Single-Stranded DNA Binding Protein (SSB) preferentially binds single-stranded DNA, forming a tetramer of four identical 18.9 kDa subunits which protects 8-16 nucleotides.
Extreme Thermostable SSB is a single-stranded DNA binding protein isolated from a hyperthermophilic microorganism, which remains fully active after incubation at 95°C for 60 minutes.
RecA Protein (E. coli) is necessary for genetic recombination reactions involving DNA repair and UV-induced mutagenesis. RecA promotes the autodigestion of the LexA repressor, UmuD protein and lambda repressor.
Tth RecA is a RecA homolog isolated from Thermus thermophilus. It has a ssDNA-dependent ATPase activity at an optimal temperature between 65 to 75ºC. The extreme thermostability makes Tth RecA ideal for molecular biology applications that require an elevated temperature condition, such as nucleic acid amplification and sequencing.
