S100A2 Human

S100 Calcium Binding Protein A2 (S100A2), also known as CaN19 or S100L, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium ions, which is crucial for their role in various cellular processes. S100A2 was first isolated from bovine lung tissue and later discovered in human mammary epithelial cells .

S100A2 is a homodimer, meaning it consists of two identical subunits. Upon binding calcium, it undergoes a conformational change that activates its function. The active form of S100A2 is involved in regulating cell proliferation and differentiation, gene transcription, and p53-dependent growth arrest and apoptosis . Additionally, S100A2 regulates both calcium and zinc within cells and increases p53 activity .

Under normal circumstances, S100A2 is highly expressed in human lungs, prostate, kidneys, hair follicles, and salivary and mammary glands . It is also expressed by multiple cell types, including keratinocytes, chondrocytes, and bronchial epithelium .

S100A2 has been functionally associated with various diseases, including neurological, cardiac, and neoplastic conditions . Overexpression of S100A2 has been detected in several cancers, such as breast, colon, prostate, pancreatic, and lung carcinomas . This overexpression suggests that S100A2 may serve as a potential tumor biomarker and a target for future diagnostic and therapeutic applications .

Recombinant S100A2 refers to the protein produced through recombinant DNA technology, which allows for the production of large quantities of the protein for research and therapeutic purposes. The recombinant form retains the same structure and function as the naturally occurring protein, making it valuable for studying the protein’s role in various biological processes and diseases .