Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme is a carboxypeptidase with optimum activity at pH 4.5-6.0. It is inhibited by d
Creative Enzymes [2015-11-16 15:05:25 ]
Cathepsin B has been found to cleave procaspase 1 and procaspase 11 and to induce apoptosis in digitonin-permeabilized cells. Translocation of cathepsin B from the cytoplasm to the nucleus contributes to bile salt induced apoptosis of Rat hepatocytes. Levels of cathepsin B in PC1
Creative Enzymes [2015-11-16 15:04:45 ]
Human rhinovirus 3C protease (HRV3C Protease) is a cysteine protease that recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln*Gly-Pro. It is supplied as a 47 kDa protein with both GST and Histidine tags for easy removal by His-Select or Glutathione agarose along with the clea
Creative Enzymes [2015-11-16 15:03:23 ]
β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. SubstRates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. https://www cre
Creative Enzymes [2015-11-16 15:02:10 ]
β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. SubstRates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. https://www cre
Creative Enzymes [2015-11-16 15:01:17 ]
β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. https://www cre
Creative Enzymes [2015-11-16 14:59:51 ]
Chitinase is an extracellular enzyme complex that degrades chitin and has a molecular mass of approximately 30 kDa. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase. The second re
Creative Enzymes [2015-11-16 14:58:25 ]
Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has s
Creative Enzymes [2015-11-16 14:57:47 ]
Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has s
Creative Enzymes [2015-11-16 14:56:57 ]
Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has s
Creative Enzymes [2015-11-16 14:55:23 ]
Catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-b
Creative Enzymes [2015-11-16 14:54:43 ]
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. https://www creative-enzymes com/product/Biotinylated-Transglutaminase-From-Human-Recombinant_16120.html
Creative Enzymes [2015-11-16 14:53:54 ]
Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. These enzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptide-bound gluta
Creative Enzymes [2015-11-16 14:53:12 ]
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. https://www creative-enzymes com/product/Transglutaminase-From-Mouse-Recombinant_16122.html
Creative Enzymes [2015-11-16 14:52:28 ]
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. https://www creative-enzymes com/product/Biotinylated-Transglutaminase-From-Human-Proenzyme-Zymogen-_16130.htm
Creative Enzymes [2015-11-16 14:51:44 ]
β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. https://www cre
Creative Enzymes [2015-11-16 14:50:48 ]
β-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. https://www creative-enzymes com/product/Native-
Creative Enzymes [2015-11-16 14:50:09 ]
A lipase is an enzyme that catalyzes the hydrolysis of fats (lipids). Lipases are a subclass of the esterases. Lipases perform essential roles in the digestion, transport and processing of dietary lipids (e g. triglycerides, fats, oils) in most, if not all, living organisms. Gene
Creative Enzymes [2015-11-16 14:49:09 ]
Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications, whose wild-type (WT) version cleaves after T, A, S, and V residues. The M190A (Met190 → Ala190) mutant of aLP has different cleavage specificities, and cleaves after M, F, and L resid
Creative Enzymes [2015-11-16 14:48:24 ]
Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications. This protease cleaves after T, A, S, and V residues. It geneRates peptides of similar average length as trypsin. aLP was first isolated from the myxobacterium Lysobacter enzymogenes. Th
Creative Enzymes [2015-11-16 14:47:28 ]
