Anti-Perforin/PRF1 Antibody Picoband® Fluoro594 Conjugated

PRF1, also known as Perforin-1, is a protein that in humans is encoded by the PRF1 gene. It is mapped to 10q22.1. PRF1 is a cytolytic protein found in the granules of Cytotoxic T lymphocytes (CTLs) and NK cells. Upon degranulation, PRF1 inserts itself into the target cell's plasma membrane, forming a pore. The lytic membrane-inserting part of perforin is the MACPF domain. This region shares homology with cholesterol-dependent cytolysins from Gram-positive bacteria. PRF1 has structural and functional similarities to complement component 9 (C9) . Like C9, this protein creates transmembrane tubules and is capable of lysing non-specifically a variety of target cells. This protein is one of the main cytolytic proteins of cytolytic granules, and it is known to be a key effector molecule for T-cell- and natural killer-cell-mediated cytolysis. PRF1 is thought to act by creating holes in the plasma membrane which triggers an influx of calcium and initiates membrane repair mechanisms. These repair mechanisms bring perforin and granzymes into early endosomes.

E.coli-derived human Perforin recombinant protein (Position: E175-W555) . Human Perforin shares 68% amino acid (aa) sequence identity with both mouse and rat Perforin.

Highly expressed in the heart, skeletal muscle, placenta and lung. Weakly expressed in the thymus, spleen, kidney and liver. Expressed on activated T- and B-cells, dendritic cells, keratinocytes and monocytes. .

Plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. .

1. Rosado CJ, Buckle AM, Law RH, Butcher RE, Kan WT, Bird CH, Ung K, Browne KA, Baran K, Bashtannyk-Puhalovich TA, Faux NG, Wong W, Porter CJ, Pike RN, Ellisdon AM, Pearce MC, Bottomley SP, Emsley J, Smith AI, Rossjohn J, Hartland EL, Voskoboinik I, Trapani JA, Bird PI, Dunstone MA, Whisstock JC (2007) . A common fold mediates vertebrate defense and bacterial attack. Science 317 (5844) : 1548–51. 2. Fink TM, Zimmer M, Weitz S, Tschopp J, Jenne DE, Lichter P (Sep 1992) . Human perforin (PRF1) maps to 10q22, a region that is syntenic with mouse chromosome 10. Genomics 13 (4) : 1300–2. 3. Shinkai Y, Yoshida MC, Maeda K, Kobata T, Maruyama K, Yodoi J, Yagita H, Okumura K (Jan 1990) . Molecular cloning and chromosomal assignment of a human perforin (PFP) gene. Immunogenetics 30 (6) : 452–7. 4. Tschopp J, Masson D, Stanley KK (1986) . Structural/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis. Nature 322 (6082) : 831–4.

Cytoplasmic granule lumen. Secreted. Cell membrane; Multi-pass membrane protein. Endosome lumen. Stored in cytoplasmic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell. Inserts into the cell membrane of target cells and forms pores. Membrane insertion and pore formation requires a major conformation change. May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes.