Merck Proteinase K from Tritirachium album

Proteinase K from Tritirachium album

free of DNA contaminants, suitable for Microbiome research, lyophilized powder, ≥30 units/mg protein

Endopeptidase K, Proteinase K from Tritirachium album

Quality Level

200

specific activity

30 units/mg protein

분자량

28.93 kDa

특징

DNA free

배송 상태

wet ice

저장 온도

−20°C

Purified Proteinase K DNA free SAE0151 undergoes strict quality control testing to ensure the absence of detectable levels of contaminating DNA using 35 cycles PCR amplification of 16S and 18S rDNA using universal primer sets.

Proteinase K is a stable serine protease with broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents. Proteinase K was isolated from a fungus able to grow on keratin and the enzyme can digest native keratin. The enzyme belongs to the subtilisin family with an active site catalytic triad (Asp39 -His69 -Ser224).
The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity. Proteinase K is usually denatured by subsequent phenol extractions.

The study of microbial communities has been revolutionized in recent years by the widespread adoption of culture independent analytical techniques such as 16S rRNA gene sequencing and metagenomics. Since DNA contamination during sample preparation is a major problem of these sequence-based approaches, DNA extraction reagents free of DNA contaminates are essential.