I_Products

ProBlock™-50, EDTA Free is designed for large volumes of extraction/lysis buffers and is supplied as 1 vial/kit (Cat# GB-326-1), 10 vials /kit (Cat# GB-326-10) or 20 vials/kit (Cat# GB-326-20), with each vial suitable for 50 ml.

ProBlock-50, EDTA Free protease inhibitor cocktail contains optimized concentrations of various protease inhibitors, which provide excellent inhibition of protease activities during protein purification. ProBlock™ is a superior general protease inhibitor cocktail that is suitable for purification from mammalian, plant, bacteria and yeast samples. The cocktail is EDTA free and contains both irreversible and reversible protease inhibitors to inhibit serine, cysteine and other proteases. At 1X concentration, ProBlock™ inhibits over 90% of protease activities (e.g. Mouse Pancreas Extract 0.5 mg/ml protein).

ProBlock™-50, Plus EDTA is designed for large volumes of extraction/lysis buffers and is supplied as 10 vials /kit (Cat# GB-334-10) or 20 vials/kit (Cat# GB-334-20), with each vial suitable for 50 ml sample. EDTA [0.5M, 100X] is also supplied with this kit as an optional metalloprotease inhibitor.

ProBlock™-50, Plus EDTA protease inhibitor cocktail contains optimized concentrations of various protease inhibitors, which provide excellent inhibition of protease activities during protein purification. ProBlock™ is a superior general protease inhibitor cocktail that is suitable for purification from mammalian, plant, bacteria and yeast samples. The cocktail contains both irreversible and reversible protease inhibitors to inhibit serine, cysteine and other proteases. EDTA is packed separately for inhibiting metalloproteases. At 1X concentration, ProBlock™ inhibits over 90% of protease activities (e.g. Mouse Pancreas Extract 0.5 mg/ml protein).

Simple Stop™ 1 is a broad-spectrum phosphatase inhibitor cocktail consisting of five phosphatase inhibitors in two solutions that target all the phosphatase categories: serine/threonine (Ser/Thr) specific phosphatase, tyrosine specific phosphatase, dual specificity phosphatases, acid phosphatase and alkaline phosphatase.

Each Simple Stop™ phosphatase inhibitor cocktail solution is a 100X concentrated, ready-to-use, solution. Simply add cocktail solution “A” and cocktail solution “B” to your extraction buffers or samples and you are ready to go. This cocktail is ideal for inhibition in tissue extractions and cell lysis experiments and is compatible with most common protein assays.

Simple Stop™ 2 is a broad-spectrum phosphatase inhibitor cocktail consisting of five phosphatase inhibitors in two solutions that target all the phosphatase categories: serine/threonine (Ser/Thr) specific phosphatase, tyrosine specific phosphatase, dual specificity phosphatases, acid phosphatase and alkaline phosphatase.

Each Simple Stop™ phosphatase inhibitor cocktail solution is a 100X concentrated, ready-to-use, solution. Simply add cocktail solution “A” and cocktail solution “B” to your extraction buffers or samples and you are ready to go. This cocktail is ideal for inhibition in tissue extractions and cell lysis experiments and is compatible with most common protein assays.

Simple Stop^TM 3 is a phosphatase inhibitor cocktail consisting of three phosphatase inhibitors that target alkaline and serine/threonine phosphatases. It is a stabilized solution of cantharidin, bromotetramisole and microcystin LR. It is compatible with IEF/2D studies.

The Simple Stop^TM phosphatase inhibitor cocktails are 100X concentrated, ready-to-use solutions that are simply added to your extraction buffers or samples. They are ideal for inhibition in tissue extractions and cell lysis experiments and are compatible with most common protein assays.

Trypsin inhibitor is a serine protease inhibitor from soybeans that is specific for trypsin and trypsin-like proteases. Trypsin inhibitor from soybeans is a monomeric protein containing 181 amino acid residues in a single polypeptide chain cross-linked by two disulfide bridges. Soybean trypsin inhibitor forms a 1:1 complex with the active protease site. Inhibition may be reversed and is pH dependent. The optimal pH for trypsin binding is 8.0.