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Diethylene+glycol+monohexyl+ether
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Diethylene+glycol+monohexyl+ether
Supplier:
Corning
Description:
Transwell® cell culture inserts are convenient, easy to use permeable support devices for the study of both anchorage-dependent and anchorage-independent cell lines. They are designed to produce a cell culture environment that closely resembles the <i>in vivo</i> state.
Supplier:
MP Biomedicals
Description:
PMA (Phorbol-12-Myristate-13-Acetate) is a diester of phorbol and is a tumor promoting compound extracted from croton oil. It is a reversible, highly potent protein kinase C (PKC) activator in vitro and in vivo at nM concentrations. PMA’s effects on PKC are attributed to its similarity to diacylgylerol, a natural activator of PKC.
PMA activates Ca2+- ATPase and potentiates forskolin-induced cAMP formation. It has been shown to inhibit apoptosis induced by the Fas antigen, but PMA induces apoptosis in HL-60 promyelocytic leukemia cells. Potent tumor promoter; activates protein kinase C in vivo and in vitro. Store at -20 °C. Protect from light.
Supplier:
MP Biomedicals
Description:
β-Mercaptoethanol can act as an enzyme reactivator in systems necessitating reduction for activation, and has been commonly used to reduce disulfide bonds in order to separate protein subunits for use in electrophoresis.
2-Mercaptoethanol is used to reduce disulfide linkages in solubilizing proteins for gel electrophoresis (typically used in SDS-PAGE sample buffer at 5% concentration). Also reduces excess oxidative polymerization of catalysts. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure. In solution, 2-mercaptoethanol is readily oxidized in air to a disulfide, especially at alkaline pH. Because of this property, it is widely used to protect proteins, enzymes in particular, from becoming inactive. An excess of 2-mercaptoethanol (generally used at 0.01 M) will maintain the protein thiol groups in their reduced state.
Supplier:
MP Biomedicals
Description:
Storage: Room Temperature, desiccate, store under nitrogen.
Dimethyl Sulfoxide is a dipola, aprotic solvent. It has been shown to accelerate strand renaturation (1-10% concentration) and is believed to give the nucleic acid thermal stability against depurination. Dimethyl Sulfoxide is used to enhance dermal absorption of many chemicals, as a solvent for many organic and inorganic compounds including fats, carbohydrates, dyes, resins, and polymers, in antifreeze or hydraulic fluids, as a cryopreservative for cell cultures, oxidation of thiols and disulfides to sulfonic acids, as a PCR cosolvent to help improve yields, especially in long PCR. DMSO is routinely used in polymerase chan reaction (PCR), amplification of cDNA libraries, DNA sequencing, column-loading buffers for poly (A)+ RNA selection, buffers for the transformation of competent E. coli, and transfection protocols. To prepare sterile solutions use a teflon or nylon membrane to sterile-filter the DMSO - do not use a cellulose acetate membrane.
Supplier:
MP Biomedicals
Description:
Bilirubin is the principal pigment of bile and constituent of many biliary calculi and also found in blood. As the major end-product of the biological breakdown of heme, bilirubin is the chromophore responsible for coloration in various forms of jaundice.
Bilirubin is suitable for use in the preparation of standard stock solutions of bilirubin for color density comparison in the determination of serum bilirubin. It appears to function as an antioxidant and efficient peroxyl radical scavenger, protecting membrane lipids from oxidation by these radicals. At nanomolar concentrations it has been shown to protect neurons from oxidative damage. Bilirubin is produced from Ox-gall which is sterilized before extraction with high pressure vapour at 120 °C. Then the bilirubin is extracted in a continuous extraction process with chloroform as a crude product. Recrystallization and purification is with ethanol and chloroform. -20°C. Protect from light.
Supplier:
MP Biomedicals
Description:
Storage: Store at Room Temperature (15-30 °C)
Glycine is a non-essential amino acid. It is only amino acid with no asymmetric carbon and thus is not chiral. It is the major inhibitory neurotransmitter. It is involved in the biosynthesis of the porphyrin rings of hemes and chlorophylls. Glycine is commonly used in buffer solutions, in electrophoresis and preparative chromatography. A study of the folding of monoclonal antibodies in the presence of glycine and their subsequent purification has been published. The use of glycine in the purification of lipopolysaccharides, lipooligosaccharides, and lipid A has been reported. It is an amino acid for use in cell culture media development applications and existing media formulations. Glycine is commonly used as a component in Tris-glycine and Tris-glycine-SDS running buffers for polyacrylamide gel electrophoresis, a component of Towbin's transfer buffer for Western blots, a buffer substance in cryoenzymology, in osmotic pressure maintenance in isoelectric focusing of erythrocytes, salting-in effect in protein chemistry, and as a buffer component in the coupled phosphatase-kinase reaction for end labelling of restriction fragments. The growth requirements of various microorganisms is reported in the Handbook of Microbiology. Glycine is a non-chiral amino acid that can be synthesized in the body from the amino acid serine by Serine Hydroxymethyltransferase. Inhibitory neurotransmitter in spinal cord, allosteric regulator of NMDA receptors.
