CD4, also known as T-cell surface glycoprotein CD4, is a critical protein in the immune system. It is primarily found on the surface of helper T cells, monocytes, macrophages, and dendritic cells. The CD4 molecule plays a significant role in the immune response by acting as a co-receptor that assists the T-cell receptor (TCR) in communicating with antigen-presenting cells (APCs).
The CD4 protein is a member of the immunoglobulin superfamily and consists of four extracellular domains (D1 to D4). The recombinant human CD4 (26-396) refers to a specific fragment of the CD4 protein, encompassing amino acids 26 to 396. This fragment includes the extracellular portion of the protein, which is crucial for its interaction with major histocompatibility complex (MHC) class II molecules.
CD4 functions primarily as a co-receptor that enhances the sensitivity of TCRs to antigens presented by MHC class II molecules. This interaction is essential for the activation of helper T cells, which in turn play a pivotal role in orchestrating the immune response by activating other immune cells, including B cells and cytotoxic T cells.
Recombinant human CD4 (26-396) is typically produced using various expression systems, such as HEK 293 cells or E. coli. The protein is expressed as a single, non-glycosylated polypeptide chain and is purified using chromatographic techniques to achieve high purity levels. For instance, the recombinant CD4 protein expressed in HEK 293 cells has a purity of ≥95% and an endotoxin level of ≤0.005 EU/µg . Similarly, the protein produced in E. coli is fused to a 25 amino acid His-tag at the N-terminus and purified to a purity greater than 85% .
Recombinant CD4 (26-396) is widely used in research to study the immune response, particularly the interactions between T cells and APCs. It is also utilized in the development of therapeutic agents and vaccines. The protein’s ability to bind to MHC class II molecules makes it a valuable tool for investigating the mechanisms of antigen presentation and T cell activation.