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PKCε Inhibitor Peptide Sale

(Synonyms: Protein Kinase Cɛ Inhibitor Peptide,ɛV1-2) 目录号 : GC44655

An inhibitor of PKCε translocation

PKCε Inhibitor Peptide Chemical Structure

Cas No.:182683-50-7

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500μg
¥215.00
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1mg
¥345.00
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5mg
¥1,620.00
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10mg
¥2,880.00
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Sample solution is provided at 25 µL, 10mM.

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实验参考方法

Cell experiment [1]:

Cell lines

Cardiomyocyte cells from 1- to 2-d-old Wistar rats

Preparation Method

Cells incubated with a mixture of 100 µg/ml of Oleic acid (OA) and 400 µg/ml of bovine serum albumin for 12, 24, or 48 h at 37 °C, while the control group was treated with BSA alone for 24 or 48 h. To determine which protein kinases were activated by OA, use the

Reaction Conditions

1 µM for 24 hours

Applications

Calphostin C blocked OA-induced Cx43 Ser368 phosphorylation, showing involvement of PKC in this signaling cascade. In addition, PKCε Inhibitor Peptide, also blocked the effect, showing that PKCε was involved.

Animal experiment [2]:

Animal models

Male FVB (H-2q) and C57BL/6J (H-2b) mice

Preparation Method

Recipient mice were treated with PKCε Inhibitor Peptide (n = 9, 20 mg/kg/day) or with TAT as a control (13 mg/kg/day; n = 8) using 0.1 mL osmotic pumps (release rate; 0.25 µL/h, 30 mM of each peptide in sterile saline) implanted subcutaneously on day 3, replaced on day 17 and left them until 30 days after transplantation.

Dosage form

osmotic pumps , 20 mg/kg/day

Applications

PKCε Inhibitor Peptide treatment significantly improved the beating score of cardiac allografts compared to TAT-peptide treatment, suggesting that adding PKCε Inhibitor Peptide treatment to CyA augmented preservation of graft function without toxic side effects. The beating score in the PKCε Inhibitor Peptide treated group at 30 days was equivalent to that after 14 days in the TAT control group

References:

[1]: Yuahn-Sieh Huang, et al. Mechanism of oleic acid-induced gap junctional disassembly in rat cardiomyocytes. J Mol Cell Cardiol. 2004 Sep;37(3):755-66.
[2]: Koyanagi T. Noguchi K. Ootani A. Inagaki K. Robbins R.C. Mochly-Rosen D. Pharmacological inhibition of ε PKC suppresses chronic inflammation in murine cardiac transplantation model. J. Mol. Cell Cardiol. 2007; 43: 517-522

产品描述

PKCε Inhibitor Peptide, also called εV1-2, is a protein kinase C ε (PKCε)-derived peptide, act as a selective PKCε inhibitor, inhibits the translocation of PKCε [1]. PKCε Inhibitor Peptide is a peptide designed to compete with native nPKC ε to bind ε-Receptors for activated C Kinase (ε-RACK) and thereby inhibits nPKC ε catalytic activity due to decreased substrate accessibility.

PKCε Inhibitor Peptide, a selective PKCε inhibitor, the addition of PKCε Inhibitor Peptide interferes with the interaction between PKCε and its anchoring protein, and abolishes the cardioprotective effects of PKCε [2]. ADP-induced thromboxane generation in human platelets pretreated with PKCε Inhibitor Peptide was more compared to the platelets pretreated with control peptide [4].

PKCε Inhibitor Peptide were used to inhibit PKCε expression and activity. Apigenin-7-O-β-D-(-6"-p-coumaroyl)-glucopyranoside (APG) preconditioning-induced PKCε translocation to the mitochondria and anti-mitochondrial oxidative stress effects were attenuated by PKCε-targeted ε-V1-2 treatment in IR-injured hearts [3].

References:
[1]. M Yedovitzky, et al. Translocation inhibitors define specificity of protein kinase C isoenzymes in pancreatic beta-cells. J Biol Chem. 1997 Jan 17;272(3):1417-20.
[2]. L. Tang, Y. Peng, T. Xu, X. Yi, Y. Liu, Y. Luo, D. Yin, M. He. The effects of quercetin protect cardiomyocytes from A/R injury is related to its capability to increasing expression and activity of PK C epsilon protein.Mol. Cell. Biochem., 382 (2013), pp. 145-152
[3]. Zhu Y, Di S, Hu W, et al.. A new flavonoid glycoside (APG) isolated from Clematis tangutica attenuates myocardial ischemia/reperfusion injury via activating PKCε signaling.Biochim Biophys Acta Mol Basis Dis. 2017; 1863:701-711. doi: 10.1016/j.bbadis.2016.12.013
[4]. Yamini Saraswathy Bynagari, B-Tech., Bela Nagy, M.D., et al. nPKC Epsilon Negatively Regulates Platelet Functional Responses 2008. Blood (2008) 112 (11): 2855.

