DTT, DL-Dithiothreitol, (RT) (1g)

SKU:
43819-1G
  • $60.10

    • Description

    DL-Dithiothreitol

    ≥99.0% (RT)

    Synonym: threo-1,4-Dimercapto-2,3-butanediol, Cleland’s reagent, DTT

    • CAS Number 3483-12-3

    • Linear Formula HSCH2CH(OH)CH(OH)CH2SH

    • Molecular Weight 154.25

    •  Beilstein Registry Number 1719757

    •  EC Number 222-468-7

    •  MDL number MFCD00004877

    Properties

    assay ≥99.0% (RT)
    impurities ≤0.3% 4,5-dihydroxy-1,2-dithiane
    mp 41-44 °C(lit.)
     - 42-43 °C
    solubility H2O: 50 mg/mL, clear, colorless
    -  H2O: freely soluble
    -  acetone: freely soluble
    -  chloroform: freely soluble
    -  diethyl ether: freely soluble
    -  ethanol: freely soluble
    -  ethyl acetate: freely soluble
    anion traces sulfate (SO42-): ≤50 mg/kg
    cation traces Ca: ≤10 mg/kg
    -  Cd: ≤5 mg/kg
    -  Co: ≤5 mg/kg
    -  Cr: ≤5 mg/kg
    -  Cu: ≤5 mg/kg
    -  Fe: ≤5 mg/kg
    -  K: ≤50 mg/kg
    -  Mg: ≤5 mg/kg
    -  Mn: ≤5 mg/kg
    -  Na: ≤250 mg/kg
    -  Ni: ≤5 mg/kg
    -  Pb: ≤5 mg/kg
    -  Zn: ≤5 mg/kg
    storage temp. 2-8°C

    Description

    Application

    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. 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. Typically, a seven fold lower concentration of DTT (100 mM) is needed than is used for 2-mercaptoethanol (5% v/v, 700 mM).

    DL-Dithiothreitol is a pivotal component used in the preparation of buffer which in turn is utilized in the platelet cytosol preparation. It is also important in isolation of RNA by using guanidinium salts and homogenisation of tissue and cells

    Biochem/physiol Actions

    DL-Dithiothreitol denatures proteins by reducing the disulphide bonds and reducing them to SH groups. It also prevents intramolecular and intermolecular disulfide bond formation between cysteine residues of proteins.