You Searched For: trans-Bis(tributylstannyl)ethylene

Supplier: Peprotech

Description: IL-17E is a disulfide-linked homodimer of two 145 amino acid polypeptide chains. It belongs to the IL-17 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-17E stimulates secretion of IL-8, and induces activation of the transcription factor NF-κB in cells that express the IL-17BR receptor. Recombinant Human IL-17E is a 33.8 kDa disulfide-linked homodimer of two 146 amino acid polypeptide chains.

Supplier: Peprotech

Description: IL-17D is a disulfide-linked homodimer of two 185 amino acid polypeptide chains. It belongs to the IL-17 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-17D has the ability to stimulate the production of IL-6, IL-8 and GM-CSF, and inhibits hemopoiesis of myeloid progenitor cells in colony-forming assays. Recombinant Human IL-17D is a 40.5 kDa disulfide-linked homodimer of two 185 amino acid polypeptide chains.

Supplier: Peprotech

Description: Neurturin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, artemin, and persephin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Neurturin signals through a multicomponent receptor system, composed of RET and one of four GFRα (α1-α4) receptors. Neurturin promotes the development and survival of sympathetic and sensory neurons by signaling through a receptor system composed of RET and GFRα2. The functional form of human neurturin is a disulfide-linked homodimer, of two 11.8 kDa polypeptide monomers (204 total amino acid residues). Each monomer contains seven conserved cysteine residues, one of which (Cys 69) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.

Supplier: Bachem Americas

Description: 1mg (Disulfide bond) CAS: 90954-53-3 C163H267N51O49S2 FW: 3789.36 . Synonym: CGRP-I (human)

Supplier: Peprotech

Description: GDF-3 is a member of the TGF-β superfamily of growth and differentiation factors, and is highly homologous to GDF-9. Unlike most TGF-β family members, GDF-3 and GDF-9 are not disulfide-linked dimers. GDF-3 is expressed in adult bone marrow, spleen, thymus, and adipose tissue. The expression of GDF-3 is upregulated in high-fat-fed wild-type FABP4/aP2 null mice and was associated with obesity, but not with the related hyperglycemia/hyperinsulinemia that characterizes Type 2 diabetes. Recombinant Human GDF-3 is a 26.0 kDa non-disulfide-linked homodimer containing two 114 amino acid polypeptide chains.

Catalog Number: (75790-186)

Supplier: Prosci

Description: Endoplasmic reticulum resident protein 27, also known as ER protein 27, C12orf46 and ERP27, is an endoplasmic reticulum luminal protein which is a member of the protein disulfide isomerase family. ERP27 contains one thioredoxin domain and does not contain a CXXC active site motif. ERP27 is widely expressed in many tissues; it has highest expression in pancreas, with lower levels in spleen, lung, kidney, thymus, and bone marrow. ERP27 interacts with PDIA3 and binds somatostatin-14 via hydrophobic interactions. ERP27 may act as a protease, protein disulfide isomerase, thiol-disulfide oxidase or phospholipase.

Supplier: Peprotech

Description: Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The four known members of this family, resistin, RELMα, RELMβ, and RELMγ, share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that resistin expression is severely suppressed in obesity, and that it may act as a feedback regulator of Adipogenesis. Recombinant Murine Resistin is a 20.2 kDa, disulfide-linked, homodimeric protein composed of two identical 94 amino acid chains linked by a single disulfide bond.

Catalog Number: (CA200062-798)

Supplier: Enzo Life Sciences

Description: The mammalian PDI (Protein disulfide-isomerase) family encompasses several highly divergent proteins which are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum by catalyzing the rearrangement of disulfide bonds.

Catalog Number: (10481-414)

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.

Catalog Number: (10481-398)

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.

Supplier: Bachem Americas

Description: 0.5mg (Disulfide bonds between Cys2 and Cys19/Cys5 and Cys28/Cys16 and Cys33/Cys20 and Cys35) CAS: 163515-35-3 C158H249N53O47S11 FW: 3995.77 . Synonym: Cltx (Egyptian scorpion)

Catalog Number: (10110-022)

Supplier: Prosci

Description: P4HB is the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Catalog Number: (75790-812)

Supplier: Prosci

Description: Protein Disulfide-Isomerase (P4HB) is an endoplasmic reticulum lumen protein that belongs to the protein disulfide isomerase family. P4HB contains two thioredoxin domains and catalyzes the formation, breakage, and rearrangement of -S-S- bonds in proteins. P4HB is involved in hydroxylation of prolyl residues in preprocollagen. P4HB has the ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner. P4HB plays a role in both the influx and efflux of S-nitrosothiol-bound nitric oxide.

Catalog Number: (10481-400)

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.

Catalog Number: (10481-394)

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.

Catalog Number: (10481-396)

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.