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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.


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


Supplier: Thermo Scientific Chemicals
Description: Thiram 97%
Catalog Number: (10110-024)
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: (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: (CAPIPA5-18690)
Supplier: Thermo Scientific
Description: This antibody is predicted to react with mouse and rat based on sequence homology. Protein disulfide isomerases resident proteins that catalyze protein folding and thiol-disulfide interchange reactions .


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: An alternative to Mob in the regioselective formation of disulfide bonds.

Supplier: Prosci
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.

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: Bachem Americas
Description: 0.5mg (Disulfide bond) CAS: 145251-83-8 C86H118N20O21S3 FW: 1864.2 . Synonym: Biotinyl-SRIF

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: Peprotech
Description: IL-17B is a disulfide-linked homodimer of two 161 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-17B is expressed by T-cells, and has been shown to stimulate release of TNF-α and IL-1β from cells of the monocyte lineage. Recombinant Human IL-17B is a 36.6 kDa non-disulfide-linked homodimer of two 161 amino acid polypeptide chains.

Catalog Number: (10104-564)
Supplier: Prosci
Description: TXNDC5 is a protein-disulfide isomerase. Its expression is induced by hypoxia and its role may be to protect hypoxic cells from apoptosis.This gene encodes a protein-disulfide isomerase. Its expression is induced by hypoxia and its role may be to protect hypoxic cells from apoptosis. This gene can be co-transcribed with the upstream gene MU.


Supplier: Peprotech
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 GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional human GDNF ligand is a disulfide-linked homodimer consisting of two 15 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Human GDNF is 30.4 kDa.

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