Enzymes

GLP-1(7-37) is a truncated form of GLP-1 (glucagon-like peptide-1), due to posttranslational processing of the proglucagon peptide in the intestinal L-cells. It is an insulinotropic hormone, playing a crucial role in insulin secretion.

GLP-1(7-37) is a truncated form of GLP-1 (glucagon-like peptide-1), due to posttranslational processing of the proglucagon peptide in the intestinal L-cells. It is an insulinotropic hormone, playing a crucial role in insulin secretion.

GLP-1(7-37) is a truncated form of GLP-1 (glucagon-like peptide-1), due to posttranslational processing of the proglucagon peptide in the intestinal L-cells. It is an insulinotropic hormone, playing a crucial role in insulin secretion.

GLP-1 (7-36) amide is a GLP-1 (glucagon-like peptide-1) is the GLP-1 secreted peptide. It acts on insulin secretion, glucagon secretion and can reduce gastric emptying. It is secreted by the L-cels of the intestinal mucosa and it is degraded by DPP-IV (dipeptidyl-peptidase-IV).

GLP-1 (7-36) amide is a GLP-1 (glucagon-like peptide-1) is the GLP-1 secreted peptide. It acts on insulin secretion, glucagon secretion and can reduce gastric emptying. It is secreted by the L-cels of the intestinal mucosa and it is degraded by DPP-IV (dipeptidyl-peptidase-IV).

Recombinant Human Prostasin (Legacy Tebubio ref. 167130-23). This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. Prostasin is highly expressed in prostate epithelia and is one of several proteolytic enzymes found in seminal fluid. The proprotein is cleaved to produce a light chain and a heavy chain which are associated by a disulfide bond. It is active on peptide linkages involving the carboxyl group of lysine or arginine. Recombinant Human Prostasin is a 32.1 kDa, 298 amino acid polypeptide consisting of a 12 amino acid light chain, a 278 amino acid heavy chain, and an 8 amino acid C-terminal His-tag. As a result of glycosylation, Recombinant Human Prostasin migrates to an apparent molecular weight of 31-37 kDa by SDS PAGE analysis, under reducing and non-reducing conditions.

Recombinant Human Prostasin (Legacy Tebubio ref. 167130-23). This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. Prostasin is highly expressed in prostate epithelia and is one of several proteolytic enzymes found in seminal fluid. The proprotein is cleaved to produce a light chain and a heavy chain which are associated by a disulfide bond. It is active on peptide linkages involving the carboxyl group of lysine or arginine. Recombinant Human Prostasin is a 32.1 kDa, 298 amino acid polypeptide consisting of a 12 amino acid light chain, a 278 amino acid heavy chain, and an 8 amino acid C-terminal His-tag. As a result of glycosylation, Recombinant Human Prostasin migrates to an apparent molecular weight of 31-37 kDa by SDS PAGE analysis, under reducing and non-reducing conditions.

Recombinant Human Furin (Legacy Tebubio ref. 167450-47-100). Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Furin is a calcium-dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa-(K/R)-R, where Xaa can be any amino acid. Recombinant Human Furi

Recombinant Lysobacter Enzymogenes Arg-C (Legacy Tebubio ref. 167450-54-100). Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Arg-C specifically cleaves at the carboxyl side of Arginine residues. Arg-C has a sulfhydryl requirement; it is activated by dithiothreitol, cysteine, or other sulfhydryl-containing reagents. The presence of calcium ions is essential. The enzyme is inhibite