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Proteases and Protease Inhibitors
 | | | | The proper functioning of the cell requires an optimum level of important structural and regulatory proteins. One mechanism whereby cells achieve a steady state level is by proteolytic degradation. Protein degradation exhibits first order kinetics and is an energy-dependent irreversible process brought about by the action of several peptidases. Peptidases (proteases) can be subdivided into two major groups: the endopeptidases and the exopeptidases, which cleave peptide bonds either at points within the protein or remove amino acids sequentially from either the N- or C-terminus, respectively. The term proteinase is also used as a synonym for endopeptidase. The International Union of Biochemistry and Molecular Biology has recognized four classes of proteases: serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. In vivo, proteins are either protected in specialized compartments or they reside in a protective conformation. Every protein isolated from cells is a potential substrate for proteolytic enzymes. Hence, protease inhibitors are often used in experimental protocols that require extraction and analysis of intact proteins. Calbiochem, a leading supplier of proteases and protease inhibitors is pleased to offer the following new proteases and protease inhibitors for your research needs. | | | | Product Name | Cat. No. | | Procathepsin K, Human, Recombinant, E. coli - NEW! | | | A cysteine proteinase that plays an important role in osteoclast-mediated bone resorption and collagen degradation. Activity: ≥ 1000 mU/mg protein. Purity: ≥ 95% by SDS-PAGE. | | | Renin, Human Kidney | | | Acts on angiotensinogen to produce angiotensin I. Purity: ≥ 90% (NuPAGE gel). | | | HtrA2/Omi, Human, Recombinant, E. coli - NEW! | | | A mitochondrial trypsin-like serine protease that is pivotal in regulating apoptotic cell death. Purity: >85% by SDS-PAGE. | | | Serpin F2/a2-Antiplasmin, His•TagŪ, Human, Recombinant, NSO Cells - NEW! | | | A member of the serpin superfamily of the serine protease inhibitors that is responsible for the dissolution of fibrin clots. Purity: ≥ 95% by SDS-PAGE. | | | HGF Activator, His•TagŪ, Human, Recombinant, NSO Cells - NEW! | | | A serine protease that cleaves the single-chain HGF precursor, generating the active heterodimer. Specific activity: ≥ 15 pmol/min/mg activated HGFA. Purity: ≥ 95% by SDS-PAGE. | | | Proteinase K, Tritirachium album | | | A serine protease that exhibits strong proteolytic activity on a wide variety of denatured and native proteins of high molecular weight. Specific activity: ≥ 20 units/mg dry weight. | | | Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free - NEW! | | | A reversible inhibitor of serine proteases. Does not contain any animal-derived material. Purity: ≥ 95% by SDS-PAGE. | |
| | | | | | Related Resource | | Inhibitor Resource: Protease Inhibitors | | | | | |
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