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Catalog Number: (75934-958)

Supplier:  Rockland Immunochemical
Description:   Voltage-gated proton (hydrogen) channels play an important role in cellular defense against acidic stress (1). NOX1 is a homolog of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox (1). Three splice variants of NOX1 have been identified, NOH-1L, NOH-1S and NOH-1Lv (2). NOH-1S is a voltage-gated proton channel that participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain (1-3). NOX1 have the potential to be effective treatments for a range of ischemic diseases (4).
Supplier:  Bioss
Description:   CYB5R3 is a 301 amino acid protein encoded by the human gene CYB5R3. CYB5R3 belongs to the flavoprotein pyridine nucleotide cytochrome reductase family and has two naturally occuring isoforms. Isoform 1 is anchored to the cytoplasmic side of the endoplasmic reticulum membrane and mitochondrion outer membrane, while isoform 2 is the soluble form found in erythrocytes. CYB5R3 is involved in the desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism and, in erythrocytes, methemoglobin reduction. A serine residue at position 117 seems to only be found in persons of African origin. The allele frequency is 0.23 in African Americans. It is not found in Caucasians, Asians, Indo-Aryans or Arabs. This difference seems to have no effect on the enzyme activity. Defects in CYB5R3 are the cause of hereditary methemoglobinemia (HM). There are three forms of this disease: type 1 (HM1), in which the enzyme is only deficient in erythrocytes with a mild cyanosis; type 2 (HM2), in which the enzyme is completely deficient; and type 3 (HM3), where the deficiency is seen in all blood cells. Type 2 is a severe form accompanied by mental retardation and neurological impairment.
Supplier:  MP Biomedicals
Description:   Storage: -20°C, desiccate
This is an ultrapure NAD, chromatographically purified to remove trace inhibitors.
β-NAD, a pyridine nucleotide and biologically active form of nicotinic acid, is a coenzyme necessary for the catalytic reaction of certain enzymes. It occurs in living cells primarily in the oxidized state. Serves as a coenzyme of the dehydrogenases, especially in the dehydrogenation of primary and secondary alcohols. NAD usually acts as a hydrogen acceptor, forming NADH which then serves as a hydrogen donor in the respiratory chain.
Many metabolites and enzymes of biological interest are present in tissues at low concentrations. With the use of β-NAD as a catalyst intermediate and several enzymes in a multistep system, known as enzyme cycling, much greater sensitivity for detection of these components is achieved. The reduced form, β-NADH, is fluorescent whereas β-NAD is not. This difference in fluorescence provides a sensitive fluorescent measurement of the oxidized or reduced pyridine nucleotides at concentrations down to 10-7 M.
Electron acceptor. β-NAD is a carrier for hydride ion, forming b-NADH. Hydride ion is enzymatically removed from a substrate molecule by the action of dehydrogenases such as malic dehydrogenase and lactic dehydrogenase. Such enzymes catalyze the reversible transfer of a hydride ion from malate or lactate to b-NAD to form the reduced product, b-NADH. Unlike b-NAD which has no absorbance at 340 nm, b-NADH absorbs at 340 nm (EmM = 6.22). The increase in absorbance at 340 nm with the formation of b-NADH is the basis for measurement of activity of many enzymes.
Supplier:  Thermo Scientific Chemicals
Description:   Waterproofing and release agent, stabilizer for PVC, lubricant, conditioning agent
MSDS SDS
Catalog Number: (76011-502)

Supplier:  Prosci
Description:   This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein. It is a central enzyme of cellular antioxidant defense, and reduces oxidized glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant. Rare mutations in this gene result in hereditary glutathione reductase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been found.
Supplier:  AMBEED, INC
Description:   H-D-2-Pal-OH, Purity: 98%, CAS Number: 37535-52-7, Appearance: Solid, Storage: Keep in dark place, Inert atmosphere, Room temperature, Size: 5g
Supplier:  THERMO FISHER SCIENTIFIC CHEMICALS
Description:   Boron tribromide 99.9%
Catalog Number: (AAA44839-KG)

Supplier:  Thermo Scientific Chemicals
Description:   99.5% 1PC
MSDS SDS
Catalog Number: (77401-380)

Supplier:  APOLLO SCIENTIFIC
Description:   Boron phosphate 99,9%
Supplier:  Strem Chemicals Inc
Description:   CAS #: 7440-42-8. Size: 50g.
Supplier:  Thermo Scientific Chemicals
Description:   MDL: MFCD00134034
MSDS SDS

Supplier:  TCI America
Description:   Boron Trichloride (ca. 17% in Hexane, ca. 1.0mol/L), Cas number: 10294-34-5, Molecular Formula: BCl3, Molecular Weight: 117.16, Appearance: Colorless - Slightly pale yellow clear liquid, Storage: 0-10 deg C, Size: 100ML
MSDS SDS
Supplier:  THERMO FISHER SCIENTIFIC CHEMICALS
Description:   Boron trifluoride, 12% (1.5M) in methanol, AcroSeal, Size: 100ml
Catalog Number: (AA40608-04)

Supplier:  Thermo Scientific Chemicals
Description:   MDL: MFCD00011317
MSDS SDS
Supplier:  THERMO FISHER SCIENTIFIC CHEMICALS
Description:   Boron trichloride, 1M solution in hexane, AcroSeal, Size: 100ml
Supplier:  THERMO FISHER SCIENTIFIC CHEMICALS
Description:   Boron tribromide 1 M in methylene chloride
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
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The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
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