Bst DNA Polymerase Protein, Geobacillus stearothermophilus (His)

Bst DNA Polymerase protein, featuring polymerase and 5'-3' exonuclease activities, exhibits versatile nucleic acid processing capabilities. Beyond synthesizing DNA strands, it adeptly removes nucleotides from the 5' to 3' direction. These dual functions render Bst DNA Polymerase pivotal in molecular biology applications, ensuring efficient DNA amplification and modification processes. Bst DNA Polymerase Protein, Geobacillus stearothermophilus (His) is the recombinant Bst DNA Polymerase protein, expressed by E. coli , with N-6*His labeled tag. The total length of Bst DNA Polymerase Protein, Geobacillus stearothermophilus (His) is 584 a.a., with molecular weight of ~66.4 kDa.

In addition to its polymerase activity, the Bst DNA Polymerase protein demonstrates 5'-3' exonuclease activity. This dual functionality highlights the enzyme's versatility in nucleic acid processing, as it not only synthesizes DNA strands but also possesses the capability to remove nucleotides from the 5' to 3' direction. The combined actions of polymerase and exonuclease activities make Bst DNA Polymerase a crucial tool in various molecular biology applications, contributing to efficient DNA amplification and modification processes.

Others

E. coli

N-6*His

E1C9K5 (F301-K876)

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DQSLFAIADSVTDEMLADKAALVVEVVGDNYHHAPIVGIALANERGRFFLRPETALADPKFLAWLGDETKKKTMFDSKRAAVALKWKGIELRGVVFDLLLAAYLLDPAQAAGDVAAVAKMHQYEAVRSDEAVYGKGAKRTVPDEPTLAEHLVRKAAAIWALEEPLMDELRRNEQDRLLTELEQPLAGILANMEFTGVKVDTKRLEQMGAELTEQLQAVERRIYELAGQEFNINSPKQLGTVLFDKLQLPVLKKTKTGYSTSADVLEKLAPHHEIVEHILHYRQLGKLQSTYIEGLLKVVHPVTGKVHTMFNQALTQTGRLSSVEPNLQNIPIRLEEGRKIRQAFVPSEPDWLIFAADYSQIELRVLAHIAEDDNLIEAFRRGLDIHTKTAMDIFHVSEEDVTANMRRQAKAVNFGIVYGISDYGLAQNLNITRKEAAEFIERYFASFPGVKQYMDNIVQEAKQKGYVTTLLHRRRYLPDITSRNFNVRSFAERTAMNTPIQGSAADIIKKAMIDLSVRLREERLQARLLLQVHDELILEAPKEEIERLCRLVPEVMEQAVTLRVPLKVDYHYGPTWYDAK

Approximately 66.4 kDa

Greater than 95% as determined by reducing SDS-PAGE.