Chemicals & Small Molecules

This novel and selective probe for hydrogen sulfide (H2S) 7-azido-4-methylcoumarin (AzMC) is useful for monitoring cystathionine B-synthase (CBS) catalyzed reactions which play a critical role in human sulfur metabolism. Deactivated CBS is characterized by high plasma levels of homocysteine and H2S resulting in clinical manifestations of numerous disease states. AzMC used as a fluorgenic probe and concurrent CBS activity can be used to select compounds for activation or inhibition of this enzyme and is suitable for high-throughput screening and the development of potential therapeutics. In addition AzMC has been used as a photoaffinitry probe for the substrate binding site of human phenol sulfotransferase (SULT1A-1 or P-PST-1).Featured in References1. M.K. Thorson T. Majtan J.P. Kraus A.M. Barrios "Identification of Cystathionine β-Synthase Inhibitors Using a Hydrogen Sulfide Selective Probe." Angewandte Chemie (Int. ed. Eng.) 2013 52 4641-4144. DOI: 10.1002/anie.20130084

C6NIB is a fluorescence turn-on sensor that is suited for trace vapor detection of hydrogen peroxide (H2O2). The sensor mechanism is based on H2O2-mediated oxidation of the boronate fluorophore C6NIB which is nonfluorescent in the ICT band but is strongly fluorescent upon conversion to the phenol (C6NIO). The fluorescence turn-on reaction is extremely sensitive towards H2O2 with no sensor response to other common reagents. The negligible fluorescence background of C6NIB combined with the high fluorescent emission of C6NIO makes it an ideal candidate for efficient sensing. Dispersing C6NIB with TBAH into a silica gel matrix produces a highly efficient sensor for vapor detection of H2O2 in terms of detection limit (2.9 ppb) and response time (1 sec. under 1 ppm H2O2).References:M. Xu J-M. Han et al.“A selective fluorescence turn-on sensor for trace vapor detection of hydrogen peroxide” Chem. Commun. 2013 49 11779-11781.

Hypoxia Inducible Factor (HIF) regulates responses to hypoxia and is comprised of two subunits alpha and beta. Upon cellular exposure to hypoxic conditions the HIF complex (alpha and beta subunits) is stabilized and binds to DNA transcriptionally activating genes linked to the cellular processes of angiogenesis and glucose metabolism1. Under normal conditions the HIF-alpha subunit is hydroxylated by the enzyme HIF-alpha prolyl hydroxylase (HIF-PH) leading to ubiquitylation of HIF-alpha and subsequent destruction2. DMOG (dimethyloxalylglycine) is a cell permeable competitive inhibitor of HIF-alpha prolyl hydroxylase (HIF-PH) leading to the stabilization of HIF and subsequent angiogenesis and glucose metabolism at concentrations between 0.1 and 1 mM3 4References1) Ivan M. K. Kondo et al. (2001). "HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing." Science 292(5516): 464-8.2) Jaakkola P. D. R. Mole et al. (2001). "Targeting of HI

NOG is an analogue of alpha ketoglutarate and has been found to be an inhibitor of reactions involving alpha ketoglutarate such as xanthine hydroxylase and alpha ketoglutarate dioxygenase.References1) Montero-Moran G. M. M. Li et al. (2007). "Purification and characterization of the FeII- and alpha-ketoglutarate-dependent xanthine hydroxylase from Aspergillus nidulans." Biochemistry 46(18): 5293-304.2) Kalliri E. P. K. Grzyska et al. (2005). "Kinetic and spectroscopic investigation of CoII NiII and N-oxalylglycine inhibition of the FeII/alpha-ketoglutarate dioxygenase TauD." Biochem Biophys Res Commun 338(1): 191-7.

Monobromobimane reacts with thiols sulfide thiosulfate and sulfite to generate a fluorescent product with excitation/emission maxima at 394/490 nm.Publications Powered by Bioz See more details on Bioz1) Gainer H. and N. S. Kosower (1980). "Histochemical demonstration of thiols and disulfides by the fluorescent labeling agent monobromobimane: An application to the hypothalamo-neurohypophysial system." Histochemistry 68(3): 309-315.2) Hulbert P. B. and S. I. Yakubu (1983). "Monobromobimane: a substrate for the fluorimetric assay of glutathione transferase." Journal of Pharmacy and Pharmacology 35(6): 384.3) Alkhalfioui F.; Renard M.; Vensel W. H.; Wong J.; Tanaka C. K.; Hurkman W. J.; Buchanan B. B.; Montrichard F. (2007) Thioredoxin-linked proteins are reduced during germination of Medicago truncatula seeds. Plant Physiol. 144(3): 1559-79. 4) Catania J. M. A. M. Pershing et al. (2007). "Precision-cut tissue chips as an in vitro toxicology system." Toxicology in Vitro 2

