During myogenesis, NEURL2 controls the ubiquitination and degradation of a specific pool of CTNNB1/beta-catenin located at the sarcolemma, which is essential for muscle fiber differentiation and maturation .

Recombinant human NEURL2 protein is used extensively in research to study its role in muscle development and its potential implications in muscle-related diseases. The protein is also used in various biochemical assays to understand the mechanisms of ubiquitination and protein degradation .

For optimal stability, the recombinant NEURL2 protein should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s integrity .