Chemicals

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

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.

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

Biliverdin Hydrochloride is produced from the oxidation of heme in a reaction catalyzed by the enzyme heme oxygenase. Heme oxygenase has been implicated in tumor cell resistance to chemotherapy reduction of free radical formation reduction of inflammation and has been associated with vascular repair. In vivo biliverdin is reduced to bilirubin. Biliverdin Hydrochloride is soluble in basic aqueous solutions (pH > 9 for intitial dissolution) and soluble down to pH 7 once in solution as well as methanol and ethanol if made slightly basic.References1) Seta F. L. Bellner et al. (2006). "Heme Oxygenase-2 Is a Critical Determinant for Execution of an Acute Inflammatory and Reparative Response." The American Journal of Pathology 169(5): 1612.2) 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

Bilirubin dimethyl ester is a natural derivative of bilirubin and is found in normal sera representing an average of 1.75% total sera bilirubin. Bilirubin is a water insoluble tetrapyrrole produced from the reduction of biliverdin in a reaction catalyzed by the enzyme bilirverdin reductase. Water insoluble bilirubin (also called indirect bilirubin) in vivo undergoes glucuronidation in the liver (addition of one or two glucuronic acids through a glycosidic bond) to form the water soluble bilirubin mono or diglucuronide (also called bilirubin conjugate or direct bilirubin).  Bilirubin conjugate is excreted from the liver in bile or is converted to urobilinogen and excreted in the urine as urobilin or in the feces as stercobilin.  Bilirubin dimethyl ester has been found to be converted to bilirubin conjugate via esterase and glucuronidase activity in vivo.References1) Muraca M. and N. Blanckaert (1983). "Liquid-chromatographic assay and identification of mono- and diester conjugates of

Bilirubin is a water insoluble tetrapyrrole produced from the reduction of biliverdin in a reaction catalyzed by the enzyme bilirverdin reductase. In vivo it undergoes glucuronidation in the liver (addition of one or two glucuronic acids through a glycosidic bond) to form the water soluble mono or diglucuronide (also called bilirubin conjugate). The conjugate is excreted from the liver in bile or is converted to urobilinogen and excreted in the urine as urobilin or in the feces as stercobilin.References1) Lee K. S. L. D. Raymond et al. (2007). "Hemin Interactions and Alterations of the Subcellular Localization of Prion Protein." Journal of Biological Chemistry 282(50): 36525-36533.2) Soares M. P. M. P. Seldon et al. (2004). "Heme Oxygenase-1 Modulates the Expression of Adhesion Molecules Associated with Endothelial Cell Activation." The Journal of Immunology 172(6): 3553-3563.3) Huber A. H. B. Zhu et al. (2012). "Fluorescence Sensor for the Quantification of Unbound Bilirubin