Date published: 2026-4-1

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Vmn1r120 Inhibitors

Vmn1r120, a member of the vomeronasal 1 receptor family, plays a crucial role in the detection and interpretation of pheromonal signals within the vomeronasal organ. Functionally, Vmn1r120 is involved in mediating cellular responses to environmental cues, orchestrating complex signaling events that influence social behaviors in response to chemical stimuli. The receptor is intricately associated with multiple signaling pathways, prominently the PI3K/Akt, MAPK/ERK, and JNK cascades, which serve as molecular conduits for transducing signals from pheromones and modulating cellular responses within sensory neurons.

The inhibition of Vmn1r120 involves the modulation of these critical signaling pathways. The inhibitors listed in the table exert their effects by disrupting key nodes within these cascades, thereby influencing downstream events that impact Vmn1r120 expression and function. For example, PI3K/Akt pathway inhibitors interfere with Vmn1r120 by perturbing downstream signaling events, causing alterations in its expression and function. Similarly, inhibitors of the MAPK/ERK and JNK cascades disrupt the intricate signaling dynamics orchestrated by Vmn1r120, leading to modifications in its activity. The underlying mechanisms of inhibition involve the perturbation of these pathways, influencing phosphorylation dynamics, protein-protein interactions, and downstream cellular responses associated with Vmn1r120. As a result, the receptor's role in decoding pheromone signals is intricately regulated by the modulation of these signaling pathways, providing valuable insights into the complex interplay between molecular events and sensory perception.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Wortmannin

19545-26-7sc-3505
sc-3505A
sc-3505B
1 mg
5 mg
20 mg
$67.00
$223.00
$425.00
97
(3)

Wortmannin is a potent PI3-kinase inhibitor, disrupting the PI3K/Akt pathway. Vmn1r120 is intricately connected to this pathway, and Wortmannin indirectly inhibits Vmn1r120 by perturbing downstream signaling events, leading to alterations in Vmn1r120 expression and function within the cellular context.

LY 294002

154447-36-6sc-201426
sc-201426A
5 mg
25 mg
$123.00
$400.00
148
(1)

LY294002 is a selective PI3-kinase inhibitor, perturbing the PI3K/Akt pathway. Vmn1r120 is associated with this pathway, and LY294002 indirectly inhibits Vmn1r120 by influencing downstream signaling cascades, causing modifications in Vmn1r120 expression and function within the cellular milieu.

PD 169316

152121-53-4sc-204168
sc-204168A
sc-204168B
sc-204168C
1 mg
5 mg
10 mg
25 mg
$88.00
$156.00
$281.00
$461.00
3
(1)

PD 169316 is a p38 MAPK inhibitor, perturbing MAPK signaling. Vmn1r120, being downstream in this pathway, is indirectly influenced by SB203580. The inhibition occurs through perturbation of p38 MAPK signaling, leading to modifications in Vmn1r120 expression and function within the cellular context.

PD 98059

167869-21-8sc-3532
sc-3532A
1 mg
5 mg
$40.00
$92.00
212
(2)

PD98059 is a MEK inhibitor, disrupting the MAPK pathway. Vmn1r120 is positioned downstream in this pathway, and its activity is indirectly influenced by PD98059. The inhibition occurs through perturbation of the MAPK signaling cascade, leading to modifications in Vmn1r120 expression and function within the cellular milieu.

SP600125

129-56-6sc-200635
sc-200635A
10 mg
50 mg
$40.00
$150.00
257
(3)

SP600125 is a JNK inhibitor, affecting the JNK signaling pathway. Vmn1r120 is indirectly influenced by SP600125, positioned downstream in the JNK pathway. The inhibition occurs through perturbation of the JNK cascade, leading to modifications in Vmn1r120 expression and function within the cellular context.

Calyculin A

101932-71-2sc-24000
sc-24000A
10 µg
100 µg
$163.00
$800.00
59
(3)

Calyculin A is a potent protein phosphatase inhibitor, disrupting cellular phosphorylation dynamics. Vmn1r120 activity is modulated by phosphorylation events, and Calyculin A indirectly inhibits Vmn1r120 by influencing protein phosphatase activity, resulting in altered phosphorylation patterns that impact Vmn1r120 function within the cell.