Enzimas em Proteínas Recombinantes

<p>Ribonuclease H from Escherichia Coli is the enzyme that breaks down RNA strand in RNA-DNA duplexes. It acts by cleaving the phosphodiester bonds of RNA and produces 3' hydroxyl and a 5' phosphate groups at the cleavage site. A common use of Ribonuclease H is to remove RNA template after reverse transcription reaction.</p>

<p>Adenosine deaminase catalyzes deamination of adenosine, converting it to inosine. It happens by the substituting of the amino group by a keto group. One Unit of the enzyme converts one micromole of adenosine to inosine per minute at 25°C, pH 7.4. Adenosine deaminase is also known by names of adenosine aminohydrolase, and ADA, EC 3.5.4.4.</p>

<p>Lipase 12 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7.5 and temp. optimum at &gt;60°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 12 was shown to hydrolyze p-Nitrophenyl esters of butyrate (60 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (30 %), stearate (14 %), arachidate (0.2 %) and behenate (0.2 %).</p>

<p>Creatinine deiminase (EC 3.5.4.21) in an enzyme that catalyzes the following reaction:  Creatinine + H2O → N-Methylhydantoin + NH3  One unit of creatinine deiminase will hydrolyze 1.0 µmole of creatinine to N-methylhydantoin and ammonia per minute at pH 7.5 and 37°C.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

<p>DNA polymerase is an essential enzymatic protein, derived from various organisms including bacteria, archaea, and eukaryotes, which plays a pivotal role in the replication and repair of DNA. This enzyme functions by adding nucleotides to the growing DNA strand in a template-dependent manner, ensuring the accurate duplication of the genetic material. It operates through a polymerization mechanism, where nucleotides are selected and incorporated complementary to the template strand, facilitating the elongation of the new DNA strand in the 5' to 3' direction.</p>

<p>Phosphoenolpyruvate carboxylase is an enzyme, often found naturally in the cytosol of plant cells, which is derived primarily from various plant species. It plays a crucial role in the photosynthetic process, particularly in C4 and CAM plants. By catalyzing the irreversible carboxylation of phosphoenolpyruvate (PEP) to oxaloacetate, this enzyme facilitates the fixation of carbon dioxide, a vital step in the conversion of carbon dioxide into organic compounds during photosynthesis.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

<p>CS2 hydrolase (Carbon disulfide hydrolase; E.C. 3.13.1.5) is an enzyme that catalyzes the following reaction:  CS2 + 2 H2O → CO2 + 2 H2S  thus converting carbon disulfide into hydrogen sulfide and carbon dioxide.</p>

<p>β-Glucosidase (β-D-glucosidase, systematic name β-D-glucoside glucohydrolase; EC 3.2.1.21) is an enzyme that catalyzes the release the terminal glucose monomers from cellulose and the other oligo- and poly saccharides with β-1,4-linked glucosyl residues. One Unit of β-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic p-nitrophenyl β-glucoside per minute under optimum conditions.</p>

<p>3-Oxo-5β-steroid Δ4-dehydrogenase is an enzyme crucial in the metabolic pathway of steroid hormones, facilitating the conversion of androgens and estrogens. It is predominantly found in the liver, but also in other tissues where steroid biosynthesis occurs. This enzyme catalyzes the dehydrogenation at the Δ4 position of 3-oxo-5β-steroids, playing a significant role in the modulation and regulation of steroid hormone levels within cells.</p>

<p>Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing</p>

Expression system: E. coli<br>Length: 26-408, Partial<br>Activity: Not Tested

<p>AOX1 Protein, Human, Recombinant (His) is expressed in E. coli.</p>

<p>PTGES3 Protein, Human, Recombinant (E. coli, His) is expressed in E. coli.</p>

<p>May play an important role in the control of the immune response and during pregnancy.</p>

<p>Expression system: E. coli&lt;br&gt;Length: 2-501, Full Length of Mature Protein&lt;br&gt;Activity: Not Tested</p>

<p>Expression system: E. coli&lt;br&gt;Length: 1-418, Full Length&lt;br&gt;Activity: Not Tested</p>

Expression system: E. coli<br>Length: 1-203 (mutation), Full Length<br>Activity: Not Tested