You Searched For: S-Trityl-D-cysteine

Supplier: Apollo Scientific

Description: Intermediate in trans-sulfuration whereby the sulfur of methionine is transferred via homocysteine to cysteine. Collection Czechoslov.

Catalog Number: (BOSSBS-5808R-CY5)

Supplier: Bioss

Description: 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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Catalog Number: (BOSSBS-5808R-HRP)

Supplier: Bioss

Description: 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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Catalog Number: (BOSSBS-5808R-FITC)

Supplier: Bioss

Description: 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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Catalog Number: (BOSSBS-5808R-CY5.5)

Supplier: Bioss

Description: 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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Catalog Number: (BOSSBS-8300R-A647)

Supplier: Bioss

Description: 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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Supplier: Apollo Scientific

Description: Boc-Cys(pMeOBzl)-OH 97+%

Catalog Number: (BOSSBS-4009R)

Supplier: Bioss

Description: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9515R-CY7)

Supplier: Bioss

Description: 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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Catalog Number: (BOSSBS-4009R-CY3)

Supplier: Bioss

Description: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4009R-CY5)

Supplier: Bioss

Description: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.

UOM: 1 * 100 µl

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Catalog Number: (ENZOALX522031C050)

Supplier: ENZO LIFE SCIENCES

Description: Produced in HEK 293 cells. The cysteine-rich region of human CD137 (4-1BB) (aa 1-186) is fused to the Fc portion of human IgG1.

UOM: 1 * 50 µG

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Catalog Number: (ENZOALX522016C050)

Supplier: ENZO LIFE SCIENCES

Description: Produced in HEK 293 cells. The cysteine-rich region (aa 21-193) of human CD40 is fused to the Fc portion of human IgG1.

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-12936R-HRP)

Supplier: Bioss

Description: The cystatin superfamily is a well-established family of cysteine protease inhibitors. All true cystatins inhibit cysteine peptidases of the papain family, such as cathepsins, while some also inhibit legumain family enzymes. The CRES (cystatin-related epididymal spermatogenic) protein defines a new subgroup in the family 2 cystatins of the cystatin superfamily. CRES proteins lack two of the three consensus sites necessary for the cystatin inhibition of C1 cysteine proteases. They are also preferentially expressed in postmeiotic germ cells, the proximal caput epididymidis, and anterior pituitary gonadotrophs. Therefore, CRES proteins may perform unique and tissue-specific functions in the reproductive and neuroendocrine systems. As a member of the CRES subfamily, Cystatin-like 1 (CSTL1) is a 145 amino acid protein and is expressed in testis.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12936R-CY3)

Supplier: Bioss

Description: The cystatin superfamily is a well-established family of cysteine protease inhibitors. All true cystatins inhibit cysteine peptidases of the papain family, such as cathepsins, while some also inhibit legumain family enzymes. The CRES (cystatin-related epididymal spermatogenic) protein defines a new subgroup in the family 2 cystatins of the cystatin superfamily. CRES proteins lack two of the three consensus sites necessary for the cystatin inhibition of C1 cysteine proteases. They are also preferentially expressed in postmeiotic germ cells, the proximal caput epididymidis, and anterior pituitary gonadotrophs. Therefore, CRES proteins may perform unique and tissue-specific functions in the reproductive and neuroendocrine systems. As a member of the CRES subfamily, Cystatin-like 1 (CSTL1) is a 145 amino acid protein and is expressed in testis.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12936R-A350)

Supplier: Bioss

Description: The cystatin superfamily is a well-established family of cysteine protease inhibitors. All true cystatins inhibit cysteine peptidases of the papain family, such as cathepsins, while some also inhibit legumain family enzymes. The CRES (cystatin-related epididymal spermatogenic) protein defines a new subgroup in the family 2 cystatins of the cystatin superfamily. CRES proteins lack two of the three consensus sites necessary for the cystatin inhibition of C1 cysteine proteases. They are also preferentially expressed in postmeiotic germ cells, the proximal caput epididymidis, and anterior pituitary gonadotrophs. Therefore, CRES proteins may perform unique and tissue-specific functions in the reproductive and neuroendocrine systems. As a member of the CRES subfamily, Cystatin-like 1 (CSTL1) is a 145 amino acid protein and is expressed in testis.

UOM: 1 * 100 µl

Sale