You Searched For: S-Trityl-D-cysteine

Supplier: ENZO LIFE SCIENCES

Description: Methyltransferase inhibitor

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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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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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-2976R-A488)

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-A750)

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-9217R-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. Due to their expression patterns, it is likely that CRES proteins may perform unique and tissue-specific functions in the reproductive and neuroendocrine systems. As a member of the CRES subfamily, Cystatin 9, also designated CLM, is a 159 amino acid protein that is expressed in heart, placenta, lung, liver, skeletal muscle and pancreas. Cystatin 9 is thought to play a role in hematopoietic differentiation or inflammation. It has also been shown to be upregulated by LPS in some cancer cell lines, such as promyelocytic leukemia (HL-60) and myelomonocytic leukemia.

UOM: 1 * 100 µl

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Catalog Number: (1013057.)

Supplier: USP

Description: USP Reference Standards are specified for use in conducting official USP–NF tests and assays. USP also provides Reference Standards specified in the Food Chemicals Codex as well as authentic substances—high-quality chemical samples—as a service to analytical, clinical, pharmaceutical and research laboratories. To confirm accuracy and reproducibility, USP Reference Standards are rigorously tested and evaluated by multiple independent laboratories including USP, commercial, regulatory, and academic labs. USP also provide publicly available, official documentary standards for pharmaceutical ingredients in the USP–NF that link directly with our primary reference standards.

UOM: 1 * 25 mg

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Catalog Number: (BOSSBS-9547R)

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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Supplier: G-Biosciences

Description: Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues and typically there is little or no cleavage at arginyl-proline and lysyl-proline bonds. The distribution of these residues in proteins allows trypsin digestion to produce peptides that are readily identified by mass spectrometry.

Supplier: Merck

Description: L(+)-Cysteine hydrochloride, Sigma-Aldrich®

Catalog Number: (BOSSBS-1328R-CY3)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-6039R-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 the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. Expression of the protein has been observed in various human cancer cell lines established from malignant tumors.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1328R-A350)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-1328R-A680)

Supplier: Bioss

Description: 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

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