You Searched For: Dithiothreitol+(DTT,+Cleland\\\\\\\'s+reagent)

Supplier: VWR Chemicals

Description: Dithiothreitol (DTT, Cleland's reagent) ≥98%

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Supplier: VWR Chemicals

Description: Dithiothreitol (DTT, Cleland's reagent) ≥99.4%, Proteomics Grade

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Catalog Number: (BAKRF781-05)

Supplier: Avantor

Description: Dithiothreitol (DTT, Cleland's reagent) ≥99.0%, Biotech Reagent, J.T.Baker®

UOM: 1 * 1 kg

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Supplier: Avantor

Description: Dithiothreitol (DTT, Cleland's reagent) ≥99.5%, Ultrapure Bioreagent, J.T.Baker®

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Supplier: Thermo Scientific

Description: Dithiothreitol (DTT, Cleland's reagent) ≥98%

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Supplier: Thermo Scientific

Description: Dithiothreitol (DTT, Cleland's reagent) ≥99% for electrophoresis

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Supplier: VWR Chemicals

Description: An excellent reagent for maintaining SH groups in reduced state; quantitatively reduces disulfides. DTT is effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE.

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Supplier: Thermo Scientific

Description: Used as a protective agent for SH groups.

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Supplier: PanReac AppliChem

Description: Dithiothreitol (DTT, Cleland's reagent) ≥99.5% for molecular biology

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Supplier: PanReac AppliChem

Description: Dithiothreitol (DTT, Cleland's reagent) ≥99.5% (by iodometry) for biochemistry

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Catalog Number: (ICNA04856126)

Supplier: MP Biomedicals

Supplier Article Number:: 04856126

Description: DL-Dithiothreitol is also known as Clelands reagent; Protective agent for sulfhydryl groups (-SH). Quantitatively reduces disulfides (-S-S- to -SH). In this reaction the DTT is oxidized to the cyclic disulfide which ensures the reduction of other disulfides in solution. Disulfide reduction occurs quickly at pH 8.
Dithiothreitol is useful for stabilizing sulfhydryl containing enzymes. Effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE. DTT can also be used for reducing the disulfide bridge of the cross-linker N,N'-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel. DTT is less pungent and is less toxic than 2-mercaptoethanol.
Useful for stabilizing sulfhydryl-containing enzymes.

UOM: 1 * 5 g

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Supplier: PanReac AppliChem

Description: Dithiothreitol (DTT, Cleland's reagent) 1 mol/l in aqueous solution

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Supplier: MP Biomedicals

Description: Dithiothreitol (DTT, Cleland's reagent) ≥99% for molecular biology

Supplier: MP Biomedicals

Description: Dithioerythritol is an erythro isomer of 2,3-dihydroxy-1,4-dithiolbutane, and an isomer of 1,4-dithiothreitol which is a reagent for maintaining thiols in the reduced state; prevents oxidation of sulfhydryl-containing proteins during SDS-polyacrylamide gel electrophoresis. It also quantitatively reduces disulfides.

Catalog Number: (PIER20490)

Supplier: Thermo Fisher Scientific

Supplier Article Number:: 20490

Description: Thermo Scientific Pierce TCEP-HCl is a potent, versatile, odorless, thiol-free reducing agent with broad application to protein and other research involving reduction of disulfide bonds. The unique compound is easily soluble and very stable in many aqueous solutions. TCEP reduces disulfide bonds as effectively as dithiothreitol (DTT), but unlike DTT and other thiol-containing reducing agents, TCEP does not have to be removed before certain sulfhydryl-reactive crosslinking reactions.

UOM: 1 * 1 g

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Supplier: MP Biomedicals

Description: Guanidine Hydrochloride is a protein denaturant and thus having an important role in molecular weight determinations.
Guanidine Hydrochloride is a strong chaotropic agent useful for the denaturation and subsequent refolding of proteins. This strong denaturant can solubilize insoluble or denatured proteins such as inclusion bodies. This can be used as the first step in refolding proteins or enzymes into their active form. Urea and dithiothreitol (DTT) may also be necessary. Guanidine HCl is used in the isolation of RNA to dissociate the nucleoprotein into its nucleic acid and protein moieties. It is an inhibitor of RNase. Highly concentrated (6 - 8 M) Guanidine HCl solutions are used to denature native globular proteins. It apparently disrupts hydrogen bonds which hold the protein in its unique structure. However, there also is evidence suggesting that guanidine hydrocholoride may disrupt hydrophobic interactions by promoting the solubility of hydrophobic residues in aqueous solutions.