You Searched For: Formamidine+disulfide+dihydrochloride

Catalog Number: (10397-122)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

Catalog Number: (H-5968.1000BA)

Supplier: Bachem Americas

Description: BNP, originally isolated from porcine brain, belongs to the class of natriuretic peptides, having an amino acid sequence and a pharmacological activity spectrum (including diuretic-natriuretic, hypotensive, and vasorelaxant actions) remarkably similar to that of atrial natriuretic peptide (ANP). Meanwhile, BNP precursor molecules have also been shown to exist in human and rat cardiac tissue. Comparison of the precursor sequences demonstrates structural species differences between the mammalian BNPs, a finding which contrasts with the highly conserved ANP sequences.

Catalog Number: (10397-118)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

Supplier: Peprotech

Description: The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are secreted in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF-3 is expressed by goblet cells and in the uterus, and has also been shown to be expressed in certain cancers, including colorectal, hepatocellular, and in biliary tumors. TFF3 may be useful as a molecular marker for certain types of cancer, but its role, if any, in tumorigenesis is unknown. TFF3 also promotes airway epithelial cell migration and differentiation. Recombinant Human TFF-3 is a 13.2 kDa homodimeric protein consisting of two 59 amino acid chains, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.

Supplier: Peprotech

Description: The originally described IL-17 protein, now known as IL-17A, is a homodimer of two 136 amino acid chains that are secreted by activated T-cells, which act on stromal cells to induce production of proinflammatory and hematopoietic bioactive molecules. Today, IL-17 represents a family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17A exhibits cross-species bioactivity between human and murine cells. Recombinant Murine IL-17A is a 30.0 kDa, disulfide-linked homodimer of two 133 amino acid, polypeptide chains.

Supplier: Peprotech

Description: Activin A is a TGF-β family member that exhibits a wide range of biological activities, including regulation of cellular proliferation and differentiation, and promotion of neuronal survival. Elevated levels of Activin A in human colorectal tumors and in postmenopausal women have been implicated in colorectal and breast cancers, respectively. The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-β antagonist, follistatin. Activin A binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). Activins are homodimers or heterodimers of different β subunits. They are produced as precursor proteins with an amino terminal propeptide that is cleaved to release the C-terminal bioactive ligand. Recombinant Human/Murine/Rat Activin A is a 26.0 kDa disulfide-linked homodimer of two βA chains, each containing 116 amino acid residues.

Certificates

Supplier: Peprotech

Description: Lectins, of either plant or animal origin, are carbohydrate-binding proteins that interact with glycoproteins and glycolipids on the surface of animal cells. The Galectins are lectins that recognize and interact with β-galactoside moieties. Galectin-3 regulates a number of biological processes, including embryogenesis, inflammatory responses, cell progression and metastasis. Galectin-3 is normally expressed in epithelia of a variety of tissues, including colon and endometrium, and in various inflammatory cells, including macrophages. Galectin-3 can function intracellularly, controlling the cell cycle and preventing T-cell apoptosis, and also extracellularly, by activating various cells, including monocytes/macrophages, mast cells, neutrophils, and lymphocytes. Expression of Galectin-3 is affected by neoplastic transformation, being up-regulated in certain types of lymphomas, and in thyroid and hepatic carcinomas. Conversely, it is down-regulated in other cancers such as colon, breast, ovarian, and uterine. Recombinant Human Galectin-3 is a globular 26.0 kDa protein containing 250 amino acid residues, but no disulfide bonds.

Supplier: VWR

Description: An excellent reagent for maintaining SH groups in reduced state; quantitatively reduces disulfides. DTT is effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE. DTT can also be used for reducing the disulfide bridge of the cross-linker N,N′-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel. DTT is less pungent and is less toxic than 2-mercaptoethanol. Typically, a seven fold lower concentration of DTT (100 mM) is needed than is used for 2-mercaptoethanol (5% v/v, 700 mM).

SDS Certificates

Supplier: Thermo Scientific Chemicals

Description: Alkylating agent used in peptide mapping because it covalently binds with the thiols in cysteine to prevent disulfide bond formation

Certificates

Catalog Number: (76303-724)

Supplier: Peprotech

Description: GDF-11 is a myostatin-homologous protein that acts as an inhibitor of nerve tissue growth. GDF-11 has been shown to suppress neurogenesis through a myostatin-like pathway, which involves the arrest of the progenitor cell cycle in the G1 phase. Similarities between myostatin and GDF-11, which are 90% identical in their amino acid sequence, suggest that the regulatory mechanisms responsible for maintaining proper tissue size during neural and muscular development might be the same. Recombinant Human/Murine/Rat GDF-11 is a 25.0 kDa disulfide-linked homodimer containing two 109 amino acid polypeptide chains. It is highly homologous to myostatin/GDF-8, sharing 90% amino acid sequence identity.

Supplier: Peprotech

Description: Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-β family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Certificates

Supplier: Bachem Americas

Description: Highly potent and selective β-MSH-derived melanocortin-4 receptor (MC-4R) agonist with sub-nanomolar potency. The binding affinities for human MC-4R, MC-1R, MC-3R and MC-5R were 0.55 ± 0.06, 16.78 ± 1.53, 56.79 ± 4.66, and < 500 nM, respectively. Daily subcutaneous injection of H-6268 to diet-induced obese rats over a period of 14 days demonstrated an effect on reduction of fat mass.

Supplier: Peprotech

Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, and β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-β1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts, and recently it has been implicated in the formation of skin tumors. Recombinant Human TGF-β1 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Supplier: G-Biosciences

Description: The conjugation and modification reactions used to cross-link proteins or couple labels to proteins, such as biotin, enzymes, and fluorescent dyes, require certain conditions, including pH and chemical composition, for optimal conjugation

Catalog Number: (10397-120)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

Catalog Number: (76078-436)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.