Spa2 Activators encompass a spectrum of chemical compounds that facilitate the enhancement of Spa2's functional activity through various signaling pathways and cellular processes. Forskolin, by escalating cAMP concentrations, indirectly fortifies Spa2's role in cell signaling by activating PKA, which may phosphorylate substrates within pathways Spa2 influences, thereby amplifying its function. PMA, as an activator of PKC, fosters alterations in cytoskeletal organization-a domain where Spa2 is presumed to contribute-thus indirectly bolstering its activity in cellular architecture modulation. S1P, through its receptor-mediated signaling, prompts actin cytoskeleton reconfiguration, which could consequently augment Spa2's operational efficacy in related processes. Ionomycin, by raising intracellular calcium levels, potentially primes calcium-dependent pathways that Spa2 could be part of, leading to its activation. EGCG, through kinase inhibition, and LY294002, a PI3K pathway antagonist, might channel signaling towards Spa2-engaged routes, indirectly amplifying its function, while U0126 could shift the balance of MAPK signaling to favor Spa2's pathway engagement.
Additionally, Thapsigargin's interference with calcium homeostasis could create a conducive environment for Spa2 activation due to elevated cytosolic calcium, presumed to be a cofactor in processes where Spa2 is implicated. Dibutyryl-cAMP, mimicking endogenous cAMP, likely potentiates Spa2 activity by engaging PKA-mediated signaling events. Staurosporine, with its broad kinase inhibition spectrum, might inadvertently activate Spa2 pathways by lifting the inhibition exerted on them, hence facilitating Spa2's role in signaling. Calyculin A, by inhibiting protein phosphatases, is theorized to enhance the phosphorylation status of proteins within Spa2's orbit, indirectly bolstering its activity. Jasplakinolide's stabilization of actin filaments could provide the structural integrity necessary for the cellular functions Spa2 regulates, hence serving as an indirect activator. Collectively, these Spa2 Activators, by targeting specific cellular pathways and processes, serve to enhance the functional activity of Spa2 without necessitating the upregulation of its expression or direct activation.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $76.00 $150.00 $725.00 $1385.00 $2050.00 | 73 | |
Forskolin activates adenylate cyclase, increasing cAMP levels in cells. Elevated cAMP can activate PKA, which may phosphorylate proteins involved in the cellular processes that Spa2 modulates, leading to its functional enhancement in signal transduction and cell polarization. | ||||||
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $40.00 $129.00 $210.00 $490.00 $929.00 | 119 | |
PMA is a potent activator of protein kinase C (PKC). PKC activation can lead to changes in cytoskeletal dynamics and cell adhesion, processes in which Spa2 might be implicated. As a result, PMA could indirectly enhance Spa2's role in cytoskeletal reorganization. | ||||||
D-erythro-Sphingosine-1-phosphate | 26993-30-6 | sc-201383 sc-201383D sc-201383A sc-201383B sc-201383C | 1 mg 2 mg 5 mg 10 mg 25 mg | $162.00 $316.00 $559.00 $889.00 $1693.00 | 7 | |
S1P binds to its G-protein-coupled receptors, leading to downstream signaling events that can result in actin cytoskeleton rearrangement. Spa2, being potentially involved in similar pathways, would have its functionality indirectly enhanced through these cytoskeletal changes. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $76.00 $265.00 | 80 | |
Ionomycin is a calcium ionophore that increases intracellular calcium levels, which can activate calcium-dependent signaling pathways. If Spa2 is involved in such pathways, ionomycin could enhance the functional activity of Spa2 by providing a favorable environment for its activation. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $42.00 $72.00 $124.00 $238.00 $520.00 $1234.00 | 11 | |
EGCG inhibits several protein kinases, potentially reducing competitive signaling and allowing Spa2-related pathways to be more active. This could indirectly enhance the functional activity of Spa2 in processes it regulates. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $121.00 $392.00 | 148 | |
LY294002 is an inhibitor of the PI3K pathway, which could lead to a compensatory upregulation of alternative pathways that Spa2 is involved in, such as those related to cellular morphogenesis and polarity, thereby enhancing Spa2 activity. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
Thapsigargin disrupts calcium homeostasis by inhibiting the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). The resulting increase in cytosolic calcium levels could activate calcium-dependent processes where Spa2 may play a role, thereby indirectly enhancing its activity. | ||||||
Dibutyryl-cAMP | 16980-89-5 | sc-201567 sc-201567A sc-201567B sc-201567C | 20 mg 100 mg 500 mg 10 g | $45.00 $130.00 $480.00 $4450.00 | 74 | |
db-cAMP is a cell-permeable cAMP analog that activates cAMP-dependent pathways such as PKA. By mimicking cAMP, it could enhance Spa2 activity by engaging signaling events or structural changes in the cell that Spa2 is associated with. | ||||||
Staurosporine | 62996-74-1 | sc-3510 sc-3510A sc-3510B | 100 µg 1 mg 5 mg | $82.00 $150.00 $388.00 | 113 | |
Staurosporine is a broad-spectrum protein kinase inhibitor. By inhibiting certain kinases, it may lead to the activation of Spa2 through the release of inhibition on Spa2-related pathways or by promoting its role in cellular signaling events. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A sc-24000B sc-24000C | 10 µg 100 µg 500 µg 1 mg | $160.00 $750.00 $1400.00 $3000.00 | 59 | |
Calyculin A is an inhibitor of protein phosphatases 1 and 2A. Inhibition of these phosphatases can lead to increased phosphorylation of proteins within pathways that Spa2 is a part of, thereby potentially enhancing Spa2's functional activity. | ||||||