PKCε Inhibitor Peptide,也称为 εV1-2,是一种蛋白激酶 C ε (PKCε) 衍生肽,作为选择性 PKCε 抑制剂,抑制 PKCε 的易位 [1]。 PKCε 抑制肽是一种肽,旨在与天然 nPKC ε 竞争结合激活 C 激酶 (ε-RACK) 的 ε-受体,从而由于底物可及性降低而抑制 nPKC ε 催化活性。

PKCε Inhibitor Peptide,一种选择性的PKCε抑制剂,PKCε Inhibitor Peptide的加入会干扰PKCε与其锚定蛋白的相互作用,从而消除PKCε的心脏保护作用[2]。与用对照肽预处理的血小板[4]相比,用 PKCε 抑制剂肽预处理的人血小板中 ADP 诱导的血栓素生成更多。

PKCε 抑制肽用于抑制 PKCε 的表达和活性。芹菜素-7-O-β-D-(-6\-p-coumaroyl)-glucopyranoside (APG) preconditioning-induced PKCε translocation to the mitochondria and anti-mitochondrial oxidative stress effects were attenuated by PKCε-targeted ε-V1-2en_zh_2022q2.mdtreatment in IR-injured hearts [3].

en_zh_2022q2.md

Chemical Properties

Cas No. 182683-50-7 SDF
别名 Protein Kinase Cɛ Inhibitor Peptide,ɛV1-2
Canonical SMILES [H]N[C@@H](CCC(O)=O)C(N[C@H](C(N[C@@H](C(C)C)C(N[C@@H](CO)C(N[C@@H](CC(C)C)C(N[C@@H](CCCCN)C(N1CCC[C@H]1C(N[C@]([C@@H](C)O)([H])C(O)=O)=O)=O)=O)=O)=O)=O)C)=O
分子式 C37H65N9O13 分子量 844
溶解度 100mg/mL in DMSO 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.1848 mL 5.9242 mL 11.8483 mL
5 mM 0.237 mL 1.1848 mL 2.3697 mL
10 mM 0.1185 mL 0.5924 mL 1.1848 mL
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Research Update

Ethanol-Induced Changes in PKCε: From Cell to Behavior

Front Neurosci2018 Apr 12;12:244.PMID: 29706864DOI: 10.3389/fnins.2018.00244

The long-term binge intake of ethanol causes neuroadaptive changes that lead to drinkers requiring higher amounts of ethanol to experience its effects. This neuroadaptation can be partly attributed to the modulation of numerous neurotransmitter receptors by the various protein kinases C (PKCs). PKCs are enzymes that control cellular activities by regulating other proteins via phosphorylation. Among the various isoforms of PKC, PKCε is the most implicated in ethanol-induced biochemical and behavioral changes. Ethanol exposure causes changes to PKCε expression and localization in various brain regions that mediate addiction-favoring plasticity. Ethanol works in conjunction with numerous upstream kinases and second messenger activators to affect cellular PKCε expression. Chauffeur proteins, such as receptors for activated C kinase (RACKs), cause the translocation of PKCε to aberrant sites and mediate ethanol-induced changes. In this article, we aim to review the following: the general structure and function of PKCε, ethanol-induced changes in PKCε expression, the regulation of ethanol-induced PKCε activities in DAG-dependent and DAG-independent environments, the mechanisms underlying PKCε-RACKε translocation in the presence of ethanol, and the existing literature on the role of PKCε in ethanol-induced neurobehavioral changes, with the goal of creating a working model upon which further research can build.

mTORC and PKCε in Regulation of Alcohol Use Disorder

2020;20(17):1696-1708.PMID: 32579497DOI: 10.2174/1389557520666200624122325

Alcohol use disorder (AUD) is characterized by compulsive binge alcohol intake, leading to various health and social harms. Protein Kinase C epsilon (PKCε), a specific family of PKC isoenzyme, regulates binge alcohol intake, and potentiates alcohol-related cues. Alcohol via upstream kinases like the mammalian target to rapamycin complex 1 (mTORC1) or 2 (mTORC2), may affect the activities of PKCε or vice versa in AUD. mTORC2 phosphorylates PKCε at hydrophobic and turn motif, and was recently reported to be associated with alcohol-seeking behavior, suggesting the potential role of mTORC2-PKCε interactions in the pathophysiology of AUD. mTORC1 regulates translation of synaptic proteins involved in alcohol-induced plasticity. Hence, in this article, we aimed to review the molecular composition of mTORC1 and mTORC2, drugs targeting PKCε, mTORC1, and mTORC2 in AUD, upstream regulation of mTORC1 and mTORC2 in AUD and downstream cellular mechanisms of mTORCs in the pathogenesis of AUD.

