pka i

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 Acetate is a synthetic peptide which selectively inhibits PKA activity by binding to its substrate site (IC50 < 2 nM).

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.

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.

8-MA-cAMP (8-Methylamino-cAMP) is a cyclic adenosine monophosphate analog that acts as a site-selective PKA agonist, exhibiting similar affinity for the B site of both Type I and Type II protein kinase A. When used in conjunction with analogs that preferentially target site A, such as 8-piperidinyl cAMP, 8-MA-cAMP facilitates selective stimulation of Type I enzymes.

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]

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.

PKI (5-24), amide (IP20-amide) is a potent inhibitor of cAMP-dependent protein kinase (PKA) with an inhibition constant (K i) of 2.3 nM [1]. This 20-residue peptide mirrors the active segment of the heat-stable inhibitor protein specific to PKA, showcasing significant inhibitory efficacy.

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.

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).

AKAP disruptor. Selectively binds PKA-RI with high affinity (KD values are 6.2 and 12.1 nM for the RIα and β subunits, respectively) and blocks its interaction with AKAP. Inhibits type I PKA-mediated phosphorylation in live cells. Cell permeable.

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).

Fasudil mesylate (HA-1077; AT877) is a nonspecific, orally active inhibitor of RhoA ROCK, exhibiting additional inhibitory effects on protein kinases with a K i of 0.33 μM for ROCK1. It shows IC 50 values of 0.158 μM for ROCK2, and 4.58 μM, 12.30 μM, and 1.650 μM for PKA, PKC, and PKG, respectively. Furthermore, Fasudil mesylate acts as a potent Ca 2+ channel antagonist and vasodilator, enhancing its pharmacological profile [1] [2] [3] [4] [5] [6].

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.

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

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.

Sp-8-pCPT-cGMPS is a potent agonist for cyclic guanosine monophosphate-gated (CNG) channels and serves as a lipophilic activator for PKG (types I α, I β, and II) and PKA II. It exhibits excellent cell membrane permeability and stability against phosphodiesterases. This compound is utilized in studying the role of cGMP in synaptic transmission and neural plasticity.

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].

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].

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.