Protein Kinase A (PKA)

STAD 2 is a potent and selective disruptor of protein kinase A regulatory subunit type II (PKA-RII), exhibiting a dissociation constant (Kd) of 6.2 nM. It specifically interferes with the interactions between PKA and A-kinase anchoring proteins (AKAP) in an isoform-selective manner. Additionally, STAD 2 demonstrates antimalarial activity through a mechanism that is independent of PKA, making it a valuable tool for research into PKA-related signaling pathways and malaria therapeutics.

PKI (14-24)amide TFA is a potent inhibitor of protein kinase A (PKA) that effectively blocks cyclic AMP-dependent protein kinase activity in various cellular contexts. This compound demonstrates significant inhibitory action, making it valuable for studies involving PKA-related signaling pathways. Its utilization in research can provide insights into the molecular mechanisms of PKA-mediated processes in health and disease.

PKI (14-24)amide is a potent inhibitor of Protein Kinase A (PKA), effectively disrupting the activity of cyclic AMP-dependent protein kinase. This compound has been shown to strongly inhibit PKA activity in cell homogenates, making it a valuable tool for studying PKA-related signaling pathways and their biological implications. Its application in research can facilitate investigations into cellular processes regulated by PKA, contributing to a better understanding of various physiological and pathological conditions.

Rp-8-CPT-cAMPS sodium is a competitive antagonist of cAMP, specifically inhibiting the activation of protein kinase A (PKA) types I and II. It demonstrates preferential binding to site A of the regulatory subunit RI and site B of the regulatory subunit RII, making it a valuable tool for dissecting cAMP signaling pathways. This compound is widely utilized in research focused on intracellular signaling, pharmacology, and the role of PKA in various physiological processes.

Sp-8-CPT-cAMPS is a potent and selective activator of cAMP-dependent protein kinase A (PKA), specifically targeting PKA I and PKA II. This cAMP analog demonstrates a remarkable 153-fold selectivity for Site A of RI over Site A of RII and a 59-fold selectivity for Site B of RII over Site B of RI. Its ability to effectively modulate PKA activity makes it a valuable tool for research in signaling pathways and cellular responses associated with cAMP.

H1-7 is a synthetic polypeptide designed as a substrate for protein kinase A (PKA). This compound effectively mimics histone H1 phosphorylation sites, allowing for the study of PKA-mediated phosphorylation processes. Its application is significant in understanding PKA signaling pathways and epigenetic modifications associated with histones in various biological contexts.

Rp-8-CPT-cAMPS is a potent antagonist of cAMP-dependent protein kinase A (PKA), inhibiting the activation of both PKA I and II. This cAMP analog selectively targets site A of the regulatory subunit type I over site A of type II, as well as site B of type II over site B of type I. Its ability to modulate PKA activity makes it a valuable tool for investigating downstream signaling pathways influenced by cAMP. Researchers can utilize Rp-8-CPT-cAMPS in studies focused on cellular responses and signal transduction mechanisms.

GEM-231 is an 18mer antisense oligonucleotide that specifically targets the mRNA of the PKA-I (RIα regulatory subunit of cAMP-dependent protein kinase type I). This compound has demonstrated the ability to induce cell growth arrest, apoptosis, and differentiation across various cancer cell lines in vitro, as well as in tumor models in vivo. GEM-231 serves as a valuable tool for investigating PKA signaling pathways and their implications in cancer biology.

8-Br-cAMP-AM is a cyclic adenosine monophosphate (cAMP) analog that functions as a protein kinase A (PKA) agonist. By mimicking cAMP, it activates critical signaling pathways such as PKA and Epac, facilitating studies on heart-related conditions. This compound is particularly useful for investigating cardiac ischemia and reperfusion injury, providing valuable insights into these pathological processes.

PKI (5-24), amide is a potent inhibitor of cAMP-dependent protein kinase A (PKA), derived from the active region of the heat-stable inhibitor protein. With an inhibition constant (Ki) of 2.3 nM, it effectively disrupts PKA signaling pathways. This reagent is valuable for research applications focusing on PKA-mediated cellular functions and signaling cascades in various biological contexts.

Aplithianines A is a selective inhibitor of J-PKAcα, exhibiting an IC50 value of 1 μM, while also demonstrating inhibition of wild-type PKA with an IC50 of 84 nM. This compound exerts its inhibitory effects by competitively binding to the ATP pocket of J-PKAcα, thereby affecting its catalytic activity. Aplithianines A is valuable for research applications involving protein kinase signaling pathways and the study of PKA-related cellular processes.

PKItide is a potent inhibitor of Protein Kinase A (PKA), exhibiting an IC50 of 0.2 μM for cAMP-dependent PKA. This compound effectively disrupts PKA signaling pathways, making it a valuable tool for studying cellular processes regulated by cAMP. Research applications include investigating the role of PKA in various physiological and pathological conditions, as well as exploring therapeutic strategies targeting PKA-related diseases.

