2-Mercaptoethanol (BME) ยี่ห้อ Sigma

PROPERTIES

grade

for molecular biology

Quality Level

200

vapor density

2.69 (vs air)

vapor pressure

1 mmHg ( 20 °C)

product line

BioUltra

Assay

≥99.0% (GC)

form

liquid

expl. lim.

18 %

concentration

14.3 M (pure liquid)

technique(s)

RNA extraction: suitable

protein extraction: suitable

impurities

DNases, none detected

RNases, none detected

insoluble matter, passes filter test

phosphatases, none detected

proteases, none detected

refractive index

n20/D 1.500 (lit.)

n20/D 1.501

pH

4.5-6 (20 °C, 500 g/L)

bp

157 °C (lit.)

solubility

H₂O: 0.5 M at 20 °C, clear, colorless

density

1.114 g/mL at 25 °C (lit.)

cation traces

Al: ≤0.5 mg/kg

Ba: ≤0.1 mg/kg

Bi: ≤0.1 mg/kg

Ca: ≤0.5 mg/kg

Cd: ≤0.05 mg/kg

Co: ≤0.02 mg/kg

Cr: ≤0.02 mg/kg

Cu: ≤0.02 mg/kg

Fe: ≤0.1 mg/kg

K: ≤0.5 mg/kg

Li: ≤0.1 mg/kg

Mg: ≤0.1 mg/kg

Mn: ≤0.02 mg/kg

Mo: ≤0.1 mg/kg

Na: ≤1 mg/kg

Ni: ≤0.05 mg/kg

Pb: ≤0.1 mg/kg

Sr: ≤0.1 mg/kg

Zn: ≤0.1 mg/kg

SMILES string

OCCS

λ

0.5 M in H₂O

UV absorption

λ: 260 nm A_max: 1.5

λ: 280 nm A_max: 0.3

storage temp.

2-8°C

InChI

1S/C2H6OS/c3-1-2-4/h3-4H,1-2H2

InChI key

DGVVWUTYPXICAM-UHFFFAOYSA-N

DESCRIPTION

Application

2-Mercaptoethanol has been used

·       in the protein extraction buffer prepared for leaf samples.[1]

·       as a supplement in cell culture media.[2]

·       in the procedure of RNA extraction.[3]

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 bonds[4]