4 Citations

• Species :
  Human
• Description
  Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin.Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

1 Citations

• Species :
  Bovine
• Description
  Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. Enterokinase will not work if the recognition site is followed by a proline. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.

• Species :
  Human
• Reconstitution
  Reconstitute the lyophilized protein in distilled water up to 100 μg/mL.
• Description
  Mammary serine protease inhibitor (Maspin), also known as serpin B5 is a non-inhibitory serpin that is encoded by the SERPINB5 gene in humans. The protein is expressed predominantly in normal mammary epithelial cells but at significantly reduced levels or absent in most breast carcinomas. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. The maspin functions as tumor suppressor, blocking the growth, invasion, and metastatic properties of mammary tumors. This anti-tumor activity is achieved, in part, by the ability of maspin to inhibit angiogenesis and to preferentially promote apoptosis of tumor cells.

3 Citations

• Description
  PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro (LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as well.

1 Citations

• Description
  Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the Tobacco Etch Virus (TEV). The optimum recognition site for this enzyme is the sequence Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) [ENLYFQ(G/S)] and cleavage occurs between the Gln and Gly/Ser residues, The most commonly used sequence is ENLYFQG. The protease is used to cleave affinity Tobacco Etch Virus Protease (rTEV) contains 231 amino acids with N-terminal His tagged. A fully biologically active molecule, rTEV has a molecular mass of 28.4 kDa and is obtained by proprietary chromatographic techniques at GenScript.

• Reconstitution
  We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
• Description
  Staphylokinase (SAK), a 16kDa profibrinolytic protein from the Staphylococcus aureus, has been demonstrated to induce highly fibrin-specific thrombolysis in both human plasma and in limited clinical trials. Recent studies on the thrombolytic potential of recombinant SAK in achieving early perfusion in myocardial infarction and in the dissolution of platelet-rich clot have clearly established its immense utility in clinical medicine as a thrombolytic agent and suggested that it can be developed as a potent clot-dissolving agent.

• Species :
  Bovine
• Reconstitution
  Reconstitute lyophilized EK powder in sterile deionized water at 1mg/ml, then dilute in EK Dilution/Storage Buffer according to your requirement.
• Description
  Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys(DDDDK↑). Enterokinase will not work if the recognition site is followed by a proline. rbEKhas the highest activity than EK of other species and is used wildly in biochemical applications. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed to be removed from digestion system. Recombinant Bovine Enterokinase (His-tagged) (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 × His at C-terminus. A fully biologically active molecule, rbEK has a molecular mass of 40 kDa and is obtained by proprietary chromatographic techniques at GenScript.