MART-1 (27-35) (human) TFA is the amino acid fragment spanning positions 27 to 35 of the MART-1 protein, and it represents an immunogenic epitope recognizable by HLA-A2-restricted melanoma-specific tumor-infiltrating lymphocytes (TILs). MART-1 (27-35) (human) TFA can be used in studies related to melanoma [1] [2].
In Vitro, MART-1 (27-35) (human) (0.1-10 μM; 2 h at room temperature then 24 h at 4 °C) TFA binds to purified human HLA-A2 molecules, and this binding is detectable via fluorescent signals[1]. MART-1 (27-35) (human) (10 μM; overnight at 4 °C for initial complex formation) TFA forms an HLA-A2 complex, which almost completely dissociates within 24 h at 37 °C[1]. MART-1 (27-35) (human) (1 μg/mL; 1 h incubation with T2 cells, 4 h cytolytic assay) TFA is specifically recognized by human MART-1 (27-35)-specific, HLA-A2-restricted TIL clones LT8, LT11 and LT12, and induces T2 target cells to release high levels of 51Cr[1]. MART-1 (27-35) (human) (0.0001-10 μg/mL; 1 h) TFA sensitizes HLA-A*0201+ T2 cells to lysis by CLW anti-MART-1 (27-35) CD8+ cytotoxic T lymphocytes (CTLs) in a dose-dependent manner[2].
References:
[1]. Guichard G, et al. Melanoma peptide MART-1(27-35) analogues with enhanced binding capacity to the human class I histocompatibility molecule HLA-A2 by introduction of a beta-amino acid residue: implications for recognition by tumor-infiltrating lymphocytes. J Med Chem. 2000;43(20):3803-3808.
[2]. Loftus DJ, et al. Identification of epitope mimics recognized by CTL reactive to the melanoma/melanocyte-derived peptide MART-1(27-35). J Exp Med. 1996;184(2):647-657.
In Vitro, MART-1 (27-35) (human) (0.1-10 μM; 2 h at room temperature then 24 h at 4 °C) TFA binds to purified human HLA-A2 molecules, and this binding is detectable via fluorescent signals[1]. MART-1 (27-35) (human) (10 μM; overnight at 4 °C for initial complex formation) TFA forms an HLA-A2 complex, which almost completely dissociates within 24 h at 37 °C[1]. MART-1 (27-35) (human) (1 μg/mL; 1 h incubation with T2 cells, 4 h cytolytic assay) TFA is specifically recognized by human MART-1 (27-35)-specific, HLA-A2-restricted TIL clones LT8, LT11 and LT12, and induces T2 target cells to release high levels of 51Cr[1]. MART-1 (27-35) (human) (0.0001-10 μg/mL; 1 h) TFA sensitizes HLA-A*0201+ T2 cells to lysis by CLW anti-MART-1 (27-35) CD8+ cytotoxic T lymphocytes (CTLs) in a dose-dependent manner[2].
References:
[1]. Guichard G, et al. Melanoma peptide MART-1(27-35) analogues with enhanced binding capacity to the human class I histocompatibility molecule HLA-A2 by introduction of a beta-amino acid residue: implications for recognition by tumor-infiltrating lymphocytes. J Med Chem. 2000;43(20):3803-3808.
[2]. Loftus DJ, et al. Identification of epitope mimics recognized by CTL reactive to the melanoma/melanocyte-derived peptide MART-1(27-35). J Exp Med. 1996;184(2):647-657.