The recombinant human BOLA3 protein is typically produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain. It contains 130 amino acids, corresponding to the amino acids 1-107 of the native human BOLA3 protein . The recombinant protein often includes a 23 amino acid His-tag at the N-terminus, which facilitates purification through chromatographic techniques . The molecular mass of the recombinant BOLA3 protein is approximately 14.5 kDa .
Human BolA proteins belong to three different groups, each with functional divergence. The different helix-turn-helix motifs among BOLA1, BOLA2, and BOLA3 are responsible for their functional differences . BOLA3, in particular, plays a crucial role in cellular iron-sulfur cluster assembly, which is essential for various metabolic processes.
Recombinant BOLA3 protein is widely used in research to study its function and role in cellular processes. It is often utilized in SDS-PAGE assays to analyze protein purity and molecular weight . The protein is supplied in a phosphate-buffered saline (PBS) solution with 10% glycerol to maintain stability . For long-term storage, it is recommended to store the protein at -20°C and avoid multiple freeze-thaw cycles .