e.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.

E.coli DH-5 alphaBacterialprotein is a natural protein purified from E.coli DH-5 alpha bacteria.

E.coliBacterialprotein is a natural protein isolated from the bacterium Escherichia coli (E.coli).

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.

Keratanase II, from Bacillus circulans and expressed in E. coli, possesses transglycosylation activity. It effectively catalyzes α(2→3)-sialylated 6,6′-di-sulfo-LacNAc with two glycosyl acceptors, 6-sulfo-Lewis X and 6,6'-di-sulfo-LacNAc derivatives, generating sialic acid sulfohexose and sialic acid sulfopentose.

E.Coli Broth is a selective enrichment medium designed for the isolation, detection, or cultivation of Escherichia coli.

Pipecolic acid (2-Piperidinecarboxylic acid), a metabolite of lysine found in human physiological fluids such as urine, plasma and CSF, is an important regulator of immunity in plants and humans alike.

Boc-Pip-OH is a biochemical reagent that can be used as a biomaterial for life science related research and as a sulfonylation reagent for organic synthesis and drug discovery.

Boc-D-HoPro-OH is a biochemical reagent that can be used as a biomaterial for life science related research and as a sulfonylation reagent for organic synthesis and drug discovery.

α-(4-Methylpiperidino)isohexanophenone (hydrochloride) (α-Pipecolinoisohexanophenone (hydrochloride)) is classified as a cathinone and serves as an analytical reference standard.

Trisodium Phosphate is a strong alkali commonly used as a detergent, and has antibacterial activity against E. coli and S. aureus.

O-GlyCORTAR protease, recombinantly expressed from E.coli and tagged with His, is an enzyme that relies on O-glycans to cleave proteins carrying mucin-type O-glycans, including sialylated substrates and glycosylated Serine and Threonine residues at the N-terminus. This protease can process various O-glycan structures, such as sialylated core 1 and core 2 configurations, as well as the Tn antigen. Notably, O-GlyCORTAR protease does not cleave terminally modified serine or threonine residues, nor does it act on N-glycosylation sites of glycoproteins.

FabCOUPER protease is a serine protease that is recombinantly expressed in E.coli and features a 6×His tag at the C-terminus. It specifically cleaves human IgG1 at a single site above the hinge, efficiently generating intact Fab and Fc fragments within two hours without the need for reducing conditions.

O-Glycoprotease is a specific endoprotease for O-glycoproteins, capable of catalyzing the hydrolysis of peptide bonds directly adjacent to O-glycan structures in natural mucin-type O-glycosylated proteins. The sequence of O-Glycoprotease is derived from Akkermansia muciniphila, and it is recombinantly expressed in E. coli with a C-terminal 6×His tag. This enzyme maintains high activity within a pH range of 5.5 to 7.5, is resistant to 1 M NaCl, but is highly sensitive to EDTA (0.5 mM EDTA) and can be inhibited by Zn2+.

T4 lysozyme, derived from recombinant E.coli strains, is capable of lysing bacterial cell walls. It targets the peptidoglycan of bacterial cell walls, hydrolyzing the β-1,4 bond between N-acetylmuramic acid and N-acetylglucosamine.