The CD4 molecule is composed of four extracellular immunoglobulin-like domains (D1 to D4), a transmembrane region, and a cytoplasmic tail. The CD-4 (125-202 a.a.) (Human Recombinant) specifically refers to a recombinant protein that includes amino acids 125 to 202 of the CD4 molecule. This segment is fused with a 4kDa His Tag, resulting in a total molecular weight of approximately 19 kDa .
CD4 is primarily involved in the recognition of antigens presented by Major Histocompatibility Complex (MHC) class II molecules on the surface of antigen-presenting cells (APCs). This interaction is critical for the activation of T-helper cells, which in turn activate other immune cells, including B cells and cytotoxic T cells.
One of the most well-known functions of CD4 is its role as a receptor for the Human Immunodeficiency Virus (HIV). The virus binds to the CD4 molecule on the surface of T-helper cells, facilitating its entry into the cell. This interaction is a key step in the HIV infection process, leading to the depletion of T-helper cells and the eventual collapse of the immune system in untreated individuals.
The recombinant form of CD4, specifically the CD-4 (125-202 a.a.) (Human Recombinant), is produced using Escherichia coli as the expression system . This recombinant protein is typically supplied as a sterile lyophilized powder and can be reconstituted in sterile water or other aqueous solutions. It is used in various research applications, including:
Recombinant CD4 proteins are invaluable tools in immunological research. They are used to study the mechanisms of T-cell activation, the interaction between CD4 and MHC class II molecules, and the process of HIV entry into host cells. Additionally, they are employed in the development of therapeutic strategies aimed at enhancing immune responses or blocking HIV infection.