BCL7A is a component of the SWI/SNF chromatin remodeling complex, which plays a crucial role in modifying the interactions between DNA and histones using the energy from ATP hydrolysis . This complex is essential for regulating gene expression by altering chromatin structure, thereby influencing various cellular processes such as differentiation, proliferation, and DNA repair .
Mutations and alterations in the BCL7A gene have been implicated in several hematological malignancies, including B-cell non-Hodgkin lymphoma and chronic lymphocytic leukemia (CLL) . Specifically, BCL7A is involved in a three-way gene translocation with Myc and IgH in Burkitt lymphoma cell lines . This translocation disrupts the N-terminal region of the gene, which is thought to contribute to the pathogenesis of a subset of high-grade B-cell non-Hodgkin lymphomas .
Recombinant human BCL7A protein is produced using E. coli expression systems and is often tagged with a His-tag at the N-terminus for purification purposes . This recombinant protein is used in various research applications to study the function and interactions of BCL7A in cellular processes and disease mechanisms .
Research on BCL7A has shown that mutations in the amino-terminal domain can impair its tumor suppressor role, particularly in diffuse large B-cell lymphoma (DLBCL) . Additionally, promoter hypermethylation can lead to the silencing of BCL7A in hematological malignancies, further highlighting its importance in cancer biology .
Understanding the role of BCL7A in these diseases can provide insights into potential therapeutic targets and strategies for treating B-cell lymphomas and other related malignancies. The use of recombinant BCL7A protein in research continues to be a valuable tool for elucidating the molecular mechanisms underlying these conditions.