You Searched For: S-Benzyl-L-cysteine

Catalog Number: (BOSSBS-2976R-FITC)

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.

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Catalog Number: (BOSSBS-5114R-CY5.5)

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]

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Catalog Number: (BOSSBS-5114R-A350)

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]

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Catalog Number: (BOSSBS-8383R-A555)

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.

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Catalog Number: (BOSSBS-8383R-A488)

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.

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Catalog Number: (BOSSBS-2976R-CY5)

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-A680)

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 hydrolysed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyse 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 defence mechanism. Isoform 3 seems to be inactive.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9547R-CY5)

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.

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Catalog Number: (BOSSBS-9547R-CY5.5)

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-CY5)

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.

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Catalog Number: (BOSSBS-8184R-CY3)

Supplier: Bioss

Description: CRELD1 is a protein composed of Epidermal growth factor-like repeats, which represent a group of cysteine-rich domains that mediate interactions between proteins of diverse function. Such domains are found in proteins that are either completely secreted or have transmembrane regions that link the protein to the cell surface.

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Catalog Number: (BOSSBS-12503R-A750)

Supplier: Bioss

Description: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation.

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Catalog Number: (BOSSBS-8329R-A750)

Supplier: Bioss

Description: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.

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Supplier: Biotium

Description: This antibody recognizes a glycoprotein of 75 kDa, identified as low affinity Nerve Growth Factor (NGF) Receptor (p75NGFR) or Neurotrophin Receptor (p75NTR). Its epitope spans in aa 1-160 of extracellular domain of NGFR/NTR. NGF-receptor contains an extracellular domain containing four 40-amino acid repeats with 6 cysteine residues at conserved positions followed by a serine/threonine-rich region, a single transmembrane domain, and a 155-amino acid cytoplasmic domain. The cysteine-rich region contains the nerve growth factor binding domain. NGF is important for the development, differentiation, and survival of variety of neuronal and non-neuronal cells. Its action is mediated by binding two distinct receptors, the high affinity p140 and low affinity p75.

Catalog Number: (BOSSBS-3595R-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 the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes the most abundant extracellular inhibitor of cysteine proteases, which is found in high concentrations in biological fluids and is expressed in virtually all organs of the body. A mutation in this gene has been associated with amyloid angiopathy. Expression of this protein in vascular wall smooth muscle cells is severely reduced in both atherosclerotic and aneurysmal aortic lesions, establishing its role in vascular disease. [provided by RefSeq].

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Catalog Number: (BOSSBS-6236R-A647)

Supplier: Bioss

Description: This gene encodes one of several deubiquitylating enzymes. Ubiquitin modification of proteins is needed for their stability and function; to reverse the process, deubiquityling enzymes remove ubiquitin. This protein contains an OTU domain and binds Ubal (ubiquitin aldehyde); an active cysteine protease site is present in the OTU domain.

UOM: 1 * 100 µl

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