pka i

Rp-cAMPS triethylammonium salt is a competitive inhibitor of cAMP-dependent protein kinases I and II, inhibiting cAMP-induced conformational changes to block PKA activation.

PKA inhibitor fragment (6-22) amide Acetate is a synthetic peptide which selectively inhibits PKA activity by binding to its substrate site (IC50 < 2 nM).

PKI PKA Inhibitor (5-24) is a synthetic peptide inhibitor of PKA (cAMP-dependent protein kinase) (Ki= 2.3 nM) derived from the active site of the skeletal muscle inhibitor protein.1It mimics the protein substrate by binding to the catalytic site through the arginine-cluster basic subsite.1The prominent enzyme-substrate interaction site occurs where PKA catalytic subunit residues Tyr235and Phe239form a sandwich-like structure with residue Phe10of PKI (5-24).2

PKA Inhibitor Fragment (6-22) amide TFA (PKA Inhibitor Fragment (6-22) amide TFA) is a highly potent inhibitor of cAMP-dependent protein kinase A (PKA) with a Ki of 2.8 nM and reverses the pain-relieving effects of low levels of morphine in mice.

BAMB-4 (ITPKA-IN-C14) is a highly membrane-permeable inhibitor of inositol-1,4,5-trisphosphate-3-kinase A (ITPKA), effectively suppressing the metastasis-promoting effect of ITPKA in lung tumor cells (with IC50 of 37 μM in ADP-Glo Assay).

Rp-cAMPS competitively inhibits the cAMP-induced activation of cAMP-dependent protein kinase (PKA).

Rp-cAMPS sodium is a phosphorothioate analog of cAMP, a protein kinase A inhibitor and a membrane-permeable cAMP antagonist that inhibits cAMP-dependent protein kinases by blocking cAMP-induced conformational transitions, and can be used in the study of cardiovascular diseases.

PKA-IN-2 (Compound j1) is an inhibitor targeting the serine/threonine kinase J-PKAcα, with an IC50 of 6.3 nM. PKN-IN-1 is applicable for research on liver cancer, including fibrolamellar hepatocellular carcinoma.

PKA-IN-1 is a selective and potent cyclic AMP-dependent protein kinase (PKA) catalytic subunit (cAK) inhibitor (IC50: 0.03 μM).PKA-IN-1 can be used to study diseases of the immune system.

Akt1&PKA-IN-1 is a potent dual inhibitor of Akt and PKA, with IC50 values of 0.11 μM for Akt, 0.03 μM for PKAα, and 9.8 μM for CDK2, demonstrating selective inhibition of cyclin-dependent kinase 2 (CDK2).

Akt1&PKA-IN-2 ((R)-29), a compound specific to PKB/AKT and selective for cyclin-dependent kinase 2 (CDK2), effectively inhibits AKT1, PKAa, and CDK2a with IC50 values of 0.007 µM, 0.01 µM, and 0.69 µM, respectively.

Sp-cAMPS sodium salt is an analog of cAMP that serves as a potent activator of cAMP-dependent PKA I and PKA II, and as a competitive phosphodiesterase (PDE3A) inhibitor with a Ki of 47.6 μM. It also binds the PDE10 GAF domain with an EC50 of 40 μM [1] [2] [3].

Ellagic acid (Gallogen), a thickened tetracyclic natural product, is a potent CK2 inhibitor (IC50=40 nM; Ki=20 nM) with ATP-competitive properties. Ellagic acid is an antioxidant and also possesses antiproliferative activity.

A-3 hydrochloride is a potent, cell-permeable, reversible, ATP-competitive non-selective antagonist of various kinases. It inhibits PKC and casein kinase I with Ki values of 47 μM and 80 μM, respectively[1], and also inhibits PKA (Ki=4.3 μM), casein kinase II (Ki=5.1 μM), and myosin light chain kinase (MLCK) (Ki=7.4 μM).

KT5823 is a selective and potent cGMP-dependent protein kinase (PKG) inhibitor with inhibitory effects on PKA and PKC.KT5823 increases thyroid-stimulating hormone-induced (Na+/I- symporter) NIS expression and iodide ion uptake by modulating sodium iodide symporter protein expression and activity in thyroid cells. KT5823 induces apoptosis.

