Enzyme Substrates

Tested and Certified for in vivo imaging (See "Luciferin FAQ" in additional information)

Luciferin is a common bioluminescent reporter used for in vivo imaging of the expression of luciferase. This water soluble substrate for the firefly luciferase enzyme utilizes ATP and Mg2+ as cofactors to emit a characteristic yellow-green emission in the presence of oxygen, which shifts to red light in vivo at 37°C. Through the utilization of ATP, the reaction can be further used to indicate the presence of energy or life in order to function as a life-death stain.

Luciferin is a common reagent used throughout the biotechnology field and specifically for in vivo imaging. Luciferase labeled tumor cells, stem cells or infectious diseases are often inoculated into research animals such as rats or mice for investigation. The injection of luciferin allows for the real-time, noninvasive monitoring of disease progression and/or drug efficacy in these model systems through Bioluminescence Imaging (BLI).

Luciferin is also commonly used for in vitro research, including luciferase and ATP assays, gene reporter assays, high throughput sequencing and various contamination assays.

Firefly Luciferin is identical to Beetle Luciferin. (See "Additional Information" for structures.)

Luciferin is a common bioluminescent reporter used for in vivo imaging of the expression of the luciferase . This substrate for the firefly luciferase enzyme utilizes ATP and Mg2+ as cofactors and emits a characteristic yellow-green emission in the presence of oxygen, which shifts to red light in vivo at 37°C.

Luciferin is a common reagent used throughout the biotechnology field and specifically for in vivo imaging. Luciferase labeled tumor cells, stem cells or infectious diseases are often inoculated into research animals such as rats or mice for investigation. The injection of luciferin allows for the real-time, noninvasive monitoring of disease progression and/or drug efficacy in these model systems through Bioluminescence Imaging (BLI).

DMNPE-caged luciferin can be used to measure intracellular functions since it readily crosses cell membranes. Once it is inside the cell, active luciferin can be released by UV light or by the action of endogenous intracellular esterases. DMNPE-caged luciferin makes it easier to follow the changes in gene expression in live cells. It can also be used in combination with DMNPE-caged ATP.

Yellow crystalline powder that is used for the colorimetric determination of thiol groups in biological samples. DTNB is fairly soluble in water.

3-Indoxyl-β-D-glucuronic acid is used in detection and enumeration of E. coli. This chromogenic substrate is used for β-D-glucuronidase, and yields a blue precipitate upon cleavage.

H-Ala-pNAHCl is a substrate for L-alanine aminopeptidase, which is an enzyme that is localized in bacterial cell walls responsible for the cleavage of L-alanine from various peptides. Significant L-alanine aminopeptidase activity is specific to gram-negative microbes. Therefore, H-Ala-pNAHCl can be used in support of evidence that an organism is gram-positive or gram-negative. It is split by L-alanine aminopeptide into L-alanine and 4-nitroanine. The latter compound causes bacterial suspensions to turn yellow.

H-Ala-AMCTFA (L-Alanine 7-amido-4-methylcoumarin, trifluoroacetate salt) is a fluorogenic substrate for aminopeptidase that yields a blue fluorescent solution. This substrate is useful in differentiating between gram-positive and gram-negative bacteria.

Arginine is an essential amino acid found in food and plant sources, and many biological systems and is one of only 3 amino acids with basic side chains. Arginine is typically classified as a semi-essential or conditionally essential amino acid. Administered intravenously, Arginine has been shown to stimulate the secretion of human growth hormone and is frequently used in growth hormone stimulation tests. L-Arginine is a substrate of nitric oxide synthase, which is converted to citrulline and nitric oxide and is known to Induces insulin release by a nitric oxide-dependent mechanism.

L-Carnosine is a white to slightly off-white crystalline powder that is used as a substrate for carnosinase-1 and other enzymes.

L-Fucose is a six-carbon deoxy monosaccharide that is equivalent to 6-deoxy-L-galactose. L-Fucose is found on many N- and O-linked glycans present on the cell surface of a wide variety of organisms. The most well-known fucosylated glycans are the ABO blood group antigens. L-fucose present in gastrointestinal mucous represses virulence factor-encoding genes expressed by enterohemorrhagic E. coli. Mutations in the gene that encodes alpha-L-fucosidase can cause fucosidosis, leading to a buildup of fucose-containing compounds which cause cellular malfunction.

L-Glutamic acid gamma-(7-amido-4-methylcoumarin) is a substrate for aminopeptidase A. In the gamma-glutamyl transferase assay, the substrate cleaves to yield a blue fluorescent solution.

L-Glutamic acid HCl is a water-soluble organic acid and monosodium salt. It plays a crucial role as a neurotransmitter within the central nervous system and serves as a significant biochemical precursor in the biosynthesis of proteins, peptides, and nucleic acids. In vitro studies have demonstrated that L-(+)-glutamic acid HCl induces apoptosis in human HL-60 cells by elevating reactive oxygen species (ROS) levels and activating caspase-3 activity. This compound is essential for various biochemical applications and research in cellular biology and neurochemistry.

Fluorogenic substrate for aminopeptidase A, yielding a blue fluorescent solution upon cleavage.

L-Leucine 7-amido-4- methylcoumarin hydrochloride is used in leucine aminopeptidase assays as a fluorgenic substrate, showing greater sensitivity when compared to 4-methoxynapthylamide assays. Aside from the leucine aminopeptidase enzyme, L-Leucine 7-amido-4- methylcoumarin hydrochloride also works as a fluorogenic subtsrate for broad specificity aminopeptidases, such as aminopeptidase M.

The result of enzymatic activity yields a bright blue fluorescent dye: 7-amino-4methylcoumarin (excitation 380nm emission 440nm).

Leucine aminopeptidase enzymes are found across a wide range of organisms including bacteria, plants and animals, and it has been detected in human tissues, with high activity observed in the kidney and liver.

Tested and Certified for in vivo imaging (See "Luciferin FAQ" in additional information)

Luciferin is a common bioluminescent reporter used for in vivo imaging of the expression of luciferase. This water soluble substrate for the firefly luciferase enzyme utilizes ATP and Mg2+ as cofactors to emit a characteristic yellow-green emission in the presence of oxygen, which shifts to red light in vivo at 37°C. Through the utilization of ATP, the reaction can be further used to indicate the presence of energy or life in order to function as a life-death stain.

Luciferin is a common reagent used throughout the biotechnology field and specifically for in vivo imaging. Luciferase labeled tumor cells, stem cells or infectious diseases are often inoculated into research animals such as rats or mice for investigation. The injection of Luciferin allows for the real-time, noninvasive monitoring of disease progression and/or drug efficacy in these model systems through Bioluminescence Imaging (BLI).

Luciferin is also commonly used for in vitro research, including luciferase and ATP assays, gene reporter assays, high throughput sequencing and various contamination assays.

L-Luciferin is the chiralic sister to D-luciferin. While most researchers claim that L-luciferin does not produce any light, Lembert has reported that it produces a very weak and extremely slow manifesting light (Lembert, 1996). Nakamura suggested that an enzyme system incorporating luciferase might be responsible for changing the chirality of the L-luciferin to D-luciferin (Nakamura et al., 2006) (See Reference Library).

L-Lysyl-L-alanine 7-amido-4-methylcoumarin is used as an AMC fluorogenic substrate.