Chemicals

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.

Zn (II) Protoporphyrin IX is an inhibitor of heme oxygenase (the enzyme that catalyzes the conversion of heme to biliverdin in the heme degradation pathway) and guanylyl cyclase. Heme oxygenase has been implicated in tumor cell resistance to chemotherapy reduction of free radical formation and inflammation and associated with vascular repair.References1) Maines M. D. (1981). "Zinc protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat." Biochim Biophys Acta 673(3): 339-50.2) Gupta G. J. Kim et al. (1997). "Expression and Purification of Soluble Active Heterodimeric Guanylyl Cyclase from Baculovirus." Protein Expression and Purification 10(3): 325.3) 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) Abraham N. G. and A. Kappas (2005). "Heme oxygenase and the cardiovascular-renal system." Free Radic Biol Med 39(1): 1-25.5) Kim D. H. A. P. Burgess et al. (2008). "Hem

Cu (II) Protoporphyrin IX does not inhibit heme oxygenase (the enzyme that catalyzes the conversion of heme to biliverdin in the heme degradation pathway) and is used as a negative control for Zn (II) Protoporphyrin (an inihibitor of heme oxygenase).  Heme oxygenase has been implicated in tumor cell resistance to chemotherapy reduction of free radical formation and inflammation and associated with vascular repair.References1) Jozkowicz A. H. Was et al. (2007). "Heme oxygenase-1 in tumors: is it a false friend?" Antioxid Redox Signal 9(12): 2099-117.2) Abraham N. G. and A. Kappas (2005). "Heme oxygenase and the cardiovascular-renal system." Free Radic Biol Med 39(1): 1-25.3) Kim D. H. A. P. Burgess et al. (2008). "Heme oxygenase-mediated increases in adiponectin decrease fat content and inflammatory cytokines tumor necrosis factor-alpha and interleukin-6 in Zucker rats and reduce adipogenesis in human mesenchymal stem cells." J Pharmacol Exp Ther 325(3): 833-40.

Sn (IV) Protoporphyrin IX is an inhibitor heme oxygenase (the enzyme that catalyzes the conversion of heme to biliverdin in the heme degradation pathway) but has also been found to stimulate production of the heme oxygenase protein. Contrast the activity of Co (III) Protoporphyrin which has been found to have similar activities to Sn (IV) Protoporphyrin but with a greater enhancement of heme oxygenase synthesis activity such that heme oxygenase activity is actually increased when administered in vivo while in vitro administration inhibits heme oxygenase activity. Heme oxygenase has been implicated in tumor cell resistance to chemotherapy reduction of free radical formation and inflammation and associated with vascular repair.References1) Sardana M. K. and A. Kappas (1987). "Dual control mechanism for heme oxygenase: tin(IV)-protoporphyrin potently inhibits enzyme activity while markedly increasing content of enzyme protein in liver." Proc Natl Acad Sci U S A 84(8): 2464-8.2) Jozkowi

Zn (II) Deuteroporphyrin IX 2 4 bis ethyleneglycol is an inhibitor of heme oxygenase (the enzyme that catalyzes the conversion of heme to biliverdin in the heme degradation pathway) at concentrations as low at 0.5 μM. Heme oxygenase has been implicated in tumor cell resistance to chemotherapy reduction of free radical formation and inflammation and associated with vascular repair.References1) Chernick R. J. P. Martasek et al. (1989). "Sensitivity of human tissue heme oxygenase to a new synthetic metalloporphyrin." Hepatology 10(3): 365-9.2) Jozkowicz A. H. Was et al. (2007). "Heme oxygenase-1 in tumors: is it a false friend?" Antioxid Redox Signal 9(12): 2099-117.3) Abraham N. G. and A. Kappas (2005). "Heme oxygenase and the cardiovascular-renal system." Free Radic Biol Med 39(1): 1-25.4) Kim D. H. A. P. Burgess et al. (2008). "Heme oxygenase-mediated increases in adiponectin decrease fat content and inflammatory cytokines tumor necrosis factor-alpha and interleukin-6 in Z