Proteinase K
(#1019-20, 1019-20-5)
Enzyme for digesting proteins in biological samples.
A&A Biotechnology is offer in house produced, recombined, DNA / RNA free, Proteinase K of a highest available purity grade at extremely attractive pricing.
Enzyme description
Proteinase K is one of the most active endopeptidases ever known. This serine-like protease exhibits extremely effective degradation of both native and denatured proteins. Proteinase K is widely recommended for quick deactivation of endogenous RNAses and DNAses within the first steps of nucleic acids isolation.
• Highest quality due to unprecedented purity grade
• Totally DNA / RNA free enzyme, dedicated to applications sensitive to exogenous nucleic acids
• DNAse and RNAse free product
Lysozyme
(#1005-10, 1005-50)
Enzyme for efficient lysis of Gram-negative and Gram-positive bacteria cell wall.
Lysozyme is a glycoside hydrolase that damages the bacterial peptidoglycan cell wall by catalysing a hydrolysis of
1.4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine.
Lyticase
(#1018-10, 1018-50)
Lyticase is an enzymatic mixture for yeast cell wall lysis. The main component of Lyticase is β-1,3 glucanase, that hydrolyses poly-β(1–›3)-glucose such as yeast cell wall glucan.
Mutanolysin
(#1017-5, 1017-10, 1017-50)
Recombinant mutanolysin effectively digests cell wall of particulary resistant to lysis bacteria. Including but not limited to: Streptococcus, Lactobacillus, Lactococcus and Listeria.
Mutanolysin (EC 3.2.1.17) (Nacetylmuramidase) is a muralytic enzyme that cleaves the β-N-acetylmuramyl-(1→4)-N-acetylglucosamine linkage of the bacterial cell wall peptidoglycanpolysaccharide. Its carboxy terminal moieties are involved in the recognition and binding of unique cell wall structures abundant in many gram-positive bacteria.
Application
• Mild conditions formation of spheroplasts of gram-positive bacteria
• Enzymatic cell lysis in DNA and RNA isolation process
• Effective lysis of gram-positive bacteria in environmental studies and DNA-based microbial detection