The chemical class identified as v-SNARE Vti1a Activators encompasses a range of compounds that indirectly modulate the activity of the v-SNARE Vti1a protein, a crucial component in the vesicular transport system within cells. Vti1a plays a pivotal role in the fusion of transport vesicles with their target membranes, a process fundamental to various cellular functions including neurotransmitter release and intracellular material transport. The activators in this class do not directly bind or interact with Vti1a. Instead, they influence the protein's activity by modulating the cellular and biochemical pathways that govern vesicle fusion and trafficking. This indirect mode of action is achieved through the alteration of intracellular signaling cascades, ion concentrations, and phosphorylation states, which in turn can impact the environment in which Vti1a operates.
For example, compounds such as Calcium Chloride and Nifedipine influence calcium signaling and homeostasis, which are integral to the vesicle fusion process involving Vti1a. By altering calcium dynamics within the cell, these compounds can indirectly affect the conditions necessary for Vti1a's optimal functioning. Similarly, agents like Phorbol 12-myristate 13-acetate (PMA) and Forskolin, which activate protein kinase C and elevate cAMP levels respectively, can modify the phosphorylation state and activity of proteins involved in vesicular trafficking, thereby potentially influencing Vti1a-mediated processes. Additionally, the class includes GTP analogs like GTPγS that impact G-protein signaling pathways, and phosphatase inhibitors such as Okadaic Acid that alter protein phosphorylation states, both of which are crucial for the regulation of vesicle dynamics. Other members of this class, like BAPTA-AM, Tetrodotoxin, ω-Conotoxin GVIA, ω-Agatoxin IVA, Ryanodine, and Thapsigargin, function through various mechanisms to modulate intracellular calcium levels or neuronal activity, thereby creating conditions that can indirectly affect Vti1a's role in vesicular transport. Collectively, these compounds represent a diverse array of chemical entities that, through their influence on cellular signaling and ion homeostasis, have the capacity to modulate the functional landscape in which Vti1a operates, thus indirectly impacting its activity in the complex process of vesicular transport and membrane fusion.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $66.00 $262.00 | 1 | |
Influences calcium signaling, which is integral to vesicle fusion processes involving Vti1a. | ||||||
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $41.00 $132.00 $214.00 $500.00 $948.00 | 119 | |
Activates protein kinase C, which can modulate vesicle trafficking and fusion, processes involving Vti1a. | ||||||
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $78.00 $153.00 $740.00 $1413.00 $2091.00 | 73 | |
Elevates cAMP, potentially affecting pathways that influence Vti1a's role in vesicular transport. | ||||||
Guanosine 5′-O-(3-thiotriphosphate) tetralithium salt | 94825-44-2 | sc-202639 | 10 mg | $465.00 | ||
A non-hydrolyzable GTP analog, influencing G-protein signaling, potentially affecting Vti1a activity. | ||||||
BAPTA/AM | 126150-97-8 | sc-202488 sc-202488A | 25 mg 100 mg | $138.00 $458.00 | 61 | |
A calcium chelator, affecting calcium-dependent processes involving Vti1a. | ||||||
Nifedipine | 21829-25-4 | sc-3589 sc-3589A | 1 g 5 g | $59.00 $173.00 | 15 | |
As a calcium channel blocker, it can influence calcium influx, indirectly affecting Vti1a's function. | ||||||
ω-Agatoxin IVA | 145017-83-0 | sc-302015 | 100 µg | $463.00 | ||
Blocks P/Q-type calcium channels, potentially influencing Vti1a's function in vesicular transport. | ||||||
Ryanodine | 15662-33-6 | sc-201523 sc-201523A | 1 mg 5 mg | $223.00 $799.00 | 19 | |
Affects calcium release from sarcoplasmic/endoplasmic reticulum, potentially influencing Vti1a. | ||||||