You Searched For: 4-n-Butoxyphenyl+isocyanate


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Description: Dopamine beta-hydroxylase inhibitor
Catalog Number: CAAAB20721-30
Supplier: Thermo Scientific Chemicals

Description: Rabbit Polyclonal antibody to ERp57 (protein disulfide isomerase family A, member 3)
Catalog Number: 89321-364
Supplier: Genetex


Description: 1mg (Disulfide bond) CAS: 64813-74-7 C76H104N18O19S2 FW: 1637.91 . somatostatin
Catalog Number: H-4664.0001BA
Supplier: Bachem Americas


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: 10772-610
Supplier: Peprotech


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: 10481-416
Supplier: Bioss


Description: 1mg (Disulfide bond) CAS: 59481-23-1 C82H108N18O20S2 FW: 1730 . somatostatin
Catalog Number: H-5000.0001BA
Supplier: Bachem Americas


Description: GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase which belongs to the Erv1/ALR family of proteins. GFER is widely expressed in various human tissues. They are two isoforms of this protein. Isoform 1 could regenerate the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. Isoform 2 may act as an autocrine hepatotrophic growth factor promoting liver regeneration. GFER could also induce the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC). S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases play an important role in the synthesis of polyamines.
Catalog Number: 75789-846
Supplier: Prosci


Description: Persephin is a disulfide-linked, homodimeric, neurotrophic factor structurally related to GDNF, artemin, and neurturin. These proteins belong to the cysteine knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFR α (α1-α4) receptors. The GFRα4 was first identified in chicken, and was later shown to be the preferential binding subunit for persephin. Persephin promotes the survival of ventral midbrain dopaminergic neurons and motor neurons after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud branching. However, in contrast to GDNF and neurturin, persephin does not support the survival of peripheral neurons. Recombinant Human Persephin is a disulfide-linked homodimer, composed of two 10.4 kDa polypeptide chains (194 total amino acid residues). Each chain contains seven conserved cysteine residues, one of which (Cys 64) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.
Catalog Number: 10781-254
Supplier: Peprotech


Description: Biotinyl-Amylin (mouse, rat) Trifluoroacetate salt, (Disulfide bond), Molecular Formula: C177H286N54O55S3, CAS: [1678414-88-4] net, for Diabetes, 1mg
Catalog Number: 10796-816
Supplier: Bachem Americas


Description: Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRalpha (alpha1-alpha4) receptors. Artemin prefers the receptor GFRalpha3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia such as sympathetic, neural crest and placodally derived sensory neurons, and dompaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer, of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
Catalog Number: 10072-620
Supplier: Prosci


Description: Persephin is a disulfide-linked, homodimeric, neurotrophic factor structurally related to GDNF, artemin, and neurturin. These proteins belong to the cysteine knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFR α (α1-α4) receptors. The GFRα4 was first identified in chicken, and was later shown to be the preferential binding subunit for persephin. Persephin promotes the survival of ventral midbrain dopaminergic neurons and motor neurons after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud branching. However, in contrast to GDNF and neurturin, persephin does not support the survival of peripheral neurons. Recombinant Murine Persephin is a disulfide-linked homodimer, composed of two 10.3 kDa polypeptide chains (192 total amino acid residues). Each chain contains seven conserved cysteine residues, one of which (Cys 63) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.
Catalog Number: 10774-814
Supplier: Peprotech


Description: MDL: MFCD00011227 Insoluble in water, in dilute HCl
Catalog Number: CAAA42943-36
Supplier: Thermo Scientific Chemicals

Description: GDNF is a disulfide-linked homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRalpha (alpha1-alpha4) receptors. GDNF specifically promotes dopamine uptake and survival and morphological differentiation of midbrain neurons. Using Parkinson's disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. Both the functional human and rat GDNF ligand is a disulfide-linked homodimer, of two 15 kDa polypeptide chains called monomers. The functional murine GDNF ligand is a disulfide-linked homodimer, of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, one of which (Cys 101) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration.
Catalog Number: 10072-244
Supplier: Prosci


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.
Catalog Number: 10779-780
Supplier: Peprotech


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: 10481-412
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: 10481-402
Supplier: Bioss


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