LFA-3 is produced using recombinant DNA technology in a Chinese Hamster Ovary (CHO) mammalian cell expression system. The recombinant human LFA-3 fusion protein has a molecular weight of approximately 91.4 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity and quality.
LFA-3 serves as a ligand for the T-lymphocyte CD2 glycoprotein. This interaction is essential for mediating various immune responses, including:
The LFA-3/CD2 interaction is crucial for the activation and adhesion of T lymphocytes, which are vital for the immune response. This interaction can also prime responses by both CD2+ and LFA-3+ cells .
The recombinant LFA-3 protein is typically provided as a sterile filtered, white lyophilized (freeze-dried) powder. The formulation includes:
For reconstitution, it is recommended to dissolve the lyophilized LFA-3 in sterile water to a concentration of at least 100 µg/ml, which can then be further diluted into other aqueous solutions .
Lyophilized LFA-3 is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage. Upon reconstitution, the protein should be stored at 4°C for short-term use (2-7 days) and below -18°C for long-term use. To prevent degradation, it is advisable to add a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), and avoid freeze-thaw cycles .
LFA-3 is used extensively in laboratory research to study immune cell interactions and functions. It is particularly valuable in understanding the mechanisms of T-lymphocyte activation and adhesion, which are critical for developing immunotherapies and vaccines.