Enzymes > Protease Products & Reviews

Trypsin is a serine protease that specifically cleaves at the carboxylic side of lysine and arginine residues.   The stringent specificity of trypsin is essential for protein identification. Native trypsin is subject to autolysis, generating pseudotrypsin, which exhibits a broadened specificity including a chymotrypsin-like activity. Such autolysis products, present in a trypsin preparation, would result in addition…

To shorten the time required to prepare samples for LC-MS/MS analysis, we have developed an optimized protocol in which rapid and efficient trypsin digestion is achieved at temperatures as high as 70°C. Using this approach, proteolytis reaction times are dramatically shortened, no chemical denaturants are added and off-line sample cleanup is unnecessary, leading to shorter preparation times and diminished sample losses.

Mass spectrometry grade for proteome research

Lyophilized enzyme provided with Proteinase K Storage Buffer.

Crude collagenases are widely used in enzymatic primary cell isolation and tissue dissociation procedures. Most researchers employ either crude collagenase preparations such as Types 1, 2, 3, and 4 or chromatographically purified collagenase (the latter usually combined with secondary enzymes such as elastase, hyaluronidase, etc). For best results, the precise mixture of proteolytic activities must be tailored to the tissue to…

Hydrolyzes peptide bonds on the N-terminal side of aspartic and cysteic acid residues (Asp and Cys)

The FabRICATOR Enzyme is supplied as a lyophilized powder with no preservatives added, and is available in 2000 and 5000 unit vials for digestion of up to 2 - 5 mg IgG.

Thermo Scientific Proteinase K is a versatile and non-specific endolytic protease and is an essential tool for a wide array of proteolytic applications. Applications • General digestion of proteins • DNase and RNase inactivation • Cell digestion • Cell surface protein and glycoprotein modifications • Protein structure studies

Widely used in DNA purification, Proteinase K is a broad-spectrum protease from Tritirachium album that is ideal for preparing chromosomal DNA. It cleaves peptide bonds where carbonyl groups are surrounded by aromatic, hydrophobic, or aliphatic amino acids.

IdeS Protease is an immunoglobulin-degrading enzyme from Streptococcus pyogenes (IdeS). It is an engineered recombinant protease overexpressed in E. coli that cleaves Immunoglobulin G (IgG) with high specificity at a single site below the hinge region, yielding F(ab’)2 and Fc fragments. The protocol for a standard reaction is to add the IdeS Protease to the IgG sample, add 1 unit of IdeS Protease per 1µg of IgG to be digested…

IdeZ Protease is an immunoglobulin-degrading enzyme from Streptococcus equi subspecies zooepidemicus. It is an engineered recombinant protease overexpressed in E. coli. Like IdeS Protease, IdeZ Protease specifically cleaves IgG molecules below the hinge region to yield F(ab′)2 and Fc fragments. However, IdeZ Protease has significantly improved activity against mouse IgG2a and IgG3 subclasses compared to IdeS Protease.

Lysyl Endopeptidase, Mass Spectrometry Grade is a freeze dried product that retained sufficient activity for in-gel digestion and packed in very small quantities for convenience purposes.

Trypsin NB with unique resistance to autolytic digestion  for in-gel digestion and mass spec

Mass Spectrometry MS grade manufactured by Wako Pure Chemicals 

Trypsin EDTA Solution B (0.25%), EDTA (0.05%)

Animal component-free cell dissociation solution, Defined alternative to porcine trypsin

Animal component-free cell dissociation solution, Defined alternative to porcine trypsin

suitable for protein sequencing, lyophilized powder

lyophilized powder, for use in Total Dietary Fiber Assay, TDF-100A

Type XIV, ≥3.5 units/mg solid, powder

lyophilized powder, 40-300 NIH units/mg protein (biuret)

lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280, 18.3)

protease

lyophilized powder, 50-150 units/mg protein

Zymolyase® , produced by a submerged culture of Arthrobacter luteus, has strong lytic activity against living yeast cell walls, to produce protoplast or spheroplast of various strains of yeast cells. An essential enzyme for the lytic activity of Zymolyase® is Beta-1,3-glucan laminaripentaohydrolase. It hydrolyzes linear glucose polymers at Beta-1,3-linkages and releases specifically laminaripentaose as the main and minimum pro…