CD274 Human
Description
CD274 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
The recombinant human CD274 protein is typically expressed in Escherichia coli (E. coli) and is available in various forms, including those with tags for purification and detection purposes. For example, the extracellular domain of recombinant human CD274 (amino acids 19-238) can be constructed with codon optimization and expressed with a small T7-His-TEV cleavage site tag at its N-terminal . This recombinant protein is often refolded using specialized techniques to ensure proper structure and functionality .
CD274/PD-L1 is an immune inhibitory receptor ligand that interacts with its receptor, Programmed Death-1 (PD-1), on T cells and B cells. This interaction plays a significant role in downregulating immune responses, which can be beneficial in preventing autoimmunity but can also be exploited by tumors to evade immune surveillance . The expression of CD274 on tumor cells can inhibit the activity of T cells, allowing the tumor to grow and spread unchecked .
Recombinant CD274 is widely used in research and clinical applications, including:
- Cancer Immunotherapy: CD274 is a target for cancer immunotherapy drugs, such as checkpoint inhibitors, which block the interaction between PD-L1 and PD-1, thereby enhancing the immune system’s ability to attack tumors.
- Diagnostic Development: CD274 can serve as a biomarker for certain types of cancer and autoimmune diseases, aiding in the diagnosis and monitoring of these conditions .
- Cell Culture Studies: Recombinant CD274 is used in cell culture studies to investigate its role in immune cell activation and differentiation .
The production of recombinant CD274 involves several steps, including gene cloning, protein expression in E. coli, and purification. The protein is typically purified using affinity chromatography techniques, which take advantage of the tags added to the protein during the cloning process . The purified protein is then refolded to ensure it retains its native structure and biological activity .
