BAALC is a non-glycosylated polypeptide chain consisting of 165 amino acids, with a molecular mass of approximately 17.7 kDa . The recombinant form of BAALC is typically produced in Escherichia coli (E. coli) and includes a 20 amino acid His Tag at the N-terminus to facilitate purification . The protein is purified using standard chromatography techniques and is available in a sterile, filtered, colorless solution containing 20mM Tris buffer (pH 8), 1mM DTT, 20% glycerol, and 2mM EDTA .
BAALC is overexpressed in several types of cancer, including acute myeloid leukemia (AML) and breast cancer . In AML, BAALC expression is associated with poor prognosis and increased cell proliferation . In breast cancer, BAALC expression is progressively increased in primary tumors and metastases compared to normal breast tissue . Overexpression of BAALC in breast cancer cells has been shown to enhance proliferation, anchorage-independent growth, invasion, and migration . Conversely, knockdown of BAALC expression reduces these malignant properties .
The oncogenic effects of BAALC are mediated through various signaling pathways. In breast cancer, BAALC-associated migration and invasion are driven by focal adhesion kinase (FAK)-dependent signaling . This process is accompanied by an increase in matrix metalloproteinase (MMP)-9 activity, which plays a role in the degradation of the extracellular matrix, facilitating cancer cell invasion .
Given its role in cancer progression, BAALC is a potential therapeutic target. Inhibiting BAALC expression or function could reduce the proliferation and invasiveness of cancer cells, offering a novel approach to cancer treatment. Additionally, BAALC expression levels could serve as a biomarker for prognosis and treatment response in cancers where it is overexpressed .