Proteases

General description Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin.

α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein. The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.

α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein. The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.

Protein Purity&gt:95% by SDS-PAGEExtinction Coeff.A280 nm = 8.9 at 1.0 mg/mlMolecular Weight93,000 Da (1 chain)General DescriptionC2 is central to the activation of both the classical and the lectin pathways of complement. It forms the proteolytic

Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 10.16 at 1.0 mg/ml for pure C3Molecular Weight~185,000 Da (2 chains)General DescriptionRabbit C3 is purified from pooled normal rabbit serum. C3 is central to the activation of all three

Protein Purity&gt:90% by SDS-PAGEExtinction Coeff.A280 nm = 1.03 at 1.0 mg/mLMolecular Weight205,000 Da (3 chains)General DescriptionNative human C4 is a naturally glycosylated polypeptide containing three disulfide-linked chains. C4 is central to

Protein Purity&gt:90% by SDS-PAGEExtinction Coeff.A280 nm = 1.03 at 1.0 mg/mLGeneral DescriptionC4b is derived from native C4 upon proteolytic cleavage by C1s and release of C4a. C4b is central to the function of both the classical and lectin

Application Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been

Application Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been

Application Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been

Carboxypeptidase A (CPA) is a secreted protease is liberated after the activation of mast cells to facilitate acute anaphylaxis. Carboxypeptidase A has a long half-life in vivo, when compared to other secreted proteases.

Carboxypeptidase A (CPA) is a secreted protease is liberated after the activation of mast cells to facilitate acute anaphylaxis. Carboxypeptidase A has a long half-life in vivo, when compared to other secreted proteases.