Enzyme

<p>CA inhibitor 10 targets MCF-7 cells, IC50: 11.9 μM; potent h CA IX inhibitor, Ki: 6.2 nM. Anti-cancer research.</p>

<p>β-Glucuronidase/hCAII-IN-2 (Compound 12e) is a compound that effectively inhibits both β-glucuronidase and human Carbonic Anhydrase II (hCA II), exhibiting IC50</p>

<p>NSC 828467 is one of the top five CA-IX inhibitors with significant in vitro anticancer activity (IC50: 27.2 nM).</p>

<p>Valerate sodium is a potential Carbonic anhydrase 1/2 inhibitor for biochemical experiments.</p>

<p>Isobutylamido thiazolyl resorcinol is a tyrosinase (Tyrosinase) inhibitor that prevents pigment deposition induced by ultraviolet radiation.</p>

<p>α-Glucosidase-IN-63 (Compound 4d) serves as an α-Glucosidase inhibitor with an IC 50 value of 0.44 μM. Additionally, it exhibits inhibitory activity against hCA II, demonstrating a K i of 7.0 nM. The compound is also effective when administered orally. [1]</p>

<p>Carbonic anhydrase inhibitor 3 (compound 11g) is an inhibitor of carbonic anhydrase II that reduces the intraocular pressure in glaucomatous rabbits [1].</p>

<p>Tyrosinase-IN-29 (compound 5c) is an effective inhibitor of abTYR tyrosinase, demonstrating an IC50 value of 6.11 μM. It is suitable for further research into the inhibition of excessive skin pigmentation.</p>

<p>hCAVII/IX-IN-1 (compound 4) functions as an inhibitor of hCAVII/IX, exhibiting Ki values of 56.5 nM and 38.2 nM, respectively. It is applicable in the field of cancer research.</p>

<p>Tyrosinase-IN-39 (compound 5r) is a competitive inhibitor of tyrosinase, with an IC50 of 6.4 μM, and is used in the study of skin diseases.</p>

<p>CAII-IN-1 (3n) is a selective bovine CA-II inhibitor with 10.3 μM IC50, used in carbonic anhydrase disorder studies.</p>

<p>hCAI/II/XII-IN-1 (compound 7) is an inhibitor of human carbonic anhydrases hCAI, hCAII, and hCAXII, with Ki values of 78.5 nM, 9.1 nM, 605 nM, 7.7 nM, and 3.7 nM.</p>

<p>AChE/CA I-IN-1 (Compound 2g) acts as an inhibitor for both AChE and hCA I, with Ki values of 1.85 µM and 0.53 µM, respectively. It has shown potential applications in the research of Alzheimer's disease, glaucoma, and epilepsy.</p>

<p>β-Glucuronidase/hCAII-IN-2 is a potent inhibitor of β-glucuronidase and hCA II, and their IC50 values were 670.7 μM and 21.77 μM, respectively.</p>

<p>Expression system: HEK297 Cells&lt;br&gt;Length: 21-472, Full Length of Mature Protein&lt;br&gt;Activity: Not Tested</p>

<p>Expression system: E. coli&lt;br&gt;Length: 1-169, Partial&lt;br&gt;Activity: BLI</p>

<p>Carboxypeptidase B2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.</p>

<p>Carbonic Anhydrase 9 Protein, Human, Recombinant (His &amp; Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag.</p>

<p>Fructose-2,6-biphosphatase 3, also known as 6-phosphofructo-2-kinase or PFK2 or PFKFB3, is a potent activator of phosphofructokinase, which is a rate-limiting</p>

<p>GUCY2C Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.</p>

<p>GUCY2C Protein, Canine, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.</p>

<p>ACE2/ACEH Protein, Human, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with hFc tag.</p>

<p>Protein kinase C iota type, also known as Atypical protein kinase C-lambda/iota, aPKC-lambda/iota and PRKCI, is a cytoplasm, membrane and nucleus protein which</p>

<p>VEGFR3/FLT4 Protein, Human, Recombinant (His &amp; Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag.</p>

<p>Glucosyltransferase201-freeze dried is an enzymatic preparation that is primarily sourced from bacterial or plant organisms. It functions by catalyzing the transfer of glucose moieties from donor molecules, such as UDP-glucose, to specific acceptor molecules, thus forming glycosidic bonds. This mode of action is crucial in the biosynthesis and modification of polysaccharides and glycoconjugates.</p>

<p>Peroxidase 12 recombinantly expressed in P. pastoria comes in a freeze-dried formulation. It has its pH optimum at 5-8 and temp. optimum at 20-40°C. Peroxidases can be utilized as enzymes catalyzing e.g. aromatic ring hydroxylation, epoxidation, halogenation, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. Peroxidase 12 was shown to act on styrene, veratryl alcohol, vanillyl alcohol, n-methyl anthranilate and thioanisole.</p>

<p>Phospholipase D 040, concentrated (100 U/mg), spray-dried, recombinant, of prokaryotic origin, is an enzyme preparation designed for advanced biochemical applications. This enzyme is derived from a prokaryotic source through recombinant DNA technology, allowing for high purity and activity. Phospholipase D functions by catalyzing the hydrolysis of phospholipids to produce phosphatidic acid and free head groups, which is a crucial reaction in both lipid signaling and membrane dynamics.</p>

<p>A proprietary potent and stable alternative to chemical neutralizers such as pyruvate - for the utilization in environmental monitoring applications. Use of catalase as a supplement in media plates offers a more effective and reliable solution for safe and secure environmental monitoring of sterilization in clean rooms, isolators or production facilities by also removing remaining traces and spots of high concentration of H2O2. Currently, agar plates for monitoring disinfection or sterilization are supplemented with pyruvate, which is consumed during the neutralization of hydrogen peroxide. One of the main benefits of this catalase is its high stability in agar media at 50°C, which allows easy preparation of media and processing into plates. Due to the high stability no special storage conditions are needed and a shelf-life of &gt; 6 months at 4-25°C can be guaranteed.<br>Key features are:</p>

<p>Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications.</p>

<p>Freeze-dried powder with 3300 IU beta-lactamase I activity per vial against all relevant penicillins.  Our penase (penicillinase) posesses a specific substrate range solely against all relevant penicillins.</p>

<p>A catalase product which neutralizes hydrogen peroxide at much higher concentrations (&gt;10 %) compared to pyruvate, which is only capable of completely neutralizing hydrogen peroxide at the lowest concentration tested (2 %). Catalase (EC 1.11.1.6) catalyzes the following reaction:2H2O2 → 2H2O + O21 unit of catalase will decompose 1.0 μmole of H2O2 per min at pH 7.0 and 25 °C.</p>

<p>ALPK1 Protein, Human, Recombinant (His &amp; Myc) is expressed in Baculovirus.</p>

<p>The kit contains 8 different Glucosyltransferases (GTases), which are enzymes that transfer glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities, as shown on Table 1. The kit is especially designed for screening and finding the most well-suited GTase for your specific process. All GTases in the kit are also available individually for bulk purchase.</p>

<p>Nitrile hydratase 21 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.</p>

<p>A pyridoxal phosphate-containing enzyme that converts L-methionine to α-ketobutyrate, ammonia and methyl mercaptan. Recombinant from e.coli source.  <br>EC 4.4.1.11</p>

<p>A protease enzyme from bacillus subtilis which catalyzed proteolysis, a process that breaks down proteins and peptides to small polypeptides or amino acids</p>