Date published: 2026-5-2

1-800-457-3801

SCBT Portrait Logo
Seach Input

EAAT1 Inhibitors

The chemical class of EAAT1 inhibitors encompasses a diverse array of compounds designed to modulate the activity of excitatory amino acid transporter 1 (EAAT1), shedding light on its intricate roles in glutamate homeostasis. These inhibitors can be broadly categorized into direct and indirect modulators, offering unique insights into the regulatory mechanisms governing EAAT1 function. Direct inhibitors such as L-β-threo-Ethylaspartate, TFB-TBOA, UCPH-101, and diTBOA specifically target the transport function of EAAT1, disrupting the clearance of extracellular glutamate. By inhibiting glutamate uptake, these inhibitors provide precise tools for studying the physiological consequences of altered EAAT1 activity, unraveling the intricacies of glutamate homeostasis and its impact on neuroexcitability. Indirect modulators like (S)-MCPG, Dihydrokainate, Evans Blue, and Benzylserine influence EAAT1 through alternative mechanisms. (S)-MCPG, a metabotropic glutamate receptor antagonist, indirectly modulates EAAT1 by blocking glutamate receptors, highlighting the interplay between metabotropic glutamate receptors and EAAT1-mediated glutamate transport. Dihydrokainate and Benzylserine competitively inhibit glutamate transport by mimicking the structure of glutamate and L-serine, respectively. Evans Blue sequesters extracellular glutamate, indirectly modulating EAAT1 activity. Additionally, compounds like WAY-855, DL-Threo-β-Benzyloxyaspartate, MS-153, and L-α-Aminoadipic Acid provide alternative avenues for studying EAAT1. WAY-855 directly modulates EAAT1 activity by interfering with glutamate transport, while DL-Threo-β-Benzyloxyaspartate competes with endogenous substrates for binding to EAAT1. MS-153 and L-α-Aminoadipic Acid directly inhibit glutamate transport, offering additional tools for investigating the role of EAAT1 in maintaining glutamate homeostasis. In conclusion, this chemical class of EAAT1 inhibitors offers a comprehensive toolkit for researchers seeking to unravel the complex roles of EAAT1 in regulating glutamate homeostasis. The diversity in mechanisms, ranging from direct catalytic inhibition to indirect modulation through metabotropic glutamate receptors and substrate competition, provides a nuanced understanding of the regulatory networks governing EAAT1 function in diverse cellular contexts.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

UCPH 101

1118460-77-7sc-361391
sc-361391A
10 mg
50 mg
$388.00
$908.00
3
(1)

UCPH 101 is a selective modulator of excitatory amino acid transporters (EAAT1), characterized by its unique structural features that facilitate specific hydrogen bonding and electrostatic interactions with the transporter. Its distinct molecular architecture promotes conformational flexibility, enhancing the efficiency of substrate translocation. Additionally, UCPH 101 influences the allosteric regulation of the transporter, potentially altering the dynamics of glutamate uptake and release, thereby affecting synaptic signaling pathways.

L-(-)-threo-3-Hydroxyaspartic acid

7298-99-9sc-204033
10 mg
$218.00
1
(0)

L-(-)-threo-3-Hydroxyaspartic acid acts as a potent modulator of excitatory amino acid transporters (EAAT1), exhibiting unique stereochemistry that enhances its binding affinity. Its hydroxyl group facilitates specific interactions with the transporter, promoting optimal substrate recognition. The compound's kinetic profile reveals rapid association and dissociation rates, allowing for efficient transport dynamics. Furthermore, it may influence the conformational states of EAAT1, impacting glutamate homeostasis.

(S)-MCPG

150145-89-4sc-202329
sc-202329A
5 mg
25 mg
$146.00
$964.00
(0)

(S)-MCPG, a selective group I/II metabotropic glutamate receptor antagonist, indirectly influences EAAT1 by blocking glutamate receptors. By preventing excessive glutamate receptor activation, (S)-MCPG modulates glutamate levels, indirectly impacting EAAT1 activity.

L-trans-Pyrrolidine-2,4-dicarboxylic acid

64769-66-0sc-200477
sc-200477A
5 mg
25 mg
$66.00
$419.00
8
(1)

L-trans-Pyrrolidine-2,4-dicarboxylic acid serves as a selective inhibitor of excitatory amino acid transporters (EAAT1), characterized by its unique cyclic structure that enhances its interaction with the transporter. The presence of two carboxyl groups allows for multiple hydrogen bonding opportunities, stabilizing the binding complex. Its distinct reaction kinetics demonstrate a slower dissociation rate, which may prolong its effects on glutamate transport and influence neuronal signaling pathways.

Dihydrokainic acid

52497-36-6sc-200442B
sc-200442
sc-200442A
1 mg
10 mg
50 mg
$110.00
$302.00
$914.00
3
(0)

Dihydrokainate, a non-transportable substrate analog, indirectly influences EAAT1 by competitively inhibiting glutamate transport. By mimicking the structure of glutamate, Dihydrokainate competes for binding to EAAT1, preventing the transport of endogenous substrates.

Evans Blue

314-13-6sc-203736B
sc-203736
sc-203736A
1 g
10 g
50 g
$47.00
$69.00
$265.00
15
(1)

Evans Blue, a blood-brain barrier impermeant dye, indirectly influences EAAT1 by binding to extracellular glutamate. By sequestering glutamate in the extracellular space, Evans Blue modulates glutamate levels, indirectly impacting EAAT1 activity. This indirect inhibition offers insights into the consequences of altered glutamate clearance by EAAT1, providing a tool for studying the regulatory mechanisms governing glutamate homeostasis and its impact on neuroexcitability.

L-α-Aminoadipic acid

1118-90-7sc-202200
sc-202200A
50 mg
250 mg
$19.00
$32.00
(0)

L-α-Aminoadipic Acid, a non-transportable substrate analog, indirectly influences EAAT1 by competitively inhibiting glutamate transport. By mimicking the structure of glutamate, L-α-Aminoadipic Acid competes for binding to EAAT1, preventing the transport of endogenous substrates.

(S)-(+)-N-Benzylserine

17136-45-7sc-220044
1 g
$205.00
1
(0)

Benzylserine, an L-serine analog, indirectly influences EAAT1 by competitively inhibiting glutamate transport. By mimicking the structure of the endogenous substrate L-serine, Benzylserine competes for binding to EAAT1, preventing the transport of glutamate.