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ECO Brij® L23

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Brij® L23, Brij 35, C12E23, Polyoxyethylene (23) lauryl ether
CAS Number:
MDL number:



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greener alternative product characteristics

Use of Renewable Feedstocks
Design for Degradation
Learn more about the Principles of Green Chemistry.


≤3.0% water


91 μM

acid number

≤1.0 mg KOH/g

hydroxyl value

40‑60 mg KOH/g



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General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Green Chemistry. This product is a biobased surfactant and is aligned with the 7th principle of Green Chemistry "Use of Renewable Feedstocks" and the 10th principle "Design for Degradation.


Brij®L23 is a detergent used for measuring the concentration of carbon black in lung tissues. It has also been used for selective and rapid solubilization of microbial membrane aldehyde dehydrogenase. Additionally, the product has also been used for assessing whether acrolein could lead to pro-enzyme activation by using gelatin zymography.

Biochem/physiol Actions

Brij® L23 also referred to as Brij 35 or Polyoxyethylene (23) lauryl ether is a non-ionic detergent that lowers the non-specific protein adsorption and reduces electroosmotic pumping drastically. This allows the pH to be varied without adversely affecting the flow rate. It also used as a nonionic surfactant that decreases the absorbance of the blank, inhibits turbidity as well as provides linearity.

Features and Benefits

  • 100 % Renewable
  • 100 % Bio-based
  • Certified to the USDA BioPreferred Program
  • Lower carbon footprint than petrochemical-based versions

Physical properties

The ECO Brij series of ethoxylated fatty alcohols are non-ionic surfactants manufactured using renewable sources. ECO Brij L23 is a mixture of tricosaethylene glycol alkyl ethers, primarily dodecyl (C12) ether. The alkyl ether profile of ECO Brij L23 may differ lot-to-lot due to natural variability in the lipid starting material (palm oil).

Other Notes

Non-ionic polyoxyethylene ether. Used for selective and rapid solubilization of microbial membrane aldehyde dehydrogenase.

Legal Information

Brij is a registered trademark of Croda International PLC

Storage Class Code

11 - Combustible Solids



Flash Point(F)

300.2 °F - closed cup

Flash Point(C)

> 149 °C - closed cup

Certificates of Analysis (COA)

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B T Dumas et al.
Clinica chimica acta; international journal of clinical chemistry, 258(1), 21-30 (1997-02-03)
A rapid and reliable method for measuring serum albumin employing bromcresol green is described. The addition of albumin to a solution of bromcresol green in a 0.075 M succinate buffer pH 4.20 results in an increase in absorbance at 628
Cheol-Hong Lim et al.
Environmental health and toxicology, 28, e2013014-e2013014 (2013-12-05)
This study was conducted to determine whether nano-sized carbon black exposure results in greater damage in high fat diet-induced overweight rats than normal weight ones and to identify the possible causes of any differences. Two groups of Sprague-Dawley rats allocated
J K Towns et al.
Analytical chemistry, 63(11), 1126-1132 (1991-06-01)
Capillary zone electrophoretic separations of proteins have been achieved by using nonionic surfactant coated capillaries. Capillaries were prepared by derivatization of the silica surface with octadecylsilane followed by the deposition of a layer of nonionic surfactant from an aqueous solution
Hitesh S Deshmukh et al.
American journal of respiratory cell and molecular biology, 38(4), 446-454 (2007-11-17)
Chronic obstructive pulmonary disease (COPD), a global public health problem, is characterized by progressive difficulty in breathing, with increased mucin production, especially in the small airways. Acrolein, a constituent of cigarette smoke and an endogenous mediator of oxidative stress, increases
R Hommel et al.
Journal of basic microbiology, 30(4), 297-300 (1990-01-01)
An improved solubilization procedure for the membrane-bound quinoprotein aldehyde dehydrogenase from Acetobacter rancens CCM 1774 was established. After the first solubilization of membrane enzymes by Brij 35 which provided important extraction of membrane proteins other than aldehyde dehydrogenase, the application

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