coli

Biotin-Lipopolysaccharide, fromE.coliO111:B4, is a biotin-conjugated Lipopolysaccharide (LPS) capable of binding with streptavidin proteins. Biotin-Lipopolysaccharide, fromE.coliO111:B4, can be utilized for the identification of Lipopolysaccharide ligands.

Lipopolysaccharides from *E. coli* (Escherichia coli) O26:B6 are endotoxins derived from *E. coli* that function as TLR-4 activators. These S-type LPS molecules can trigger pathogenic-associated molecular patterns (PAMP) and encourage the release of exosomes. Structurally, they are composed of three parts: O-antigen, core oligosaccharide, and Lipid A, and can be identified by the monoclonal antibody MAb J8-4C10. This compound can increase pro-inflammatory cytokines in plasma, leading to activation of the hypothalamic-pituitary-adrenal (HPA) axis and causing oxidative damage to the adrenal glands. However, the pathogenic activity of Lipopolysaccharides from *E. coli* O26:B6 can be inhibited by PD149163 .

Lipopolysaccharides from E. coli O127:B8 (LPS, from Escherichia coli (O127:B8)) are endotoxins and TLR-4 activators extracted from the bacterium E. coli O127:B8. This smooth (S) type LPS features a typical tripartite structure: an O antigen, an R3 core oligosaccharide, and lipid A. When lipopolysaccharides from E. coli O127:B8 activate TLR-4 on immune cells, they can trigger inflammatory responses and ileal contractility, making them useful for developing intestinal inflammation models.

Lipopolysaccharides, from E. coli O128:B12 (LPS, from Escherichia coli [O128:B12]) are lipid polysaccharide endotoxins and TLR-4 activators derived from E. coli O128:B12, characterized as a smooth (S) type LPS. This compound features a typical three-part structure: O antigen, R3 core oligosaccharide, and lipid A. It activates TLR-4 in immune cells, is useful for developing neonatal brain inflammation models in animals, and may impact preterm birth in neonates.

Lipopolysaccharides, from E. coli (Escherichia coli) K-235, are endotoxins derived from Escherichia coli and serve as TLR-4 activators. They are an S-type LPS capable of activating pathogen-associated molecular patterns (PAMP) of the immune system and inducing the secretion of exosomes. This compound is characterized by a typical three-part structure comprising the O-antigen, core oligosaccharide, and Lipid A. Additionally, lipopolysaccharides from E. coli K-235 stimulate mitogenesis in C57BL/10ScN spleen cells and, when purified by butanol and deoxycholate methods, can stimulate spleen cells from C57BL/10ScCR and C3H/HeJ mice.

Glycol chitosan, a chitosan derivative with hydrophilic ethylene glycol branches, inhibits E. coli, S. aureus, and S. enteritidis growth (MICs: 4 μg/mL, 32 μg/mL, and <0.5 μg/mL), and enhances membrane permeability and leakage in Glycine max [Harosoy 63W] cells.

5'-O-(4,4'-Dimethoxytrityl)-2'-deoxyuridine (5'-O-DMT-dU) is a competitive inhibitor of dUTP nucleotidohydrolase (dUTPase) in E. coli with a Ki greater than 1 mM. 5'-O-(4,4'-Dimethoxytrityl)-2'-deoxyuridine can be used in machine-assisted DNA synthesis.

E. coli Extract Total is derived from Escherichia coli (ATCC 11303) cultured under 37°C conditions during its three-quarters logarithmic growth phase, and it is suitable for use in the preparation of unilamellar vesicles.

E. coli Extract Polar is a polar lipid extract from Escherichia coli, consisting of phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin, useful for reconstituting membrane proteins.

E. coli DNAligase is an NAD++ dependent enzyme that catalyzes the formation of phosphodiester bonds between the complementary 3′-OH and 5′-P ends of double-stranded DNA (dsDNA).

