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Catalog Number: (76712-080)
Supplier: AFG Bioscience
Description: Mouse WAP Four-disulfide Core Domain Protein 2(WFDC2) ELISA Kit


Catalog Number: (76710-502)
Supplier: AFG Bioscience
Description: Human Protein Disulfide Isomerase A4 (PDIA4) ELISA Kit


Catalog Number: (10086-642)
Supplier: Proteintech
Description: PDIA3, also named as P58, ER60, ERp57, ERp60, ERp61, GRP57, GRP58 and PI-PLC, is a member of the PDI family, participates in the oxidation, reduction, and isomerization of disulfide bonds for correct folding of secretory proteins before modification and transport in the endoplasmic reticulum. It is associated with apoptosis or inhibition of cancer cell growth. PDIA3 was once thought to be a phospholipase; however, it has been demonstrated that this protein actually has protein disulfide isomerase activity. It is thought that complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.


Supplier: Thermo Scientific Chemicals
Description: Thiram 97%
Catalog Number: (TCD1395-025ML)
Supplier: TCI America
Description: [for Determination of Sulfur Content by Energy Dispersive X-ray Fluorescence Method]
CAS Number: 629-45-8
MDL Number: MFCD00009467
Molecular Formula: C8H18S2
Molecular Weight: 178.35
Purity/Analysis Method: >98.5% (GC)
Form: Clear Liquid
Boiling point (°C): 226
Flash Point (°C): 93
Specific Gravity (20/20): 0.94

Catalog Number: (76705-966)
Supplier: AFG Bioscience
Description: Mouse Protein Disulfide-isomerase A4(PDIA4) ELISA Kit


Catalog Number: (10749-244)
Supplier: Prosci
Description: PDIA1 (protein disulfide isomerase family A member 1) 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. PDIA1 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.


Supplier: Peprotech
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 GFRα (α1-α4) receptors. Artemin prefers the receptor GFRα3-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 dopaminergic 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.

Supplier: TCI America
Description: CAS Number: 1142-19-4
MDL Number: MFCD00013642
Molecular Formula: C12H8Cl2S2
Molecular Weight: 287.22
Purity/Analysis Method: >98.0% (GC)
Form: Crystal
Boiling point (°C): 180
Melting point (°C): 72
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: (H-4774.0001BA)
Supplier: Bachem Americas
Description: 1mg (Disulfide bond) CAS: 54518-51-3 C71H96N16O17S2 FW: 1509.77 . somatostatin


Catalog Number: (76109-024)
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: (10481-412)
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
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: 1G (Disulfide bond) CAS: 7369-94-0 C24H30N4O8S2 FW: 566.66

Catalog Number: (75790-684)
Supplier: Prosci
Description: Thioredoxin (TXN) is a member of the Thioredoxin family. Thioredoxin exists as a disulfide-linked homodimer and contains one Thioredoxin domain. Thioredoxin is up-regulated by ionizing radiation. Thioredoxin participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin also plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide.


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