You Searched For: Aluminium+oxide

Catalog Number: (470165-354)

Supplier: EMEDCO

Description: These labels help identify hazardous items in your facility.

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Supplier: 3M

Description: Stikit™ Gold abrasive sheets features continuous lengths of A-weight paper, easily cut to size to greatly reduce product waste. Aluminum oxide mineral abrasive delivers a sharp cut and uniform finish during collision repair.

Catalog Number: (10280-238)

Supplier: Bioss

Description: Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH9A1 (aldehyde dehydrogenase family 9 member A1), also known as E3, ALDH4, ALDH7, ALDH9 or TMABADH, is a 494 amino acid cytoplasmic protein that is highly expressed in adult liver, skeletal muscle, kidney and embryonic brain. ALDH9A1 converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine and catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in a NAD-dependent reaction.

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Catalog Number: (10297-626)

Supplier: Bioss

Description: Glucose Oxidase is a dimeric enzyme that binds to β-D-glucose and aids in its oxidation into D-glucono-1,5-lactone which then hydrolyzes to gluconic acid. Flavin adenine dinucleotide (FAD) is a cofactor to Glucose Oxidase that acts as the initial electron acceptor and is required for this oxidation to occur. Glucose Oxidase is a natural preservative found in honey, where it reduces atmospheric oxygen into hydrogen peroxide which acts as an antibacterial barrier. Glucose Oxidase is also commonly used in biosensors in which it conveys levels of glucose by keeping track of the number of electrons passed through the enzyme. In this application, Glucose Oxidase is connected to an electrode and the resulting charge is measured.

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Catalog Number: (10085-504)

Supplier: Proteintech

Description: CYP1A2, also named as CP12; P3-450 and P450(PA), belongs to the cytochrome P450 family. Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, CYP1A2 is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active of CYP1A2 is in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. It also acts in the metabolism of aflatoxin B1 and acetaminophen. CYP1A2 participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. It catalizes the reaction: RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. The antibody is specific to CYP1A2.

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Catalog Number: (76707-170)

Supplier: AFG BIOSCIENCE LLC

Description: Human Diamine Oxidase(DAO) ELISA Kit

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Catalog Number: (76714-762)

Supplier: AFG BIOSCIENCE LLC

Description: Rat Monoamine Oxidase A(MAOA) ELISA Kit

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Catalog Number: (76078-434)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

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Catalog Number: (76190-868)

Supplier: Safety & Industrial Supplies

Description: Forged alloy steel.

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Supplier: GS Medical Packaging

Description: All STERIL-PEEL® products are manufactured from medical grade bleached kraft paper, hydrogen peroxide, rather than chlorine is used as the bleaching agent

Certificates

Catalog Number: (68100-000)

Supplier: Baxter

Description: Solutions for irrigation.

SDS Certificates Sale

Catalog Number: (10091-298)

Supplier: Proteintech

Description: NRF2, also named as NFE2L2, belongs to the bZIP family and CNC subfamily. It is a transcription activator that binds to antioxidant response (ARE) elements in the promoter regions of target genes. NRF2 is important for the coordinated up- regulation of genes in response to oxidative stress. It may be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region.Nrf2 is a key player in the regulation of genes encoding for many antioxidative response enzymes.The expression of NRF2 may be induced under oxidative stress .In lung cancer, Nrf2 activation in malignant cells has been associated with tumor progression and chemotherapy resistance. Identifying patients with abnormal NRF2 expression may be important for selection for chemotherapy in NSCLC.This antibody is a rabbit polyclonal antibody raised against the C-terminal amino acid residues (C-350 aa) of human NRF2 protein.

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Catalog Number: (10332-126)

Supplier: Bioss

Description: Cytochromes P45 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase.

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Catalog Number: (10332-140)

Supplier: Bioss

Description: Cytochromes P45 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase.

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Catalog Number: (10336-436)

Supplier: Bioss

Description: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.

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Catalog Number: (76082-348)

Supplier: Bioss

Description: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and SKT4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner.

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