Topoisomerase IV, E. coli (EC 5.99.1.) is produced by overexpressing the parC and parE subunits in Escherichia coli. In its active form, Topoisomerase IV dissolves in a diluted buffer solution as a heterotetrameric complex.

Taurine Dioxygenase, E. coli (EC 1.14.11.17), is an Fe (II) and α-ketoglutarate-dependent dioxygenase that enables Escherichia coli to utilize taurine as a sulfur source. It catalyzes the conversion of the amino acid taurine (2-aminoethane-1-sulfonic acid) into sulfite and aminoacetaldehyde.

β-Phosphoglucomutase, E. coli (EC 5.4.2.6), is an enzyme from the isomerase family that catalyzes the conversion of β-D-glucose-1-phosphate to β-D-glucose-6-phosphate. This enzyme plays a role in the metabolism of starch and sucrose.

Phosphatase, Escherichia coli (EC 3.1.3.-), is an enzyme that removes phosphate groups from substrates, generating phosphate ions and molecules with free hydroxyl groups through the hydrolysis of phosphate monoesters.

Trehalose-6-phosphate hydrolase, Escherichia coli (EC 3.2.1.93), is a member of the hydrolase family, functioning as a glycosidase that hydrolyzes O- and S-glycosyl compounds. This enzyme plays a role in the metabolism of starch and sucrose, with substrates α,α-trehalose-6-phosphate and water, producing D-glucose and D-glucose-6-phosphate.

β-Galactosidase Mutein, E. coli, is a hydrolase enzyme that facilitates the conversion of β-galactosides into monosaccharides. The substrates for various β-galactosidases include ganglioside GM1, lactosylceramide, lactose, and an array of glycoproteins.

Sugar-phosphatase, Escherichia coli (EC 3.1.3.23) is a member of the hydrolase enzyme family, specifically targeting the hydrolysis of phosphomonoester bonds. Its substrates include sugar phosphates and water, with its reaction products being sugar and phosphate.

Uridine phosphorylase, E. coli (EC 2.4.2.3), catalyzes the reversible phosphorolysis of uridine, resulting in the production of ribose-1-phosphate and uracil.

α-Galactosidase, positionally specific, Escherichia coli (EC 3.2.1.22), is a glycoside hydrolase enzyme that catalyzes the hydrolysis of α-galactosyl residues from the termini of glycolipids and glycoproteins. It exists in two recombinant forms known as α-galactosidase (INN) and β-galactosidase (INN).

Pyranose Oxidase, E. coli (EC 1.1.3.10), catalyzes the oxidation of aldopyranose at the C-2 position to produce the corresponding 2-ketoaldopyranose. This enzyme is a homotetrameric protein that contains a covalently bound flavin adenine dinucleotide (FAD).

α-Glucosidase, Escherichia coli (EC 3.2.1.20), is a glucosidase found in the brush border of the small intestine that acts on 1,4-α-glycosidic bonds, breaking down starches and disaccharides into glucose.

α-Amylase, Escherichia coli (EC 3.2.1.1) is a protein enzyme that hydrolyzes the α-glycosidic bonds of large α-linked polysaccharides, such as starch and glycogen, producing glucose and maltose.

E.coli tRNA adenosine deaminase is derived from Escherichia coli and functions as an adenosine deaminase. It effectively deaminates adenine within single-stranded RNA (ssRNA, primarily in the loop regions of tRNA) or double-stranded RNA (dsRNA) but lacks deaminase activity on DNA. This enzyme is a protein-engineered mutant form of adenosine deaminase, efficiently deaminating adenine in ssDNA, making it useful for adenine base editing (ABE) and RNA m6A methylation sequencing.

Thioredoxin Reductase, E. coli (EC 1.8.1.9) is an enzyme derived from Escherichia coli. Unlike mammalian TrxR, it does not possess the redox-active site at the C-terminal containing -Cys-SeCys-.