aKMT Protein, Sulfolobus islandicus (His, Strep)

Lysine methyltransferase (aKMT) is responsible for catalyzing the methylation of lysine residues in target proteins, using S-adenosyl-L-methionine (SAM) as a methyl donor. The enzyme exhibits broad substrate specificity, showing methylation primarily at "Lys-11", "Lys-16" and "Lys-31" of the vault chromatin protein Cren7 as well as several recombinant Sulfolobus proteins in vitro Ability. aKMT Protein, Sulfolobus islandicus (His, Strep) is the recombinant aKMT protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of aKMT Protein, Sulfolobus islandicus (His, Strep) is 160 a.a., .

The aKMT protein functions as a lysine methyltransferase, catalyzing the methylation of lysine residues in target proteins. This enzymatic activity is accomplished using S-adenosyl-L-methionine (SAM) as the methyl donor. aKMT displays broad substrate specificity and has the capability to methylate various target proteins. In particular, it has been observed to methylate the crenarchaeal chromatin protein Cren7 at specific lysine residues, including 'Lys-11,' 'Lys-16,' and 'Lys-31.' Additionally, aKMT exhibits sequence-independent lysine methylation, showcasing its versatility in modifying a range of target proteins in vitro.

Others

E. coli

N-Strep;N-6*His

F0NBH8 (S2-K161)

8761611

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.