Sie suchten nach: N-Acetyl-L-cystein

Artikel-Nr: (BOSSBS-8300R-CY5)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-8300R-CY5

Beschreibung: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.

UOM: 1 * 100 µl

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Artikel-Nr: (BOSSBS-8300R-CY7)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-8300R-CY7

Beschreibung: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.

UOM: 1 * 100 µl

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Lieferant: Thermo Fisher Scientific

Beschreibung: Alkylating agent used in peptide mapping because it covalently binds with the thiols in cysteine to prevent disulfide bond formation.

Sicherheitsdatenblätter Zertifikate

Artikel-Nr: (BOSSBS-2640R)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-2640R

Beschreibung: Human thiol dioxygenases include cysteine dioxygenase (CDO; MIM 603943) and cysteamine (2-aminoethanethiol) dioxygenase (ADO; EC 1.13.11.19). CDO adds 2 oxygen atoms to free cysteine, whereas ADO adds 2 oxygen atoms to free cysteamine to form hypotaurine (Dominy et al., 2007 [PubMed 17581819]).[supplied by OMIM]

UOM: 1 * 100 µl

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Lieferant: Apollo Scientific

Beschreibung: Fmoc-Cys(Me)-OH

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Cysteine protease inhibitor

New Product

Artikel-Nr: (BOSSBS-9515R)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-9515R

Beschreibung: Catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure.Defects in CTH are the cause of cystathioninuria (CSTNU). It is an autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.

UOM: 1 * 100 µl

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Lieferant: Apollo Scientific

Beschreibung: Fmoc-Cys-OH 96%

Artikel-Nr: (1294848.)

Lieferant: USP

Hersteller Artikel Nummer : 1294848

Beschreibung: USP Reference Standards are specified for use in conducting official USP–NF tests and assays. USP also provides Reference Standards specified in the Food Chemicals Codex as well as authentic substances—high-quality chemical samples—as a service to analytical, clinical, pharmaceutical and research laboratories. To confirm accuracy and reproducibility, USP Reference Standards are rigorously tested and evaluated by multiple independent laboratories including USP, commercial, regulatory, and academic labs. USP also provide publicly available, official documentary standards for pharmaceutical ingredients in the USP–NF that link directly with our primary reference standards.

UOM: 1 * 30 mg

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Artikel-Nr: (BOSSBS-8300R-A750)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-8300R-A750

Beschreibung: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidised to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidised to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidised Prx can be reduced back to the active form during recovery after oxidative stress.

UOM: 1 * 100 µl

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Artikel-Nr: (APOSBIM110-1G)

Lieferant: Apollo Scientific

Hersteller Artikel Nummer : BIM110-1G

Beschreibung: Modifies sulphhydryl on cysteine. Substitute for ethylene imine.

UOM: 1 * 1 g

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Artikel-Nr: (BOSSBS-5774R-CY5)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-5774R-CY5

Beschreibung: The cysteine-rich, adipose tissue-specific, secretory factor resistin (resistance to insulin, also known as ADSF) is a secreted hormone that potentially links obesity to diabetes. Resistin is rich in serine and cysteine residues and contains a unique cysteine repeat motif. Resistin and the resistin-like molecules share the characteristic cysteine composition and other signature features. Resistin-like a is a secreted protein that has restricted tissue distribution and is most highly expressed in adipose tissue. Another family member, Resistin-like b, is a secreted protein expressed only in the gastrointestinal tract, particularly in the colon, in both mouse and human. Resistin-like b expression is highest in proliferative epithelial cells and is markedly increased in tumors, suggesting a role in intestinal proliferation.

UOM: 1 * 100 µl

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Lieferant: Thermo Fisher Scientific

Beschreibung: Appearance: White to light yellow Powder

Sicherheitsdatenblätter

Artikel-Nr: (BOSSBS-5808R)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-5808R

Beschreibung: CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

UOM: 1 * 100 µl

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Artikel-Nr: (BOSSBS-5808R-CY7)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-5808R-CY7

Beschreibung: CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

UOM: 1 * 100 µl

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Artikel-Nr: (BOSSBS-5808R-A488)

Lieferant: Bioss

Hersteller Artikel Nummer : BS-5808R-A488

Beschreibung: CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

UOM: 1 * 100 µl

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