Catalog Number:
(IC856126)
Supplier:
MP Biomedicals
Description:
DL-Dithiothreitol is also known as Clelands reagent; Protective agent for sulfhydryl groups (-SH). Quantitatively reduces disulfides (-S-S- to -SH). In this reaction the DTT is oxidized to the cyclic disulfide which ensures the reduction of other disulfides in solution. Disulfide reduction occurs quickly at pH 8.
Dithiothreitol is useful for stabilizing sulfhydryl containing enzymes. Effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE. DTT can also be used for reducing the disulfide bridge of the cross-linker N,N'-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel. DTT is less pungent and is less toxic than 2-mercaptoethanol. Useful for stabilizing sulfhydryl-containing enzymes.
Catalog Number:
(IC0210116625)
Supplier:
MP Biomedicals
Description:
β-NADP is a coenzyme necessary for the alcoholic fermentation of glucose and the oxidative dehydrogenation of other substances. It occurs widely in living tissue, especially in the liver. Nicotinic acid can be converted to nicotinamide in the body and, in this form, is found as a component of two oxidation-reduction coenzymes: nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The nicotinamide portion of the coenzyme transfers hydrogens by alternating between oxidized quaternary nitrogen and a reduced tertiary nitrogen. NADP is an essential coenzyme for glucose-6-phosphate dehydrogenase which catalyzes the oxidation of glucose-6-phosphate to 6-phosphogluconic acid. This reaction initiates metabolism of glucose by a pathway other than the citric acid cycle. This route is known as the hexose phosphate shunt or phosphogluconate pathway. Other enzymes which utilize NADP as a coenzyme are: Alcohol dehydrogenase:NADP dependent; Aromatic ADH:NADP dependent; Ferredoxin-NADP reductase; L-Fucose dehydrogenase; Gabase; Galactose-1-phosphate uridyl transferase; Glucose dehydrogenase; L-Glutamic dehydrogenase; Glycerol dehydrogenase:NADP specific; Isocitric dehydrogenase; Malic enzymes; 5,10-Methylenetetrahydrofolate dehydrogenase; 6-Phosphogluconate dehydrogenase and Succinic semialdehyde dehydrogenase.
Supplier:
MP Biomedicals
Description:
Urea is the principal end product of nitrogen metabolism in most mammals, formed by the enzymatic reactions of the Kreb's cycle.
Urea is a mild agent usually used in the solubilization and denaturation of proteins. It is also useful for renaturing proteins from samples already denatured with 6 M guanidine hydrochloride such as inclusion bodies; and in the extraction of the mitochondrial complex. It is commonly used to solubilize and denature proteins for denaturing isoelectric focusing and two-dimensional electrophoresis and in acetic acid-urea PAGE gels. Urea is used in cell or tissue culture media to increase the osmolality. Urea has also been used as fertilizer because of the easy availability of nitrogen; in animal feeds; it is reacted with aldehydes to make resins and plastics; condensed with malonic ester to form barbituric acid; used in the paper industry to soften cellulose; used as a diuretic; enhances the action of sulfonamides; an antiseptic. Urea in solution is in equilibrium with ammonium cyanate. The form that reacts with protein amino groups is isocyanic acid. Urea in the presence of heat and protein leads to carbamylation of the proteins. Carbamylation by isocyanic acid interferes with protein characterization because isocyanic acid reacts with the amino terminus of proteins, preventing N-terminal sequencing. Isocyanic acid also reacts with side chains of lysine and arginine residues resulting in a protein that is unsuitable for many enzymatic digests. In addition, carbamylation often leads to confusing results from peptides having unexpected retention times and masses. When performing enzymatic protein digests it is important to remove urea first. Even though some enzymes will tolerate small amounts of urea, the elevated temperature used for most reactions will lead to carbamylation during the course of the digest. The urea can be removed prior to digestion by fast reversed phase chromatography, spin columns, or dialysis. Dissolve urea in deionized water to the desired concentration.For every 10 ml of solution, add 1 g of Amberlite® IRA-910.Stir for one hour at room temperature
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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