D_Products

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.

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. ^®

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.

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.)

D-lysine is an alpha amino acid. D-lysine based polyamino acids help cells and proteins attach to solid surfaces, and the D conformation useful in promoting adhesion to solid substrates. Poly-D-lysine based hydrogels have been used for traumatic brain injuries. Crystal structures based on chiral PNA-DNA duplexes with d-lysine are also observed.

D-Melibiose is a reducing disaccharide formed from galactose and glucose. It can be used to differentiate between Saccharomyces pastorianus, which breaks down D-Melibose, from Saccharomyces cerevisiae which does not. This characteristic may be shared among other bacteria, giving D-Melibiose an ability to differentiate bacterial species. D-Melibiose has also been used to study water plasticization of amorphous disaccharides and in a study improvind the preparation of benzoylated ethyl. It also has moderate protective effects on anti-pig antibodies in pig kidney cells.

D-Norvaline is an alpha-amino acid. It is a natural component of an antifungal peptide of Bacillus subtilis, and may be part of the production of cell walls resistant to vancomycin. As a reagent it has been used to synthesize MMP inhibitors.

D-Tryptophan is used in the liver and kidneys to produce d-kynurenine. It can be used as a reagent for chemical synthesis.

Murine D17Wsu104e (SF20) is a bone marrow stroma-derived growth factor, sometimes called IL25 (not to be confused with IL17E/IL25). SF20 is expressed in bone marrow, spleen stroma cells, resting mononuclear cells, resting CD8+ and CD19+ cells and activated CD8+ T-cells. SF20 has also been shown to bind to the surface of cells expressing the receptor TSA-1 (Thymic shared Ag-1). Among its biological activities, SF20 stimulates the proliferation of FDCP2 cells (a mouse factor-dependent hemopoietic cell line) and mouse lymphoid cells.

DAB tetrahydrochloride hydrate is a water soluble form of 3-3'-diaminobenzidine and is used to stain for peroxidase activity. The intensity of DAB staining can be increased with the addition of cobalt, nickel or silver ions.

Dabrafenib is a compound used as a serine/threonine-protein kinase B-Raf inhibitor for oncology research. It competitively inhibits V600E BRAF gene mutations which are characteristic in melanoma cancers. Inhibition of B-Raf proteins, by dabrafenib, interrupts mitogen-activated protein kinase/extracellular signal regulated kinase (MAPK/ERK) pathways, which regulate cell growth.This action halts cell proliferative activity and engages apoptosis.

Dacarbazine (DTIC) is an anti-cancer prodrug that has been used as a standard for comparing the efficacy of new antineoplastic compounds. It is used with other anti-cancer compounds to both increase potency and disrupt side-effects generated by DTIC. While being a strong antineoplastic agent, DTIC has also been shown to stimulate interleukin 8 (IL8) and vascular endothelial growth factor (VEGF) expression in cancer cells.

DTIC is transformed by liver enzymes into its active methyl diazonium cation form. The active form of DTIC has displayed anti-tumor activity following light exposure. It has been shown that the light exposure catalyzes methyl diazonium cation to form a carbine and aryl radical. These radicals damage DNA of malignant cancer cells, producing cytotoxic effects and eventual cell death.

Human beta-defensin 1 (DEFB1) is an antimicrobial peptide that contributes to the innate and adaptive immune system and is active against bacteria, fungi, and viruses. Like the other β-defensins, DEFB1 is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is constitutively expressed in epithelial cells, mainly of the kidney and the female reproductive tract, as well as in monocytes, macrophages, and dendritic cells. DEFB1 is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB1 than for Ca+2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. The primary role of DEFB1 is believed to be prevention of microbial colonization on epithelia. Inhibition of DEFB1 by high salt concentration may play a role in the pathogenesis of cystic fibrosis. DEFB1 may also play a role in the pathogenesis of severe sepsis.

Murine beta-defensin 1 (DEFB1) is an antimicrobial peptide that contributes to the innate and adaptive immune systems and is active against bacteria, fungi, and viruses. Like the other β-defensins, DEFB1 is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is constitutively expressed in epithelial tissue, mainly of the respiratory and genitourinary tract, as well as in monocytes, macrophages, and dendritic cells. DEFB1 is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB1 than for Ca +2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. The primary role of DEFB1 is believed to be prevention of microbial colonization on epithelia. Transgenic mice lacking the Defb1 gene showed an increased load of Staphylococcus species in the bladder, suggesting a role for DEFB1 in resistance to urinary tract infection. Inhibition of DEFB1 by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

Rat beta-defensin 1 (DEFB1) is an antimicrobial peptide that contributes to the innate and adaptive immune systems and is active against bacteria, fungi, and viruses. Like the other β-defensins, DEFB1 is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is constitutively expressed in epithelial tissue, mainly of the respiratory and genitourinary tract, as well as in monocytes, macrophages, and dendritic cells. DEFB1 is a cationic peptide that disrupts the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). The primary role of DEFB1 is believed to be prevention of microbial colonization on epithelia. Inhibition of DEFB1 by high salt concentration may play a role in the pathogenesis of cystic fibrosis. DEFB1 is abnormally expressed in Goto-Kakizaki (GK) rats suggesting a role of DEFB1 in diabetic nephropathy.

Human beta-defensin 103A (DEFB103A) is an antimicrobial peptide that contributes to the innate and adaptive immune systems and is active against gram-negative and gram-positive bacteria, fungi, and viruses. Like the other β-defensins, DEFB103A is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is expressed in epithelial tissue of many organs, heart and skeletal muscle tissue, and leukocytes. Expression of DEFB103A is induced by proinflammatory cytokines such as IL1B and IFNG. DEFB103A is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB103A than for Ca+2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. DEFB103A has been shown to have a greater positive surface charge than DEFB1 or DEFB4A, giving it greater antimicrobial activity. Inhibition of DEFB103A by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

Human beta-defensin 104A (DEFB104A) is an antimicrobial peptide that contributes to both the innate and the adaptive immune systems and is active against gram-negative and gram-positive bacteria, fungi, and viruses. Like the other β-defensins, DEFB104A is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is expressed at highest levels in the testis and stomach, and at lower levels in the uterus, neutrophils, thyroid, lung, and kidney. Expression of DEFB104A is upregulated by phorbol 12-myristate 13-acetate (PMA), as well as in response to infection with gram-positive and gram-negative bacteria. DEFB104A is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB103A than for Ca+2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. DEFB104A has been shown to be more active against Pseudomonas aeruginosa than DEFB1, DEFB4A, or DEFB103A. Inhibition of DEFB104A by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

Murine beta-defensin 2 (DEFB2) is an antimicrobial peptide that contributes to the innate immune system and is active against gram-negative bacteria, fungi, and viruses. It also contributes to the adaptive immune system through recruitment of leukocytes to sites of infection through chemotaxis. Like the other β-defensins, DEFB2 is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is expressed in the epithelia of skin and organs in the genitourinary tract, as well as in monocytes and macrophages. Expression is induced by 1,25-dihydroxyvitamin D3, LPS, and proinflammatory cytokines, such as IL1B and IFNG, and downregulated by the anti-inflammatory steroid dexamethasone. DEFB2 expression is also induced by exposure to low M.W. hyaluronic acid fragments, which is common following inflammation or tissue injury. DEFB2 is a cationic peptide that disrupts the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). In mice that have had the Defb2 gene silenced, inducible NO synthase expression was elevated. DEFB2 works in combination with DEFB3 to contribute to resistance against corneal infection. Inhibition of DEFB2 by high salt concentration may play a role in the pathogenesis of cystic fibrosis.