8-CPT-6-Phe-cAMP is a potent activator of protein kinase A (PKA), functioning as an analogue of the signaling molecule cyclic adenosine monophosphate (cAMP). This compound is widely utilized in research to study PKA-mediated pathways and cellular responses related to various physiological processes. Its ability to effectively modulate PKA activity makes it an essential tool for investigating signal transduction mechanisms and pharmacological interventions.

Rp-cAMPS is a potent antagonist of cyclic adenosine monophosphate (cAMP) that effectively inhibits the activation of protein kinase A (PKA) types I and II, exhibiting Ki values of 12.5 µM and 4.5 µM, respectively. This cAMP analog is resistant to hydrolysis by phosphodiesterases, making it suitable for research focused on cAMP signaling pathways. Rp-cAMPS is commonly used in studies investigating the regulatory role of PKA in various physiological processes and disease models.

Rp-8-Br-cAMPS is a potent inhibitor of protein kinase A (PKA) that functions by occupying the cAMP binding sites on the regulatory subunits of PKA type I. This inhibition prevents the dissociation and activation of PKA, thereby modulating downstream signaling pathways. Rp-8-Br-cAMPS is particularly useful in research applications focused on tumor biology, retrovirus-induced immune deficiency, and the regulation of insulin secretion.

PKA Substrate is a selective peptide designed for the measurement of protein kinase A (PKA) activity. This substrate undergoes phosphorylation in the presence of active PKA, allowing for the detection and quantification of kinase activity in various biological samples. Its utility in biochemical assays makes it an essential tool for researchers investigating PKA-mediated signaling pathways.

GSK466317A is a potent protein kinase A (PKA) inhibitor, exhibiting an IC50 of 12.59 μM. In addition to its primary target, GSK466317A also demonstrates inhibitory activity against GRK1, GRK2, and GRK5, with corresponding IC50 values of 1000 μM, 31.62 μM, and 39.81 μM, respectively. This compound is valuable for research applications involving signal transduction pathways and the study of G protein-coupled receptor (GPCR) functionality.

Protein Kinase Inhibitor 7 is an inhibitor of Protein Kinase A (PKA) and Protein Kinase C (PKC). This compound modulates the autocrine motility factor (AMF) signaling pathway, demonstrating potential applications in cancer research and studies involving cell signaling without influencing overall cell motility. It is a valuable tool for elucidating the roles of PKA and PKC in various biological processes.

ME 3407 is a myosin light chain kinase (MLCK) and protein kinase A (PKA) inhibitor that disrupts H+-K+-ATPase redistribution. This compound effectively blocks gastric acid secretion and inhibits aminopyrine accumulation by preventing the microsomal-to-apical membrane redistribution of H+-K+-ATPase. ME 3407 demonstrates potential for use in research related to peptic ulcers and other gastrointestinal disorders.

Sp-cAMPS-AM is a cell-permeable analog of cyclic AMP (cAMP) that functions as a potent activator of Protein Kinase A (PKA). Upon cellular uptake, it releases its parent compound, Sp-cAMPS, which subsequently promotes PKA activation and CREB phosphorylation. This reagent is valuable for research applications in signaling pathways involving cAMP and PKA, facilitating studies on gene expression and cellular response mechanisms.

Sp-8-pCPT-cGMPS is a potent activator of protein kinase G (PKG) and protein kinase A (PKA) with significant cell membrane permeability and phosphodiesterase stability. This cyclic guanosine monophosphate analog effectively engages PKG types I α, I β, and II, making it invaluable for research in signal transduction pathways. It is utilized to investigate the role of cGMP in neural plasticity, synaptic transmission, and other physiological processes influenced by these kinases.

FMP-API-1 is an inhibitor of the A-kinase anchoring protein (AKAP)-PKA interaction. By binding to the allosteric site of protein kinase A (PKA) regulatory subunits, FMP-API-1 enhances PKA activity and promotes the function of aquaporin-2 (AQP2) in PKA-knockout renal cortical collecting duct cell lines (mpkCCD cells). This compound is valuable for investigating nephrogenic diabetes insipidus (NDI) and the underlying mechanisms of renal water transport.

8-MA-cAMP (8-Methylamino-cAMP) is a cyclic AMP analog that serves as a selective agonist for protein kinase A (PKA), specifically targeting the B site of both type I and type II PKA. This compound demonstrates key biological activity by effectively modulating PKA-mediated signaling pathways. Researchers utilize 8-MA-cAMP in combination with priming analogs, such as 8-piperidinyl cAMP, to achieve precise activation of type I PKA, making it valuable for studies in cellular signaling and related therapeutic research.