Dibromobimane is a thiol reactive protein cross linking reagent that generates a fluorescent product when both of the alkylating groups have reacted with proteins. Dibromobimane has an excitation/ emission spectra of 390/450 nm.References1) Mornet D. K. Ue et al. (1985). "Stabilization of a primary loop in myosin subfragment 1 with a fluorescent crosslinker." Proceedings of the National Academy of Sciences 82(6): 1658-1662.2) Konno K. K. Ue et al. (2000). "Consequences of placing an intramolecular crosslink in myosin S1." Proceedings of the National Academy of Sciences 97(4): 1461-1466.3) Chen Z. B. L. Akin et al. (2006). "Cross-linking of C-terminal Residues of Phospholamban to the Ca2+ Pump of Cardiac Sarcoplasmic Reticulum to Probe Spatial and Functional Interactions within the Transmembrane Domain." Journal of Biological Chemistry 281(20): 14163-14172.4) Lindzen M. K.-E. Gottschalk et al. (2006). "Structural Interactions between FXYD Proteins and Na+ K+-ATPase: α/β/FX

Hemin induces the activity of the enzyme heme-oxygenase. Heme oxygenase catalyzes the conversion of heme to biliverdin CO and Fe+3. The induction of heme oxygenase activity has been associated with reduced free radical formation and inflammation vascular repair and implicated in tumor growth and metastasis. Hemin has been shown to be effective at 75 μmol/kg in mice or 5 μM for cells in culture.References1) Shibahara S. T. Yoshida et al. (1978). "Induction of heme oxygenase by hemin in cultured pig alveolar macrophages." Arch Biochem Biophys 188(2): 243-50.2) Abraham N. G. and A. Kappas (2005). "Heme oxygenase and the cardiovascular-renal system." Free Radic Biol Med 39(1): 1-25.3) Jozkowicz A. H. Was et al. (2007). "Heme oxygenase-1 in tumors: is it a false friend?" Antioxid Redox Signal 9(12): 2099-117.4) Xia Z. W. W. W. Zhong et al. (2006). "Heme oxygenase-1-mediated CD4+CD25high regulatory T cells suppress allergic airway inflammation." J Immunol 177(9): 5936-45.>5

Porphobilinogen is an intermediate in the heme synthesis pathway produced from d-Amino-levulinic acid in a reaction catalyzed by the enzyme ALA dehydrogenase. Porphobilinogen is converted to Hydroxylmethyl bilane in a reaction catalyzed by the enzyme Porphobilinogen Deaminase.References1) Roshal M. J. Turgeon et al. (2008). "Rapid Quantitative Method Using Spin Columns to Measure Porphobilinogen in Urine." Clinical Chemistry 54(2): 429-431.2) Ford R. E. M. J. Magera et al. (2001). "Quantitative Measurement of Porphobilinogen in Urine by Stable-Isotope Dilution Liquid Chromatography-Tandem Mass Spectrometry." Clinical Chemistry 47(9): 1627-1632.3) Strand A. T. Asami et al. (2003). "Chloroplast to nucleus communication triggered by accumulation of Mg-protoporphyrinIX." Nature 421(6918): 79.4) Omata Y. H. Sakamoto et al. (2004). "Purification and Characterization of Human Uroporphyrinogen III Synthase Expressed in Escherichia coli." Journal of Biochemistry 136(2): 211-220.

Protoporphyrin IX is an intermediate in the Heme synthesis pathway and is formed from Protoporphyrinogen III in a reaction catalyzed by the enzyme Protoporphyrin III oxidase. It plays an important role in living organisms as a precursor for other critical compounds like hemoglobin and chlorophyll. It can form heme when added to ferrous iron in the presence of the enzyme ferrochelatase and has been found to activate guanylate cyclase and has been found to induce apoptosis in HeLa cells.Publications Powered by Bioz See more details on Bioz1) Bednarz N. J. Zawacka-Pankau et al. (2007). "Protoporphyrin IX induces apoptosis in HeLa cells prior to photodynamic treatment." Pharmacol Rep 59(4): 474-92) Strand A. T. Asami et al. (2003). "Chloroplast to nucleus communication triggered by accumulation of Mg-protoporphyrin IX." Nature 421(6918): 79.