KEPI, or kinase-enhanced PP1 inhibitor, is a protein that plays a significant role in the regulation of serine/threonine phosphatase activity, particularly targeting protein phosphatase 1 (PP1). This regulatory role is crucial in maintaining the delicate balance of phosphorylation within cells, which is essential for various cellular processes such as cell cycle progression, muscle contraction, and neural signaling. KEPI's function revolves around inhibiting PP1, thereby prolonging the phosphorylation state of various substrates involved in these critical processes. This mechanism ensures that cellular activities requiring prolonged phosphorylation for functional activation are effectively regulated. KEPI, by modulating the activity of PP1, indirectly influences numerous pathways that depend on phosphorylation for signal transduction, thereby playing a pivotal role in cellular communication and function.
The activation of KEPI involves several cellular mechanisms, primarily through the phosphorylation by specific kinases. Phosphorylation at key sites on KEPI enhances its ability to bind to and inhibit PP1, which increases the phosphorylation levels of various downstream proteins necessary for carrying out cellular functions. This activation process is typically initiated by signals that necessitate a rapid response from the cell, such as hormonal stimuli or neural activation, which require quick changes in phosphorylation states to proceed. Additionally, the regulation of KEPI itself can be influenced by factors such as changes in intracellular calcium levels or through interaction with other regulatory proteins, which can either enhance or diminish its inhibitor activity. This level of regulation allows KEPI to be a flexible mediator in response to cellular needs, adapting its activity to facilitate appropriate cellular responses to internal and external stimuli. Understanding the mechanisms behind KEPI's activation provides insights into the complex network of cellular signaling pathways and highlights the sophisticated nature of cellular regulation mechanisms that ensure proper function and response in various physiological and potentially pathological conditions. This intricate regulatory system underscores the importance of precise modulation of protein activity within the cell, reflecting the complex interplay between different signaling molecules and pathways.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
(−)-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 | |
As a known modulator of protein expression and stability, EGCG could increase PPP1R14C levels through antioxidant response elements, indirectly enhancing its inhibitory action on PP1. | ||||||
Curcumin | 458-37-7 | sc-200509 sc-200509A sc-200509B sc-200509C sc-200509D sc-200509F sc-200509E | 1 g 5 g 25 g 100 g 250 g 1 kg 2.5 kg | $36.00 $68.00 $107.00 $214.00 $234.00 $862.00 $1968.00 | 47 | |
Curcumin influences a wide array of signaling molecules; it may enhance PPP1R14C activity by modulating gene expression and protein stability, resulting in increased inhibition of PP1. | ||||||
Resveratrol | 501-36-0 | sc-200808 sc-200808A sc-200808B | 100 mg 500 mg 5 g | $60.00 $185.00 $365.00 | 64 | |
Resveratrol can modulate protein kinase activity, which could lead to enhanced phosphorylation of PPP1R14C, potentially increasing its inhibitory effect on PP1. | ||||||
Lithium | 7439-93-2 | sc-252954 | 50 g | $214.00 | ||
Lithium is known to inhibit GSK-3β, which might lead to a stabilization of PPP1R14C, consequently increasing its inhibition of PP1. | ||||||
Sodium Butyrate | 156-54-7 | sc-202341 sc-202341B sc-202341A sc-202341C | 250 mg 5 g 25 g 500 g | $30.00 $46.00 $82.00 $218.00 | 19 | |
As a histone deacetylase inhibitor, sodium butyrate may enhance the expression of PPP1R14C, thereby indirectly increasing its inhibitory activity. | ||||||
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 | |
By elevating cAMP levels, forskolin can activate PKA which could theoretically phosphorylate PPP1R14C, potentially enhancing its inhibitory effect on PP1. | ||||||
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 activates PKC, which could phosphorylate PPP1R14C and enhance its inhibition of PP1. | ||||||
Rolipram | 61413-54-5 | sc-3563 sc-3563A | 5 mg 50 mg | $75.00 $212.00 | 18 | |
Inhibiting PDE4 with rolipram raises cAMP levels, thereby activating PKA which might increase the phosphorylation and activity of PPP1R14C. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Although a known PP1 inhibitor, okadaic acid at low concentrations might selectively modulate phosphatase activities leading to altered PPP1R14C function. | ||||||
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 | |
Similar to okadaic acid, calyculin A can inhibit PP1; however, at specific concentrations, it may differentially affect phosphorylation patterns including those related to PPP1R14C. | ||||||