Fatty Acid-Binding Protein (FABP) Cannabinoid Research

Fatty Acid-Binding Protein (FABP) Research Dashboard


Primary Studies


Related Studies


Total Studies

Clinical Studies


Clinical Meta-analyses


Double-blind Clinical Trials


Clinical Trials

Pre-Clinical Studies




Animal Studies


Laboratory Studies

What am I missing as a non-subscriber?

To see a full dashboard with study details and filtering, go to our DEMO page.

As a subscriber, you will be able to access dashboard insights including chemotype overviews and dosing summaries for medical conditions and organ system and receptor breakdowns for cannabinoid and terpene searches. Study lists present important guidance including dosing and chemotype information with the ability to drill down to the published material. And all outputs are fully filterable, to help find just the information you need. Stay up-to-date with the science of cannabis and the endocannabinoid system with CannaKeys.

CannaKeys has 101 studies associated with Fatty Acid-Binding Protein (FABP).

Here is a small sampling of Fatty Acid-Binding Protein (FABP) studies by title:

Components of the Fatty Acid-Binding Protein (FABP) Research Dashboard

  • Top medical conditions associated with Fatty Acid-Binding Protein (FABP)
  • Proven effects in clinical trials for Fatty Acid-Binding Protein (FABP)
  • Receptors associated with Fatty Acid-Binding Protein (FABP)
  • Individual study details for Fatty Acid-Binding Protein (FABP)

Ready to become a subscriber? Go to our PRICING page.

Select New Cannabinoid

Filter Cannabinoid

Members can filter by the following criteria:

  • Study Type
  • Organ Systems
  • Terpenes
  • Receptors
  • Ligands
  • Study Result
  • Year of Publication

Overview - Fatty Acid-Binding Protein (FABP)

Description of Fatty Acid-Binding Protein (FABP)

Fatty acid-binding proteins (FABPs), a family of proteins sometimes referred to as lipid chaperones, are intracellular proteins that facilitate the transport of AEA to different parts of the human body. Guided by the homeostatic mechanisms on an as-needed basis FABPs transport AEA to a cellular organelle the endoplasmic reticulum (a transport system) where the enzyme FAAH1 is found. Once in proximity, FAAH1 begins to function as a catalyst (to cause the reaction) for AEA's hydrolyses (break down). (M. Elmes et al., 2015)

When cannabinoids such as THC and CBD are present and bind to FABPs instead of AEA, they inhibit AEA's breakdown and, as such, increase its bioavailability. (D. Deutsch, 2016)

To date, 10 different types of FABPs have been identified in humans, each found in specific tissues such as the brain, kidney, or liver for example. Of these three known members, i.e., FABP3, FABP5, and FABP7 bind with THC and CBD. (M. Elmes et al., 2015)

Other Names:

Fatty Acid-Binding Protein

Fatty Acid-Binding Protein (FABP) Properties and Effects

Only Members can view Properties and Effects information. See DEMO page.

Fatty Acid-Binding Protein (FABP) Receptor Binding

Only Members can view Receptor Binding information. See DEMO page.

Information on this site is provided for informational purposes only and is not meant to substitute for the advice provided by your own licensed physician or other medical professional. You should not use the information contained herein for diagnosing or treating a health problem or disease. If using a product, you should read carefully all product packaging. If you have or suspect that you have a medical problem, promptly contact your health care provider.

Information on this site is based on scientific studies (human, animal, or in vitro), clinical experience, or traditional usage as cited in each article. The results reported may not necessarily occur in all individuals. For many of the conditions discussed, treatment with prescription or over-the-counter medication is also available. Consult your physician, nutritionally oriented health care practitioner, and/or pharmacist for any health problem and before using any supplements or before making any changes in prescribed medications.