The chemical class of Erich2 Activators comprises a diverse range of compounds postulated to modulate the activity of Erich2, a protein whose detailed functions and interactions within cellular pathways are not extensively documented. This class includes various molecules, each possessing unique properties and mechanisms to potentially engage and activate pathways associated with Erich2. From agents that increase intracellular signaling messengers like cAMP (e.g., Forskolin) to those that modulate specific receptor pathways (e.g., Epidermal Growth Factor (EGF)), the scope of these activators is broad. Other members of this class, such as Ionomycin, work by altering ion concentrations, specifically calcium, thereby influencing a range of calcium-dependent cellular processes. This variety highlights the multifaceted approach these compounds might employ to exert their influence on Erich2 activity. The activators are not limited to a single mode of action but rather represent a spectrum of interactions, including the activation of kinase pathways (e.g., Phorbol 12-myristate 13-acetate (PMA) with PKC), modification of growth factor signaling (e.g., Insulin-like Growth Factor-1 (IGF-1)), and modulation of hormone-driven pathways (e.g., Estradiol and Dehydroepiandrosterone (DHEA)).
The significance of the Erich2 Activators class lies in its potential to offer insights into the regulation and function of Erich2 within the cell. These activators, through their varied actions, provide a toolset to probe the biological roles of Erich2. They can shed light on the signaling pathways that Erich2 might be a part of, as well as its possible involvement in critical cellular functions. For instance, compounds like FGF-basic and Sphingosine-1-phosphate (S1P) underscore the potential involvement of Erich2 in processes like cell growth, differentiation, and response to external signaling molecules. Additionally, the inclusion of compounds like Nicotinamide mononucleotide (NMN), which influences NAD+ biosynthesis, opens avenues to explore Erich2's role in metabolic pathways. Collectively, this class of activators is not just a group of chemicals with a shared target but represents a key to understanding the complex network of cellular signaling and regulation. Their study and application could illuminate the intricate dance of molecular interactions and pathways within the cell, offering a deeper understanding of how proteins like Erich2 contribute to the orchestration of cellular life.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 | |
PMA activates protein kinase C (PKC), which can phosphorylate a range of proteins, including ERICH2. Given that PKC acts on a broad spectrum of cellular proteins, it can be inferred that ERICH2 is a potential substrate for PKC when activated by PMA. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $78.00 $270.00 | 80 | |
Ionomycin is a calcium ionophore that increases intracellular calcium levels, which can activate calcium/calmodulin-dependent protein kinases (CaMK). These kinases can phosphorylate and activate numerous proteins, and ERICH2 may be activated as part of the downstream effects of elevated intracellular calcium. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $291.00 $530.00 $1800.00 | 78 | |
Okadaic acid is a potent inhibitor of protein phosphatases 1 and 2A, leading to increased phosphorylation levels of various proteins due to reduced dephosphorylation. ERICH2 could be kept in an activated state by the reduced activity of these phosphatases. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $99.00 $259.00 | 36 | |
Anisomycin is known to activate stress-activated protein kinases (SAPKs), such as JNK. These kinases can phosphorylate several cellular proteins. If ERICH2 is a target for JNK or related kinases, its activation could occur as a result of anisomycin’s action on these signaling molecules. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
Thapsigargin disrupts calcium homeostasis by inhibiting the sarcoplasmic/endoplasmic reticulum Ca2+ ATPase (SERCA), causing a rise in cytosolic calcium levels. This can lead to the activation of numerous calcium-dependent enzymes and signaling pathways, potentially including those that activate ERICH2. | ||||||
Hydrogen Peroxide | 7722-84-1 | sc-203336 sc-203336A sc-203336B | 100 ml 500 ml 3.8 L | $31.00 $61.00 $95.00 | 28 | |
Hydrogen peroxide can act as an oxidizing agent and has been shown to influence various signal transduction pathways, particularly those involving oxidative stress responses. It can lead to the activation of a range of kinases that could phosphorylate and activate ERICH2 as part of their signaling actions. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc ions provided by zinc acetate can act as essential cofactors for many proteins and may directly contribute to the catalytic activity of ERICH2 if it requires zinc for its function. | ||||||
Magnesium sulfate anhydrous | 7487-88-9 | sc-211764 sc-211764A sc-211764B sc-211764C sc-211764D | 500 g 1 kg 2.5 kg 5 kg 10 kg | $46.00 $69.00 $163.00 $245.00 $418.00 | 3 | |
Magnesium ions are critical for many enzymatic reactions as cofactors. Magnesium sulfate can provide these ions, potentially stabilizing the structure of ERICH2 and enhancing its enzymatic function if it requires magnesium. | ||||||
Sodium Orthovanadate | 13721-39-6 | sc-3540 sc-3540B sc-3540A | 5 g 10 g 50 g | $49.00 $57.00 $187.00 | 142 | |
Sodium orthovanadate inhibits protein tyrosine phosphatases, which could lead to a maintained phosphorylation state of ERICH2, assuming it undergoes regulation by tyrosine phosphorylation. | ||||||
IBMX | 28822-58-4 | sc-201188 sc-201188B sc-201188A | 200 mg 500 mg 1 g | $260.00 $350.00 $500.00 | 34 | |
IBMX is a phosphodiesterase inhibitor that prevents cAMP breakdown, maintaining PKA activation. Through PKA, ERICH2 could be phosphorylated and activated, provided it is a substrate for PKA. | ||||||