You Searched For: S-(Carboxymethyl)-L-cysteine

Catalog Number: (BOSSBS-5114R-CY7)

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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Catalog Number: (BOSSBS-6701R-HRP)

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-8383R-CY3)

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-5114R-HRP)

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: Thermo Fisher Scientific

Description: (R)-3-(Benzylthio)-2-((tert-butoxycarbonyl)amino)propanoic acid 98%

Catalog Number: (ENZOBMLSE5680005)

Supplier: ENZO LIFE SCIENCES

Description: Recombinant glycosylated procathepsin F cloned from human cDNA (NM_003793), expressed in insect cells, and purified as the active form of the enzyme. Cathepsin F, a member of the papain family of lysosomal cysteine proteases, acts upon proteins such as MHC Class II-associated invariant chain and ApoB-100.

UOM: 1 * 5 µG

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Catalog Number: (BOSSBS-2976R-A350)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2976R-CY3)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2976R-A647)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

UOM: 1 * 100 µl

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Supplier: G-Biosciences

Description: Antibody Fab and F(ab)₂ Fragmentation of Mouse IgG₁ Kits are designed for the generation and isolation of Fab and F(ab)₂ fragments from mouse IgG₁ molecules. The kit utilises Immobilised Ficin resin. Ficin (or Ficain) (~25000 Da) is a cysteine protease enzyme (EC 3.4.22.3) isolated from fig latex that has the endopeptidase activity to cleave immunoglobulin G molecules in the hinge region. Ficin has an effective range of pH 4 to 9,5 with an optimal pH of 6,5 and cleaves bonds that involve uncharged or aromatic amino acids. Ficin is typically used to cleave mouse IgG₁ as this is difficult to cleave with papain and pepsin. In the presence of 1 to 4 mM or 10 to 20 mM cysteine, ficin generates F(ab)₂ and Fab fragments respectively.

Catalog Number: (BOSSBS-0156R)

Supplier: Bioss

Description: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.

UOM: 1 * 100 µl

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Supplier: ENZO LIFE SCIENCES

Description: Methyltransferase inhibitor

Catalog Number: (BOSSBS-6701R-CY3)

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-9547R-A555)

Supplier: Bioss

Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9548R-A488)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9548R-HRP)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

UOM: 1 * 100 µl

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