Sp-6-Phe-cAMPS is a potent, selective activator of cAMP-dependent protein kinase (PKA) that exhibits membrane permeability. This compound uniquely does not directly activate exchange factors that are normally stimulated by cAMP, serving as a useful negative control for Epac studies. Sp-6-Phe-cAMPS is valuable in research focusing on neurodegenerative diseases, facilitating investigations into PKA signaling pathways and their implications in these conditions.

6-Bn-cAMP is a potent site-selective activator of cAMP-dependent protein kinase (PKA), specifically designed not to activate Epac. This compound demonstrates enhanced hydrolytic stability against phosphodiesterases, esterases, and amidases, along with significantly improved membrane permeability compared to standard cAMP. It is widely utilized in research applications aimed at elucidating PKA signaling pathways and their biological implications.

6-Phe-cAMP is a potent and membrane-permeant activator of protein kinase A (PKA), specifically targeting site A of both PKA isozymes. This compound demonstrates strong selectivity, making it an invaluable tool for studying PKA-mediated signaling pathways. Additionally, 6-Phe-cAMP is amenable to phosphorothioate modification, facilitating further research applications in cellular and molecular biology.

Balanol is a highly selective ATP-competitive inhibitor of Protein Kinase C (PKC) and Protein Kinase A (PKA), demonstrating potent activity against various human PKC isozymes, including α, β-I, β-II, γ, δ, ε, η, and ζ, with IC50 values ranging from 4 to 150 nM. This compound effectively inhibits the phosphorylation of key downstream targets such as cyclic AMP response element-binding protein (CREB) and myristoylated alanine-rich C kinase substrate (MARCKS). Balanol can be isolated from the fungus Verticillium balanoides, making it a valuable tool for research involving PKC/PKA signaling pathways.

PKA/AKAP-IN-2 is a non-peptide inhibitor targeting the interaction between protein kinase A (PKA) and A kinase anchoring proteins (AKAP). This compound disrupts the PKA-AKAP binding, providing valuable insights into signaling pathways influenced by cAMP. PKA/AKAP-IN-2 is useful for research into diseases linked to cAMP dysregulation and the broader implications of PKA signaling in cellular processes.

4-Cyano-3-methylisoquinoline is a potent protein kinase A (PKA) inhibitor, exhibiting an IC50 at the micromolar range. This compound has demonstrated the ability to reverse morphine tolerance in murine models, highlighting its potential use in pain management research and studies exploring opioid signaling pathways. Its role as a PKA inhibitor makes it a valuable tool for investigating cellular processes regulated by this important kinase.

PKA/AKAP-IN-1 is a potent non-peptide inhibitor that selectively disrupts the interaction between protein kinase A (PKA) and A-kinase anchoring proteins (AKAP). This compound is valuable for investigating the role of cAMP signaling in various pathological conditions associated with its dysregulation. Research applications include studies on cellular signaling pathways and potential therapeutic interventions in diseases linked to altered PKA/AKAP interactions.

8-OH-cAMP (8-Hydroxy-cAMP) is a polar, membrane-impermeable analog of cyclic adenosine monophosphate (cAMP) that selectively activates protein kinase A (PKA) while resisting degradation by cyclic nucleotide-dependent phosphodiesterases. This compound serves as a valuable tool for investigating the role of cAMP signaling in various biological processes, particularly in cardiovascular and metabolic disease research. Its unique properties enable researchers to elucidate PKA-mediated pathways and their implications in disease development.

Sp-8-Br-cAMPS is a synthetic analog of cyclic adenosine monophosphate (cAMP) and serves as a potent agonist for protein kinase A (PKA) with an EC50 of 360 nM. This compound effectively activates PKA and has been shown to inhibit T cell proliferation and modulate the hemocyte non-self response in Lepidoptera larvae. Its significant biological activity makes it a valuable tool for research into PKA-mediated signaling pathways and immune responses.

Phosphate acceptor peptide is a specific substrate for cyclic AMP-dependent protein kinase (PKA), facilitating the study of phosphorylation processes. Additionally, it exhibits weak inhibitory activity against protein kinase C (PKC), making it useful in exploring the mechanisms of kinase signaling pathways. This reagent is applicable in various biochemical assays aimed at understanding cellular signaling and regulation.

st-Ht31 is a membrane-permeable peptide that inhibits protein kinase A (PKA) anchoring. It effectively induces cholesterol and phospholipid efflux and has been shown to completely reverse foam cell formation in macrophages. This compound offers valuable insights into PKA-related signaling pathways and metabolic health research.

2'-Deoxy-NAD+ sodium is a sodium salt derivative of 2'-Deoxy-NAD+ that functions as a noncompetitive inhibitor of NAD+ with a Ki value of 32 μM. This reagent is valuable for investigating ADP-ribosyl transfer reactions, providing insights into cellular processes involving protein modification. It is particularly useful in studies related to protein kinase A (PKA) activity and regulatory mechanisms in biological systems.