Proteases and Surfactants

Rapid Digestion-Trypsin and -Trypsin/Lys-C Kits

Minimize protein digestion time, maximize data output.

VA1060, VA1061

Sequencing Grade Modified Trypsin

Trypsin manufactured for maximum specificity.

V5111, V5117, V5113

Mass Spec-Compatible Yeast and Human Protein Extracts

Yeast and human protein extracts for mass spec applications such as instrument monitoring.

V7461, V7341, V6951, V6941

IdeS and IdeZ Proteases

IgG-degrading enzymes that cleave at a single site below the hinge region.

V7511, V7515, V7512, V8341, V8345, V8342

Trypsin/Lys-C Mix, Mass Spec Grade

A mixture of Trypsin Gold, Mass Spec Grade, and rLys-C, Mass Spec Grade, designed to improve digestion of proteins or protein mixtures in solution.

V5071, V5072, V5073

PNGase F

Catalyzes cleavage of N-linked oligosaccharides between the innermost GlcNAc and asparagine residues.

V4831

Thermolysin

A thermostable metalloproteinase whose high digestion temperature may work as a denaturant, improving digestion of proteolytically resistant proteins.

V4001

Pepsin

Cleaves at the C-terminus of phenylalanine, leucine, tyrosine and tryptophan. Pepsin activity is optimal at pH 1.0–3.0.

V1959

Elastase

Serine protease that preferentially cleaves at the C-terminus of alanine, valine, serine, glycine, leucine and isoleucine.

V1891

Arg-C, Sequencing Grade

Sequencing grade endopeptidase for use alone or in combination with other proteases for protein analysis by mass spectrometry.

V1881

rLys-C, Mass Spec Grade

Cleaves at the carboxyl side of lysines. Retains proteolytic activity under denaturing conditions such as 8M urea, used with proteolytically resistant proteins.

V1671

ProTEV Plus

Engineered protease with greater stability, prolonged activity over native TEV protease.

V6101, V6102

Glu-C, Sequencing Grade

Cleaves at the C-terminus of either aspartic or glutamic acid residues and has optimal activity at pH of 4.0–9.0.

V1651

Asp-N, Sequencing Grade

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

V1621

Factor Xa Protease

Preferentially cleaves after the arginine residue in the amino acid sequence Ile-Glu-Gly-Arg.

V5581