Protease

Carboxypeptidase C is a carboxypeptidase, is often used in biochemical studies. Carboxypeptidase C removes COOH-terminal lysine, arginine, and proline, as well as all other neutral, aliphatic, aromatic, and the acidic protein amino acids of a peptide chain.

Endoproteinase Arg-C is a serine endoproteinase that hydrolyzes peptide bonds on the carboxyl side of arginyl residues and has esterase and amidase activities. Endoproteinase Arg-C can be isolated from Clostridium histolyticum. Endoproteinase Arg-C is of mass spectrometry grade and can be used for peptide mapping, sequence analysis, cell separation.

Leucine Aminopeptidase(microsomal), Porcine (EC 3.4.11.2) is an enzyme that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins.

IdeS (Immobilized, Microspin) is a resin that covalently couples IdeS protease to agarose beads and cleaves IgG at specific sites to generate F(ab')2 and Fc fragments. After IdeS (Immobilized, Microspin) digestion, F(ab')2 and Fc fragments are obtained in the solution without IdeS enzyme.

Protease (Gly Cleaving) can be used to digest flexible linkers of fusion proteins composed of glycine or glycine and serine residues, repeating sequences, such as (Gly4Ser)n, GlyxSery (GS), and poly-glycine (G) linkers.

SpeB cysteine protease is a potent modifier of immunologically important host and bacterial proteins. SpeB cysteine protease degrades streptolysin O (SLO) in extracellular vesicles.

Cephalosporinase, bacillus are enzymes produced by bacillus, inactivated and degrade the ability of the cephalosporin class of antibiotics. Cephalosporins are a class of β-lactam antibiotics that are widely used to study bacterial infections.

Keratinase (KerA) is an orally active proteolytic enzyme that specifically degrades keratin, and it is mainly secreted by microorganisms such as bacteria, fungi and actinomycetes. Keratinase degrades keratin via reducing disulfide bond cross-links and cleaving peptide bonds, and it can also degrade infectious prion proteins. Keratinase can improve the nutritional bioavailability of keratin-based feed, and it can also be applied in various fields including depilation, proteolytic cleaning, organic fertilizer precursor preparation, cosmetics, bioenergy production, wastewater decolorization, biomolecule extraction, bioremediation, textile biopretreatment and feed processing.

Acetyltrypsin, Bovine pancreas is a stable trypsin derivative that can catalyze the hydrolysis of alpha-N-benzoyl-L-argininamide.

D-Aminoacylase (E.C. 3.5.1.81) catalyzes the enantioselective hydrolysis of Nacyl-D-amino acids to produce D -amino acids.

(R)-Mandelonitrile lyase (Mandelonitrile Lyase) is an enzyme that can be isolated from Prunus species.

Peptidase (IMPa) (Erepsin) is catalytically active enzyme that cleaves peptide bonds in proteins and peptides by hydrolysis.

50S Ribosomal protein L16 3-hydroxylase (EC 1.14.11.47) is an oxidoreductase that can convert L-arginyl-[ribosomal protein uL16], 2-oxoglutarate and O₂ into (3R)-3-hydroxy-L-arginyl-[ribosomal protein uL16], succinate and CO₂.

γ-D-Glutamyl-meso-diaminopimelate peptidase (EC 3.4.19.11) is a 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14 (carboxypeptidase A family) . Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism.

β-Aspartyl-peptidase (EC 3.4.19.5) is a mammalian, cytosolic enzyme.

γ-D-Glutamyl-L-lysine dipeptidyl-peptidase (EC 3.4.14.13) , characterized from the bacterium Bacillus subtilis, is involved in the recycling of the murein peptide.

α-Lytic endopeptidase (EC 3.4.21.12) belongs to the peptidase family S1 (trypsin family).

β-Lytic metalloendopeptidase (EC 3.4.24.32) digests bacterial cell walls. Type example of peptidase family M23.

β-Peptidyl aminopeptidase (EC 3.4.11.25) catalyses the following chemical reaction: cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids.

Carboxypeptidase-B rat (EC 3.4.17.2) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. Carboxypeptidase-B rat (EC 3.4.17.2) may be used for sequence analysis by successive cleavage of C-terminal basic amino acids.