You Searched For: Tungsten+disulphide

Supplier: Thermo Fisher Scientific

Description: Tungsten ≥99.95% (metals basis), foil, Thickness: 0.05 mm (0.002 in)

SDS Certificates

Supplier: Thermo Fisher Scientific

Description: Tungsten (gold coated) ≥99.95% (metals basis) Au 99.99%, wire, Ø 0.025 mm (0.001 in)

SDS Certificates

Catalog Number: (50334-100ML)

Supplier: Merck

Description: Tungsten Standard, 1000 mg/L, TraceCERT®, Supelco®, Tungsten, Matrix: 5% HNO₃/2% HF, Application: ICP standards

UOM: 1 * 100 mL

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Supplier: Thermo Fisher Scientific

Description: Tungsten, gauze woven from wire 150 mesh woven from 0.02mm (0.0008in)

Certificates

Supplier: Thermo Fisher Scientific

Description: Disulphiram 97%

SDS

Supplier: Thermo Fisher Scientific

Description: Tungsten ≥99.95% (metals basis), wire, annealed, Ø 0.5 mm (0.02 in)

SDS Certificates

Supplier: Thermo Fisher Scientific

Description: Tungsten Standard, 1000 mg/L, Specpure®, Tungsten, Matrix: 5% HNO₃, Application: ICP standards

SDS Certificates

Supplier: Thermo Fisher Scientific

Description: Tungsten (platinium coated), wire, Ø 0.25 mm (0.01 in)

SDS Certificates

Supplier: Apollo Scientific

Description: Disulphiram

Catalog Number: (BOSSBS-4250R-A750)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilised by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4250R-A647)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4250R-A350)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

UOM: 1 * 100 µl

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Supplier: Thermo Fisher Scientific

Description: 2,2'-Dithiodianiline (thulium ionophore I) 97%

SDS

Supplier: Thermo Fisher Scientific

Description: Tungsten trioxide ≥99.998% (metals basis excluding Mo), Puratronic® (max. 0.01% Mo)

SDS Certificates

Supplier: Thermo Fisher Scientific

Description: Tungsten, gauze woven from wire 40 mesh woven from 0.025mm (0.001in)

SDS Certificates

Catalog Number: (BOSSBS-4250R-A555)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

UOM: 1 * 100 µl

Sale