You Searched For: S-Benzyl-L-cysteine

Catalog Number: (BOSSBS-8300R)

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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Catalog Number: (BOSSBS-6701R-CY5.5)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-5938R)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-9515R-FITC)

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-12936R-CY5)

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: (786-045)

Supplier: G-Biosciences

Description: Antipain hydrochloride inhibits Ca2+-dependent endopeptidases, including papain, trypsin-like serine proteases, some cysteine proteases and to a lesser extent plasmin. It has a higher specificity for trypsin and papain compared to leupeptin.

UOM: 1 * 5 mg

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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-5114R-A647)

Supplier: Bioss

Description: The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins, and kininogens. This gene encodes a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. The protein is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Stefins have been proposed as prognostic and diagnostic tools for cancer. [provided by RefSeq, Jul 2008]

UOM: 1 * 100 µl

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Supplier: Apollo Scientific

Description: Boc-L-Cys-OH 97%

Catalog Number: (ENZOBMLZW86550005)

Supplier: ENZO LIFE SCIENCES

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

UOM: 1 * 5 mg

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Catalog Number: (BOSSBS-8383R-CY5)

Supplier: Bioss

Description: Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (UBE1s), ubiquitin-conjugating enzymes (UBE2s), and ubiquitin-protein ligases (UBE3s). When ubiquitin is activated by a UBE1, it is transferred to the cysteine residue on a UBE2. UBE2 then binds a UBE3, which transfers the ubiquitin from the UBE2 cysteine to a lysine residue on the target protein. Ubiquitin-conjugating enzyme E2 Q1 (UBE2Q1), also known as ubiquitin-protein ligase Q1 or ubiquitin carrier protein Q1, is an 422 amino acid protein belonging to the ubiquitin-conjugating enzyme (UBE2) family. Two named isoforms of UBE2Q1 exist as a result of alternative splicing events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-8383R-A680)

Supplier: Bioss

Description: Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (UBE1s), ubiquitin-conjugating enzymes (UBE2s), and ubiquitin-protein ligases (UBE3s). When ubiquitin is activated by a UBE1, it is transferred to the cysteine residue on a UBE2. UBE2 then binds a UBE3, which transfers the ubiquitin from the UBE2 cysteine to a lysine residue on the target protein. Ubiquitin-conjugating enzyme E2 Q1 (UBE2Q1), also known as ubiquitin-protein ligase Q1 or ubiquitin carrier protein Q1, is an 422 amino acid protein belonging to the ubiquitin-conjugating enzyme (UBE2) family. Two named isoforms of UBE2Q1 exist as a result of alternative splicing events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-8383R-A750)

Supplier: Bioss

Description: Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (UBE1s), ubiquitin-conjugating enzymes (UBE2s), and ubiquitin-protein ligases (UBE3s). When ubiquitin is activated by a UBE1, it is transferred to the cysteine residue on a UBE2. UBE2 then binds a UBE3, which transfers the ubiquitin from the UBE2 cysteine to a lysine residue on the target protein. Ubiquitin-conjugating enzyme E2 Q1 (UBE2Q1), also known as ubiquitin-protein ligase Q1 or ubiquitin carrier protein Q1, is an 422 amino acid protein belonging to the ubiquitin-conjugating enzyme (UBE2) family. Two named isoforms of UBE2Q1 exist as a result of alternative splicing events.

UOM: 1 * 100 µl

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Supplier: Thermo Fisher Scientific

Description: (R)-Ethyl-2-amino-3-mercaptopropanoate hydrochloride ≥98%

SDS Certificates

Catalog Number: (BOSSBS-8300R-A488)

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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Catalog Number: (BOSSBS-8300R-A680)

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 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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