Vmn1r122 Inhibitors
Vmn1r122, a member of the vomeronasal 1 receptor family, holds a pivotal role in the sensory perception of pheromones within the vomeronasal organ. Functionally, Vmn1r122 contributes to the interpretation of chemical cues, orchestrating complex cellular responses to environmental stimuli and influencing social behaviors. The receptor is intricately linked to several signaling pathways, prominently the PI3K/Akt, MAPK/ERK, and JNK cascades, through which it transduces signals from pheromones and mediates molecular events within sensory neurons.
The inhibition of Vmn1r122 unfolds through the modulation of these crucial signaling pathways. The inhibitors listed in the table exert their effects by disrupting key nodes within these cascades, influencing downstream events that impact Vmn1r122 expression and function. For instance, PI3K/Akt pathway inhibitors interfere with Vmn1r122 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 Vmn1r122, 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 Vmn1r122. 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 Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Wortmannin | 19545-26-7 | sc-3505 sc-3505A sc-3505B | 1 mg 5 mg 20 mg | $67.00 $223.00 $425.00 | 97 | |
Wortmannin is a potent PI3-kinase inhibitor, disrupting the PI3K/Akt pathway. Vmn1r122 is intricately connected to this pathway, and Wortmannin indirectly inhibits Vmn1r122 by perturbing downstream signaling events, leading to alterations in Vmn1r122 expression and function within the cellular context. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $123.00 $400.00 | 148 | |
LY294002 is a selective PI3-kinase inhibitor, perturbing the PI3K/Akt pathway. Vmn1r122 is associated with this pathway, and LY294002 indirectly inhibits Vmn1r122 by influencing downstream signaling cascades, causing modifications in Vmn1r122 expression and function within the cellular milieu. | ||||||
PD 169316 | 152121-53-4 | sc-204168 sc-204168A sc-204168B sc-204168C | 1 mg 5 mg 10 mg 25 mg | $88.00 $156.00 $281.00 $461.00 | 3 | |
PD 169316 is a p38 MAPK inhibitor, perturbing MAPK signaling. Vmn1r122, being downstream in this pathway, is indirectly influenced by SB203580. The inhibition occurs through perturbation of p38 MAPK signaling, leading to modifications in Vmn1r122 expression and function within the cellular context. | ||||||
PD 98059 | 167869-21-8 | sc-3532 sc-3532A | 1 mg 5 mg | $40.00 $92.00 | 212 | |
PD98059 is a MEK inhibitor, disrupting the MAPK pathway. Vmn1r122 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 Vmn1r122 expression and function within the cellular milieu. | ||||||
SP600125 | 129-56-6 | sc-200635 sc-200635A | 10 mg 50 mg | $40.00 $150.00 | 257 | |
SP600125 is a JNK inhibitor, affecting the JNK signaling pathway. Vmn1r122 is indirectly influenced by SP600125, positioned downstream in the JNK pathway. The inhibition occurs through perturbation of the JNK cascade, leading to modifications in Vmn1r122 expression and function within the cellular context. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $163.00 $800.00 | 59 | |
Calyculin A is a potent protein phosphatase inhibitor, disrupting cellular phosphorylation dynamics. Vmn1r122 activity is modulated by phosphorylation events, and Calyculin A indirectly inhibits Vmn1r122 by influencing protein phosphatase activity, resulting in altered phosphorylation patterns that impact Vmn1r122 function within the cell. | ||||||