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AB114426

Recombinant Human FAAH1 protein

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Recombinant Human FAAH1 protein is a Human Fragment protein, in the 480 to 579 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

FAAH1, FAAH, Fatty-acid amide hydrolase 1, Anandamide amidohydrolase 1, Fatty acid ester hydrolase, Oleamide hydrolase 1

1 Images
SDS-PAGE - Recombinant Human FAAH1 protein (AB114426)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human FAAH1 protein (AB114426)

ab114426 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

WB, ELISA, SDS-PAGE

applications

Biologically active

No

Accession

O00519

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"DLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS","proteinLength":"Fragment","predictedMolecularWeight":"36.63 kDa","actualMolecularWeight":null,"aminoAcidEnd":579,"aminoAcidStart":480,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"O00519","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Fatty acid amide hydrolase 1 (FAAH1) often referred to simply as FAAH is an enzyme that plays a critical role in the degradation of fatty acid amides such as anandamide in the body. This enzyme weighing approximately 63 kDa is a part of the amidase signature family and is characterized by its amidase hydrolase activity. FAAH1 is predominantly expressed in the nervous system liver and gastrointestinal tract where it hydrolyses amide bonds facilitating the termination of signaling pathways initiated by neurotransmitter-like fatty acid amides.
Biological function summary

FAAH1 is essential for maintaining homeostasis by modulating levels of bioactive lipids. It exerts control over endocannabinoid signaling by breaking down anandamide a lipid derivative functioning as a neurotransmitter. FAAH1 does not act as part of a larger protein complex. Instead it operates alone to regulate the duration and intensity of signaling rather than relying on direct interactions within a complex. The enzyme's function impacts the neurochemical milieu in tissues where it is actively expressed thereby affecting mood pain sensation and more.

Pathways

FAAH1 has a significant role in the endocannabinoid signaling pathway and fatty acid metabolism. Within these pathways it modulates signaling by hydrolysing bioactive amides like anandamide influencing overall lipid signaling. FAAH1 activities intersect with several other proteins such as cannabinoid receptors which bind the substrates that FAAH1 eventually degrades. These interactions are vital in controlling signal transduction processes that regulate physiological responses including stress and analgesia.

FAAH1 has been implicated in conditions like chronic pain and anxiety disorders. Altered FAAH1 function or expression can lead to dysregulation of endocannabinoid signaling contributing to the pathophysiology of these conditions. The enzyme's modulation of anandamide levels connects it to proteins such as CB1 and CB2 cannabinoid receptors which mediate the effects of endocannabinoids in neurological and psychiatric disorders. Research into FAAH1 inhibitors as therapeutic agents highlights its importance in potential treatments for managing pain and anxiety.
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Specifications

Form

Liquid

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General info

Function

Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed : 17015445, PubMed : 19926788, PubMed : 9122178). Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (PubMed : 17015445, PubMed : 9122178). It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed : 21049984). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).

Sequence similarities

Belongs to the amidase family.

Subcellular localisation

Cytoskeleton

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Product protocols

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Target data

Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed : 17015445, PubMed : 19926788, PubMed : 9122178). Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (PubMed : 17015445, PubMed : 9122178). It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed : 21049984). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
See full target information FAAH
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