protein kinase inhibitor peptide

Protein kinase inhibitor peptide matches the inhibitory domain of the heat-stable protein kinase inhibitor.

Protein Kinase C 19-31 acetate, a peptide inhibitor of protein kinase C (PKC), derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as protein kinase C substrate

PKC ζ pseudosubstrate acetate is an inhibitor of protein kinase C (PKC) ζ; attached to cell permeabilisation Antennapedia domain vector peptide. Consists of amino acids 113 - 129 of PKC ζ pseudosubstrate domain linked by a disulphide bridge to the Antenna

Protein kinase C (PKC ) is a calcium-independent, phospholipid- and diacylglycerol-dependent serine/threonine kinase involved in diverse signaling pathways, including those involved in neuronal signaling, cytoskeletal function, and inflammation.[1] PKC inhibitor peptide is a synthetic peptide corresponding to an amino acid sequence found in the amino terminal C2 domain of most mammalian forms of PKC .[2] It selectively and reversibly inhibits the translocation of PKC to intracellular membranes, blocking activation.[2] PKC inhibitor peptide is commonly used in cells to evaluate the role of PKC in various cellular responses.[3],[4],[5]

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].

[Ala107]MBP(104-118) TFA is a noncompetitive peptide inhibitor of protein kinase C (PKC), with IC50 values ranging from 46 to 145 μM.

[Ala113]MBP(104-118) TFA is a peptide inhibitor that acts noncompetitively against protein kinase C (PKC), with inhibitory concentrations (IC50) ranging from 28 to 62 μM [1].

Protein Kinase C (19-31) TFA is a peptide inhibitor derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31), featuring a serine substitution for alanine at position 25. It serves as a substrate peptide for evaluating Protein Kinase C (PKC) activity, playing a crucial role in modulating protein functions by phosphorylating the hydroxyl groups of serine and threonine amino acids on target proteins [1] [2].

MMI-0100, a cell-permeant peptide inhibitor of mitogen-activated protein kinase activated protein kinase II (MK2), effectively reduces intimal hyperplasia ex vivo and in vivo. It specifically suppresses IL-6 expression while not affecting IL-8 expression and mitigates fibrotic processes, including vein graft disease [1].

Phosphate acceptor peptide acts as a substrate for cAMP-dependent protein kinase (PKA) and serves as a weak inhibitor of protein kinase C (PKC) [1].

Protein Kinase C (19-35) Peptide, acting as a PKC pseudosubstrate inhibitor region, can potentially inhibit PKC activity by blocking the substrate-binding site within the kinase domain, thereby inactivating the cytoplasmic form of PKC [1] [2].

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.

Myristoylated AC3-I is a biologically active peptide and a myristoylated variant of the Autocamtide-3-Derived Inhibitory Peptide (AC3-I). It acts as a highly specific inhibitor of Calmodulin-Dependent Protein Kinase II (CaMKII) with enhanced resistance to proteolysis. This compound is a derivative of Autocamtide-3, where the Thr-9 phosphorylation site is replaced by Ala.

Myristoylated PKCθ pseudosubstrate peptide inhibitor is a synthetic peptide utilized to investigate the mechanism of action of protein kinase C theta (PKCθ) [1].

Myristoylated PKCε inhibitor peptide (Myr-PKCε-) is a cell-permeable inhibitor consisting of a peptide linked to myristic acid that specifically inhibits protein kinase C epsilon (PKCε), consequently diminishing nitric oxide (NO) release in cultured human umbilical vein endothelial cells (HUVECs) [1].

TAT-P4-(DATC5)2 TFA, a high-affinity peptide inhibitor targeting the PDZ domain of protein interacting with C kinase-1 (PICK1), exhibits a K i of 1.7 nM and demonstrates potential in mitigating addiction behaviors in rats [1].

TAT-P4-(DATC5)2 is a potent peptide inhibitor of the PDZ domain of protein interacting with C kinase-1 (PICK1), with a high affinity dissociation constant (K_i) of 1.7 nM. This compound has demonstrated the ability to mitigate addiction behaviors in rat models [1].

PKG inhibitor peptide TFA is an ATP-competitive antagonist of cGMP-dependent protein kinase (PKG) with a K_i value of 86 μM [1].

F1, an anti-inflammatory peptide, incorporates the HIV-1 Tat protein transduction domain linked with a 15-amino acid sequence from residues 46-60 of the inhibitor of NF-κB kinase-interacting peptide (IKIP). It effectively blocks LPS-induced phosphorylation of IκB kinase α (IKKα) and IKKβ, along with the nuclear translocation of NF-κB (p65) in mouse peritoneal macrophages at 5 µM concentration. F1, administered at 5 mg/kg in vivo, significantly reduces IL-6, TNF-α, and IL-1β serum levels and enhances survival in a mouse sepsis model induced by LPS.

Azurin (50-77) is a peptide fragment derived from the copper-containing bacterial protein azurin, present in P. aeruginosa. It exhibits properties that regulate the cell cycle, inhibit cancer proliferation, and manage angiogenesis, proving its potential as an anticancer agent. Specifically, this compound acts as a VEGFR2 inhibitor with an IC20 of approximately 10.7 µM. At a concentration of 20 µM, it effectively induces cell cycle arrest at the G2 M phase in MCF-7 breast cancer cells, while a higher concentration of 50 µM significantly reduces the proliferation of both MCF-7 and ZR-75-1 breast cancer cell lines. Furthermore, Azurin (50-77) impedes VEGF-A-induced capillary tube formation with an IC50 of 12 µM, and alters the cellular and extracellular levels of critical signaling and structural proteins such as F-actin, focal adhesion kinase (FAK), paxillin, and platelet endothelial cell adhesion molecule-1 (PECAM-1) in human umbilical vein endothelial cells (HUVECs) at a concentration of 25 µM. Demonstrating its efficacy in vivo, Azurin (50-77) administered at 10 mg kg per day notably reduces tumor volume in an MCF-7 mouse xenograft model, highlighting its therapeutic potential.

Protein Kinase C (19-31) TFA, a peptide inhibitor of protein kinase C (PKC), derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as protein kinase C substrate p

Protein Kinase C (19-31), a peptide inhibitor derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as a substrate peptide for testing protein kinase C activity.

Protein Kinase C (19-36) is a pseudosubstrate peptide that inhibits protein kinase C (PKC) with an IC50 of 0.18 μM.

PKG inhibitor peptide TFA (82801-73-8 free base) is an inhibitor of ATP-competitive cGMP-dependent protein kinase (PKG).