D15 Protein, Escherichia phage T5

D15 Protein, Escherichia phage T5 is the recombinant D15, expressed by E. coli , with tag Free labeled tag.

D15 is an enzyme with both 5'-exonucleolytic and structure-specific endonucleolytic activities, catalyzing the hydrolysis of DNA branched nucleic acid molecules and likely playing a role in viral genome replication. It is active on flap structures (branched duplex DNA containing a free single-stranded 5'-end), 5' overhangs, and pseudo-Y structures. The substrates require a free single-stranded 5' end, with endonucleolytic hydrolysis occurring at the junction of double- and single-stranded DNA. This function may be used, for example, to trim such branched molecules generated by Okazaki fragment synthesis during replication. by similar: The enzyme's function resembles that of other nucleases with similar activities.

Others

E. coli

Tag Free

P06229 (M1-Q291)

2777611

Full Length

MSKSWGKFIEEEEAEMASRRNLMIVDGTNLGFRFKHNNSKKPFASSYVSTIQSLAKSYSARTTIVLGDKGKSVFRLEHLPEYKGNRDEKYAQRTEEEKALDEQFFEYLKDAFELCKTTFPTFTIRGVEADDMAAYIVKLIGHLYDHVWLISTDGDWDTLLTDKVSRFSFTTRREYHLRDMYEHHNVDDVEQFISLKAIMGDLGDNIRGVEGIGAKRGYNIIREFGNVLDIIDQLPLPGKQKYIQNLNASEELLFRNLILVDLPTYCVDAIAAVGQDVLDKFTKDILEIAEQ

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.