DM243 is an EPAC1 activator and STAT3 modulator with a pIC50 of 4.769. It increases the levels of GTP-bound Rap1 in cells expressing EPAC1 without activating EPAC2 or PKA. DM243 reduces STAT3 phosphorylation levels in endothelial cells induced by IL-6/IL-6Rα. This compound inhibits the transformation of fibroblasts into myofibroblasts induced by TGF-β1, thereby decreasing the levels of α-smooth muscle actin and type I collagen in pulmonary fibroblasts. DM243 exhibits very low cytotoxicity in normal human lung fibroblasts.

DM245 serves as an EPAC1 activator and a STAT3 phosphorylation inhibitor, with a target pIC50 of 4.801. It enhances Rap1-GTP levels by activating EPAC1 without affecting EPAC2 or PKA. Additionally, DM245 reduces IL-6/IL-6Rα-induced STAT3 phosphorylation in endothelial cells and inhibits TGF-β1-induced fibroblast-to-myofibroblast transformation, decreasing αSMA and type I collagen levels.

Two Rho-associated kinases (ROCK), ROCK-I and ROCK-II, act downstream of the G protein Rho to regulate cytoskeletal stability. The ROCKs play important roles in diverse cellular functions including cell adhesion and proliferation, smooth muscle contraction, and stem cell renewal. Glycyl-H-1152 is a selective and potent ROCK inhibitor (IC50 = 11.8 nM for ROCK-II). It is a glycylated isoquinoline compound derived from the therapeutically-important ROCK inhibitor HA-1077 (Fasudil) and exhibits better specificity. Thus, it poorly inhibits Ca2+/calmodulin-dependent kinase type II, protein kinase (PK) G, and Aurora A (IC50 = 2.57, 2.35, and 3.26 μM, respectively) as well as PKA or PKC (IC50 ≥ 10 μM for each). The potency of Glycyl-H-1152 is superior to that of other ROCK inhibitors, including Y-27632 (Ki = 220 nM) and HA-1077 (IC50 = 158 nM).

Rp-8-bromo-Cyclic AMPS (Rp-8-bromo-cAMPS) is a cell-permeable cAMP analog that combines an exocyclic sulfur substitution in the equatorial position of the cyclophosphate ring with a bromine substitution in the adenine base of cAMP. It acts as an antagonist of cAMP-dependent protein kinases (PKAs) and is resistant to hydrolysis by cyclic nucleotide phosphodiesterases. Rp-8-bromo-cAMPS more effectively antagonizes cAMP-dependent activation of purified PKA type I from rabbit muscle than PKA type II from bovine heart.

Rp-8-CPT-cAMP is a structural combination of the lipophilic and non-hydrolyzable cAMP analogs, 8-CPT-cyclic AMP and Rp-cyclic AMPS .[1] It functions as a site-selective inhibitor of protein kinase A (PKA) type I and II, with preference towards site A of type I and site B of type II.2 By occupying cAMP binding sites at the regulatory subunit of PKA, Rp-8-CPT-cAMP prevents the kinase holoenzyme from dissociative activation.[2],[3]

Sp-8-CPT-cAMPS is a powerful and specific cAMP analog that activates cAMP-dependent protein kinase A (PKA I and PKA II) selectively and effectively. It exhibits a 153-fold preference for site A of RI over site A of RII, and a 59-fold preference for site B of RII over site B of RI.

Rp-8-CPT-cAMPS is a powerful and competitive antagonist of cAMP-induced activation of cAMP-dependent protein kinase (PKA) I and II. Acting as a potent cAMP analog, Rp-8-CPT-cAMPS exhibits a preference for site A of RI over site A of RII. Additionally, it favors site B of RII over site B of RI. This compound effectively inhibits cAMP-dependent PKA activation and demonstrates selectivity in binding to specific sites within the protein kinase.

Sp-cAMPS triethylamine, a cAMP analog, serves as a potent activator of cAMP-dependent PKA I and II, and acts as a competitive inhibitor of phosphodiesterase (PDE3A) with a K i of 47.6 µM. Additionally, it binds the PDE10 GAF domain with an EC 50 of 40 μM [1] [2] [3].

PKI(5-24) TFA is a synthetic peptide inhibitor of PKA (cAMP-dependent protein kinase) with potent and competitive inhibition properties, exhibiting a K i of 2.3 nM. It corresponds to residues 5-24 of the natural heat-stable protein kinase inhibitor [1][2].