Perforin-1 (PRF1) is a pore-forming cytolytic protein expressed in cytotoxic T lymphocytes and natural killer cells. It is essential for the immune system's ability to destroy infected or malignant cells. Upon recognition of a target cell, perforin is released from cytotoxic granules and facilitates the entry of granzymes into the target cell by forming pores in the plasma membrane, leading to apoptosis. Mutations or deficiencies in the PRF1 gene can result in impaired immune responses and are associated with conditions such as familial hemophagocytic lymphohistiocytosis.

Reference: https://pubmed.ncbi.nlm.nih.gov/25998963/

"Antigen Grade" is not a formally regulated industry standard, but it is commonly used to indicate that a protein is intended for antigen-based applications rather than functional assays.

Antigen Grade proteins are recombinant proteins purified under denaturing conditions (e.g., in urea) and may not retain their native conformation or biological activity. These proteins are suitable for antigen-based applications such as antibody generation, ELISA plate coating, Western blotting, and other immunological assays, but are not recommended for functional or activity assays.

Suitable Applications:

✔ Antibody production (immunogen)
✔ ELISA coating antigen
✔ Western blot positive control
✔ Dot blot
✔ Epitope mapping
✔ Antibody screening, etc.

Not Recommended:

✘ Enzyme activity assays
✘ Ligand-receptor binding assays (unless validated)
✘ Cell-based functional assays
✘ SPR/BLI kinetic studies requiring native folding

Why "Antigen Grade"?

Many bacterial proteins expressed as inclusion bodies are purified in 6–8 M urea. Although they can often be refolded, proteins sold in urea are generally not guaranteed to be correctly refolded or biologically active. "Antigen Grade" proteins are suitable for immunological applications but may not be appropriate for assays requiring native protein function.