Regulation of the cytokinesis cleavage furrow by PKCε

Biochem Soc Trans.2014 Dec;42(6):1534-7.PMID: 25399566DOI: 10.1042/BST20140240

Cytokinesis is the final act of the cell cycle where the replicated DNA and cellular contents are finally split into two daughter cells. This process is very tightly controlled as DNA segregation errors and cytokinesis failure is commonly associated with aneuploidy and aggressive tumours. Protein kinase Cε (PKCε) is a lipid-activated serine/threonine kinase that is part of the PKC superfamily. PKCε plays a complex role in the regulation of migration, adhesion and cytokinesis and in the present article we discuss the interplay between these processes. Integrin-mediated interaction with the actin cytoskeleton is a known regulator of cell adhesion and migration and there is emerging evidence that this pathway may also be essential for cytokinesis. We discuss evidence that a known actin-binding region in PKCε is involved in PKCε-mediated regulation of cytokinesis, providing a link between integrin-mediated stabilization of the cytokinesis furrow and PKCε recruitment..

Electroacupuncture Regulates Pain Transition Through Inhibiting PKCε and TRPV1 Expression in Dorsal Root Ganglion

Front Neurosci.2021 Jul 20;15:685715.PMID: 34354561DOI: 10.3389/fnins.2021.685715

Many cases of acute pain can be resolved with few side effects. However, some cases of acute pain may persist beyond the time required for tissue injury recovery and transit to chronic pain, which is hard to treat. The mechanisms underlying pain transition are not entirely understood, and treatment strategies are lacking. In this study, the hyperalgesic priming model was established on rats to study pain transition by injection of carrageenan (Car) and prostaglandin E2 (PGE2). The expression levels of protein kinase C epsilon (PKCε) and transient receptor potential vanilloid 1 (TRPV1) in the L4-L6 dorsal root ganglion (DRG) were investigated. Electroacupuncture (EA) is a form of acupuncture in which a small electric current is passed between a pair of acupuncture needles. EA was administrated, and its effect on hyperalgesia and PKCε and TRPV1 expression was investigated. The PKCε-TRPV1 signaling pathway in DRG was implicated in the pain transition. EA increased the pain threshold of model animals and regulated the high expression of PKCε and TRPV1. Moreover, EA also regulated hyperalgesia and high TRPV1 expression induced by selective PKCε activation. We also found that EA partly increased chronic pain threshold, even though it was only administered between the Car and PGE2 injections. These findings suggested that EA could prevent the transition from acute to chronic pain by inhibiting the PKCε and TRPV1 expression in the peripheral nervous system.

Activation of PKCε-ALDH2 Axis Prevents 4-HNE-Induced Pain in Mice

Biomolecules.2021 Nov 30;11(12):1798. PMID: 34944441DOI: 10.3390/biom11121798

Protein kinase Cε (PKCε) is highly expressed in nociceptor neurons and its activation has been reported as pro-nociceptive. Intriguingly, we previously demonstrated that activation of the mitochondrial PKCε substrate aldehyde dehydrogenase-2 (ALDH2) results in anti-nociceptive effects. ALDH2 is a major enzyme responsible for the clearance of 4-hydroxy-2-nonenal (4-HNE), an oxidative stress byproduct accumulated in inflammatory conditions and sufficient to induce pain hypersensitivity in rodents. Here we determined the contribution of the PKCε-ALDH2 axis during 4-HNE-induced mechanical hypersensitivity. Using knockout mice, we demonstrated that PKCε is essential for the nociception recovery during 4-HNE-induced hypersensitivity. We also found that ALDH2 deficient knockin mice display increased 4-HNE-induced nociceptive behavior. As proof of concept, the use of a selective peptide activator of PKCε (ΨεHSP90), which favors PKCε translocation to mitochondria and activation of PKCε-ALDH2 axis, was sufficient to block 4-HNE-induced hypersensitivity in WT, but not in ALDH2-deficient mice. Similarly, ΨεHSP90 administration prevented mechanical hypersensitivity induced by endogenous production of 4-HNE after carrageenan injection. These findings provide evidence that selective activation of mitochondrial PKCε-ALDH2 axis is important to mitigate aldehyde-mediated pain in rodents, suggesting that ΨεHSP90 and small molecules that mimic it may be a potential treatment for patients with pain.