Date published: 2025-11-1

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MrgB13 Inhibitors

The chemical class of MrgB13 inhibitors comprises a diverse group of compounds that can interfere with the signaling and trafficking of the MAS-related GPR, member B13 receptor. Inhibitors in this class operate through various mechanisms affecting receptor function. Some function by impeding the internalization or recycling of the receptor, such as Substance P, which can lead to receptor desensitization, Chloroquine, which affects intracellular vesicle pH and receptor recycling, and Dynasore, which disrupts dynamin-mediated endocytosis. Other compounds like ML-141 and SecinH3 interfere with GTPases that regulate cytoskeletal dynamics and membrane trafficking, which are crucial for receptor signaling. Brefeldin A and Monensin can disrupt cellular organelles and ion gradients, respectively, which are vital for proper receptor localization and function.

Additional inhibitors affect the cytoskeleton directly, such as Cytochalasin D and Latrunculin A, which inhibit actin polymerization, and Nocodazole, which disrupts microtubules, all leading to potential alterations in MrgB13 receptor distribution and downstream signaling. Lastly, compounds like Gö6976 and Wiskostatin modulate signaling pathways, with Gö6976 targeting protein kinase C, thereby influencing MrgB13 indirectly, and Wiskostatin affecting the N-WASP-Arp2/3 complex involved in actin remodeling, which can impact receptor trafficking. These inhibitors can alter the signaling of MrgB13 by modifying the cellular environment and machinery that control receptor activity and expression.

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Items 1 to 10 of 12 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Substance P

33507-63-0sc-201169
1 mg
$55.00
(1)

Substance P is a neuropeptide that acts as an agonist of the MrgB13 receptor, which can lead to receptor desensitization and internalization thus reducing MrgB13 signaling.

Chloroquine

54-05-7sc-507304
250 mg
$68.00
2
(0)

Chloroquine is known to alkalinize intracellular vesicles and could impair the recycling of internalized MrgB13 receptors back to the cell surface, thereby reducing receptor availability for activation.

Dynamin Inhibitor I, Dynasore

304448-55-3sc-202592
10 mg
$87.00
44
(2)

Dynasore is a GTPase inhibitor that can disrupt dynamin-dependent endocytosis, potentially affecting the internalization and recycling of MrgB13, which can alter receptor signaling.

ML 141

71203-35-5sc-362768
sc-362768A
5 mg
25 mg
$134.00
$502.00
7
(1)

ML-141 is a Cdc42 GTPase inhibitor which may interfere with actin cytoskeleton remodeling, thus potentially influencing MrgB13 receptor trafficking and signaling.

SecinH3

853625-60-2sc-203260
5 mg
$273.00
6
(1)

SecinH3 inhibits cytohesin exchange factors, which can impact G-protein-coupled receptor signaling, potentially affecting MrgB13 receptor activity.

Brefeldin A

20350-15-6sc-200861C
sc-200861
sc-200861A
sc-200861B
1 mg
5 mg
25 mg
100 mg
$30.00
$52.00
$122.00
$367.00
25
(3)

Brefeldin A disrupts Golgi apparatus function and can impede the trafficking of membrane proteins like MrgB13, possibly leading to a decrease in receptor signaling.

Monensin A

17090-79-8sc-362032
sc-362032A
5 mg
25 mg
$152.00
$515.00
(1)

Monensin is an ionophore that disrupts transmembrane ion gradients and could affect the trafficking and signaling of MrgB13 as a result of altered cellular homeostasis.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$145.00
$442.00
64
(4)

Cytochalasin D is a potent inhibitor of actin polymerization which may impede the proper trafficking and function of MrgB13 by disrupting the cytoskeleton.

Gö 6976

136194-77-9sc-221684
500 µg
$223.00
8
(1)

Gö6976 is a protein kinase C inhibitor that can modulate signal transduction pathways, potentially influencing MrgB13 receptor signaling indirectly.

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
$260.00
$799.00
36
(2)

Latrunculin A binds to actin monomers and inhibits polymerization, which could affect MrgB13 receptor trafficking and signaling due to changes in the cytoskeletal architecture.