What is leupeptin used for?

Leupeptin, also known as N-acetyl-L-leucyl-L-leucyl-L-argininal, is a naturally occurring protease inhibitor that can inhibit cysteine, serine and threonine peptidases. It is often used during in vitro experiments when a specific enzymatic reaction is being studied.

How does Leupeptin inhibit trypsin?

Aprotinin is a competitive serine protease inhibitor blocking the activity of trypsin, chymotrypsin, kallikrein and plasmin. The inhibitory mechanism of aprotinin is to form stable complexes with the proteases and thus to block the active sites of enzymes.

How do you dissolve Leupeptin?

Leupeptin: Dissolve 50 mg in 10.5 ml of water to get 10 mM stock (1000X). Working concentration is 10 µM, so add 1µl of stock in 1 ml of lysis buffer.

How do you use protease inhibitor tablets?

To use Pierce Protease Inhibitor Tablets, simply dissolve 1 tablet in 50 mL of buffer or lysate. The protease inhibitor formulation is compatible with most detergent-based cell lysis reagents, including Pierce Cell Lysis solutions. Pierce Protease Inhibitor Tablets do not contain phosphatase inhibitors.

What is aprotinin used for?

Aprotinin, also known as bovine pancreatic trypsin inhibitor or BPTI (Trasylol, Bayer), is a drug used to reduce bleeding during cardiopulmonary bypass (CPB). Aprotinin slows down fibrinolysis, the process that leads to the breakdown of blood clots.

What does cathepsin B do?

Structurally, cathepsin B is a bilobal protein with cysteine, histidine, and aspartic acid forming active site of the enzyme at the interface between the two lobes [37]. Cathepsin B can function as an endopeptidase, cleaving internal peptide bonds, as well as an exopeptidase (carboxydipeptidase activity) [37, 38].

How does PMSF inhibit trypsin?

Thermo Scientific PMSF is a protease inhibitor that reacts with serine residues to inhibit trypsin, chymotrypsin, thrombin and papain. In addition to inhibiting serine proteases, PMSF will also inhibit cysteine proteases, like papain (reversible by DTT treatment), and mammalian acetylcholinesterase.

How do you dissolve pepstatin?

Pepstatin A is only sparingly soluble in water. 4 It is normally dissolved in a solvent such as ethanol, methanol, or DMSO and diluted into buffer. The stock solution should be of a concentration that the solvent used is diluted at least 1000X in the working solution.

How much Pmsf do I add?

To prepare a 100 mM solution, add 17.4 mg of PMSF per milliliter of isopropanol. Store at −20°C. PMSF is inactivated in aqueous solutions. The rate of inactivation increases with increasing pH and is faster at 25°C than at 4°C.