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IPTG 1 g

Price:
$23.00
SKU:
GB-I2481C
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Isopropyl-beta-D-thiogalactoside (IPTG)

(isopropyl-β-D-thiogalactopyranoside)

Purity > 99.5 %

Molecular Biology Grade, synthetically made and not from animal origin

  CAS Number:
  367-93-1
  Chemical Formula:   C9H18O5S
  Molecular Weight:   238.3 g/mol

 

IPTG, dioxane free is an analog of lactose that inactivates the lac repressor. The lac repressor is a DNA binding protein that inhibits gene expression therefore you can think of IPTG operating by inhibiting an inhibitor thus allowing expression to occur. IPTG serves as a mimic of the naturally occurring allolactose that is an inducer of the lac operon.  This is commonly referred to as IPTG induction and used in protein expression. 

IPTG cannot be hydrolyzed or broken down by the E. coli therefore the concentration remains constant during cell replication. IPTG is often used at a final concentration ranging from 0.5-1.0 mM. X-Gal is often used with IPTG since it provides an easy visual method to monitor whether protein expression has occurred. X-Gal as the name implies contains a galactose group that once metabolized causes a bright blue color change.

IPTG Certification of Analysis

  Test   Results
  Appearance   White crystalline powder
  Solution (1% in Water)   Colorless, clear
  IR   Corresponds to Reference
  Melting Point   111.4°-113.2 °C
  Assay (IC)   99.6 % (HPLC)
  Dioxane Content   < 1 ppm (GC)

 

Stock Solution Preparation of 1 M IPTG

  1. Dissolve 2.38 g of IPTG in 8 mL of distilled H2O.
  2. Bring to a final volume of 10 mL with molecular biology grade H2O.
  3. Filter sterilize with a 0.22 μ syringe filter.
  4. Store in 1mL aliquots at -20 °C.

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Celebrity Endorsements

Manithody, C. et. al. Identification of a Basic Region on Tissue Factor that Interacts with the First Epidermal Growth Factor-like Domain of Factor X. Biochemistry, 2007, 46 (11), 3193–3199.

Aktas, et. al. Proper Positioning of the Nicotinamide Ring Is Crucial for the Ascaris suum Malic Enzyme Reaction. Biochemistry, 2008, 47 (8), 2539–2546.

Derewenda, Z. S. (2004) The use of recombinant methods and molecular engineering in protein crystallization. Methods. Vol 34. 354–363.

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