| Description | Lysyl Endopeptidase cleaves peptide bonds at the carboxy-terminal of both lysine residues and S-aminoethylcysteine residues, making it a valuable tool for analysis of peptide and protein primary structure and for enzymatic synthesis of Lys-X compounds. Also, it can retain complete activity after Lysyl Endopeptidase cleaves peptide bonds at the carboxy-terminal of both lysine residues and S-aminoethylcysteine residues, making it a valuable tool for analysis of peptide and protein primary structure and for enzymatic synthesis of Lys-X compounds. Also, it can retain complete activity after incubation in 4M urea or in 0.1% SDS solution.
This is package is designed for usage with mass spec. samples.
Pkg: 5 x 20ug... Read More | Achromopeptidase Crude has a broad range of activity, lysing the cell walls of many pathological Gram Positive organisms as well as a number of Gram-negative organisms.
Crude: 1,000 units/mg
Origin: Achromobacter lyticus M497-1 F.W.: ~ 20,000
Preparation: Powder (contains lactose)
Optimum pH: 7.5 ~ Achromopeptidase Crude has a broad range of activity, lysing the cell walls of many pathological Gram Positive organisms as well as a number of Gram-negative organisms.
Crude: 1,000 units/mg
Origin: Achromobacter lyticus M497-1 F.W.: ~ 20,000
Preparation: Powder (contains lactose)
Optimum pH: 7.5 ~ 8.5
Pkg: 1 g... Read More | 'Preparation: Lyophilized, salt-free
Specificity: In ammouniun carbonate buffer (pH 7.8 or ammonium acetate buffer (pH 4.0): Cleaves C-terminal peptide bonds of glutamic acid. In phosphate buffer (pH 7.8): Cleaves C-terminal peptide bonds of glutamic acid and aspartic acid.
Pkg: 50 µg | !-- cnDescClose -->Anti OMP is highly specific for mature olfactory neurons and their axons and terminals in tissue sections of many vertebrate species including rodents, humans, marsupials and amphibia. | Activity: min. 20 units/mg
Preparation: Lyophilized form
V8 Protease, a Staphylococcal serine proteinase, specifically cuts the C-end of glutamic acid. Pkg: 2 mg |