Sie suchten nach: L(+)-Cystein+Hydrochlorid

Artikel-Nr: (BOSSBS-8300R)

Lieferant: Bioss

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

Aktion

Artikel-Nr: (ENZOALX522040C050)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Produced in HEK 293 cells. The cysteine-rich region of human DR3 (aa 25-199) is fused to the Fc portion of human IgG1.

UOM: 1 * 50 µG

New Product Aktion

Artikel-Nr: (ENZOALX522024C050)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Produced in HEK 293 cells. The cysteine-rich region of mouse GITR (aa 20-152) is fused to the Fc portion of human IgG1.

UOM: 1 * 50 µG

New Product Aktion

Artikel-Nr: (ENZOBMLZW86550005)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: A ketoaldehyde. An excellent inhibitor of the chymotrypsin-like activity of the proteasome and serine and cysteine proteases in general.

UOM: 1 * 5 mg

New Product Aktion

Artikel-Nr: (BOSSBS-1328R-A647)

Lieferant: Bioss

Beschreibung: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-9515R-CY7)

Lieferant: Bioss

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

Aktion

Artikel-Nr: (BOSSBS-8300R-A680)

Lieferant: Bioss

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

Aktion

Artikel-Nr: (BOSSBS-6701R-CY5.5)

Lieferant: Bioss

Beschreibung: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.

UOM: 1 * 100 µl

Aktion

Lieferant: Apollo Scientific

Beschreibung: Boc-L-Cys-OH 97%

Artikel-Nr: (BOSSBS-8300R-A488)

Lieferant: Bioss

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

Aktion

Artikel-Nr: (BOSSBS-9515R-A555)

Lieferant: Bioss

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

Aktion

Artikel-Nr: (BOSSBS-9515R-A750)

Lieferant: Bioss

Beschreibung: catalyses 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 Signalling 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 characterised by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-9515R-A488)

Lieferant: Bioss

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

Aktion

Artikel-Nr: (BOSSBS-5938R)

Lieferant: Bioss

Beschreibung: LIM domain only 3 (LMO3) belongs to the rhombotin family of cysteine-rich LIM domain oncogenes. It is transcribed mainly in the brain. It interacts with the neuronal transcription factor, HEN2, and acts as an oncogene in neuroblastoma.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-8300R-A647)

Lieferant: Bioss

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

Aktion

Artikel-Nr: (BOSSBS-12936R-CY5)

Lieferant: Bioss

Beschreibung: 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

Aktion