Molecule

DB03345 

Drug information: experimental

02190242 

Used to reduce disulfide linkages in solubilizing proteins for gel electrophoresis. Also reduces excess oxidative polymerization of catalysts.
1 ml = approx. 1.12 g

02194705 

Cell Culture Reagent
Used to reduce disulfide linkages in solubilizing proteins for gel electrophoresis. Also reduces excess oxidative polymerization of catalysts.
Density = 1.12 g/ml

02194834 

Molecular Biology Reagent
Purity: 98+%
Specially purified for molecular biology applications.

04806443 

Purity: >98%
Specially purified for use in solubilizing proteins for gel electrophoresis.

04806444 

Purity: >98%
Specially purified for use in solubilizing proteins for gel electrophoresis.

04806445 

Purity: >98%
Specially purified for use in solubilizing proteins for gel electrophoresis.

2-Mercaptoethanol 

M6250 

Application
BME 用于在聚丙烯酰胺凝胶电泳前还原蛋白质二硫键，通常以 5% 的浓度包含在用于 SDS-PAGE 的样本缓冲液中。裂解分子间（亚基之间）的二硫键，从而使蛋白质亚基在 SDS-PAGE 上各自分开。裂解分子内（亚基内）的二硫键从而使亚基完全变性，以便每个肽按照其链长迁移而不受二级结构的影响。
广泛用于延缓溶液中生物化合物的氧化。
包装
1, 2.5 L in glass bottle
10, 100, 250, 500 mL in glass bottle

M7154 

Application
BME 用于在聚丙烯酰胺凝胶电泳前还原蛋白质二硫键，通常以 5% 的浓度包含在用于 SDS-PAGE 的样本缓冲液中。裂解分子间（亚基之间）的二硫键，从而使蛋白质亚基在 SDS-PAGE 上各自分开。裂解分子内（亚基内）的二硫键从而使亚基完全变性，以便每个肽按照其链长迁移而不受二级结构的影响。
包装
25, 100 mL in glass bottle

M7522 

Application
BME 用于在聚丙烯酰胺凝胶电泳前还原蛋白质二硫键，通常以 5% 的浓度包含在用于 SDS-PAGE 的样本缓冲液中。裂解分子间（亚基之间）的二硫键，从而使蛋白质亚基在 SDS-PAGE 上各自分开。裂解分子内（亚基内）的二硫键从而使亚基完全变性，以便每个肽按照其链长迁移而不受二级结构的影响。
包装
100, 250, 500 mL in glass bottle

M3148 

Application
BME 用于在聚丙烯酰胺凝胶电泳前还原蛋白质二硫键，通常以 5% 的浓度包含在用于 SDS-PAGE 的样本缓冲液中。裂解分子间（亚基之间）的二硫键，从而使蛋白质亚基在 SDS-PAGE 上各自分开。裂解分子内（亚基内）的二硫键从而使亚基完全变性，以便每个肽按照其链长迁移而不受二级结构的影响。
还原剂
包装
25, 100, 250, 500 mL in glass bottle

568678 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.
Legal Information
Product of Arkema Inc.

516732 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.
Legal Information
Product of Arkema

M3701 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.
Charge transfer agent for the preparation of polyvinyl chloride. Synthon for the preparation of 1,3-oxathiolanes.

63689 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.
Other Notes
Isolation of RNA using guanidinium salts. Inclusion of a reductant enhances denaturation by breaking intramolecular protein disulfide bonds1

63700 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.

19-1335 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.
Suitability
for biological purposes

19-1330 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.

63690 

Application
BME is suitable for reducing protein disulfide bonds prior to polyacrylamide gel electrophoresis and is usually included in a sample buffer for SDS-PAGE at a concentration of 5%. Cleaving intermolecular (between subunits) disulfide bonds allows the subunits of a protein to separate independently on SDS-PAGE. Cleaving intramolecular (within subunit) disulfide bonds allows the subunits to become completely denatured so that each peptide migrates according to its chain length with no influence due to secondary structure.
Other Notes
A reducing agent in fluorescent reaction of o-phthaldialdehyde and amino acids in alkaline medium1,2,3; For the dissociation of proteins4,5