目录号 | 产品详情 | 靶点 | |
---|---|---|---|
TN1136 | LDL Calcium Channel PKC | ||
Procyanidin A1 (Proanthocyanidin A1) 是一种原花青素二聚体,具有抗过敏作用,可抑制蛋白激酶 C 激活下游脱粒或 RBL-213 细胞内部储存的 Ca2+流入。 | |||
T81449 | PKC | ||
PKC-ε translocation inhibitor peptide,作为一种特定的PKC-ε易位抑制剂,能够特异性地调控FcγR介导的调理珠内化速率,而对FcαR运输不产生影响。 | |||
T3S1416 | Apoptosis PKC | ||
Decursin (Decursinol angelate) 是一种细胞毒性剂,是一种来自朝鲜当归根的有效蛋白激酶 C 激活剂。它通过 Hippo/YAP 信号通路抑制 HepG2 细胞的生长。它通过下调 CXCR7 表达来抑制胃癌中的肿瘤生长,迁移和侵袭。 | |||
T3375 | Apoptosis PARP Antibacterial PKC p53 HSV | ||
Verbascoside (Kusaginin) 是从Lantana camara 中得到的糖苷类物质,是具有ATP 竞争性的PKC 抑制剂,IC50值为 25 µM,它还有抗炎,抗肿瘤,抗神经性疼痛等作用。 | |||
T14069 | CaMK Casein Kinase PKA PKC | ||
A-3 hydrochloride 是一种细胞可渗透的、可逆的、ATP 竞争性非选择性拮抗剂。它抑制 PKA 、酪蛋白激酶 II 和肌球蛋白轻链激酶,Ki 值分别为4.3 µM、5.1 µM 和7.4 µM。它还抑制 PKC 和酪蛋白激酶 I 的活性,Ki 分别为 47 µM 和 80 µM。 | |||
T6513 | PDGFR PKC | ||
Bisindolylmaleimide I (GF109203X) 是一种有效且高度选择性的蛋白激酶 C(PKC) 抑制剂,Ki 值为 14 nM。 | |||
T7792 | Endogenous Metabolite PKC | ||
Hispidin 是来自裂蹄木层孔菌的酚类天然产物,是一种 PKC 抑制剂,具有很强的抗氧化、抗癌、抗糖尿病和抗痴呆作用。 | |||
TN1299 | PI3K CDK PKC | ||
Desmethylglycitein (6,7,4'-Trihydroxyisoflavone) 是大豆中苷元的代谢产物,具有抗氧化性和抗癌活性。它是蛋白激酶 C(PKC)α 的直接抑制剂,抑制正常人皮肤成纤维细胞中的太阳紫外线诱导的基质金属蛋白酶1。它在体内直接结合CDK1和CDK2,抑制 CDK1 和 CDK2 活性。 | |||
T17019 | GSK-3 JAK PKC | ||
TCS 21311 (NIBR3049) 是一种高选择性JAK3抑制剂,IC50为 8 nM,它的选择性是 JAK1、JAK2 和 TYK2 的100倍以上,还抑制PKCα、PKCθ和GSK3β,IC50值分别为 13、68 和 3 nM。 | |||
T3689 | PKC | ||
Ruboxistaurin hydrochloride (LY 333531 hydrochloride) 是蛋白激酶 C(PKC) 的同工酶选择性抑制剂,竞争性且可逆地抑制 PKCβI 和 PKCβII,IC50 值分别为 4.7 和 5.9 nM。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-04456 | PKC nu Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Serine/threonine-protein kinase D3, also known as Protein kinase C nu type, Protein kinase EPK2, PRKD3, EPK2 and PRKCN, is a cytoplasm and membrane protein that belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family and PKD subfamily. PRKD3 / PRKCN contains one PH domain, two phorbol-ester/DAG-type zinc fingers and one protein kinase domain. Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. They also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role. PRKD3 / PRKCN converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in resistance to oxidative stress. PRKD3 / PRKCN is activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester with high affinity and mediate translocation to the cell membrane. Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC relieves auto-inhibition by the PH domain. PRKD3 / PRKCN can be activated rapidly by the agonists of G protein-coupled receptors. It resides in both cytoplasm and nucleus, and its nuclear accumulation is found to be dramatically enhanced in response to its activation. PRKD3 / PRKCN can also be activated after B-cell antigen receptor (BCR) engagement, which requires intact phospholipase C gamma and the involvement of other PKC family members.
|
|||||
TMPY-04455 | PKC iota Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Protein kinase C iota type, also known as Atypical protein kinase C-lambda/iota, aPKC-lambda/iota and PRKCI, is a cytoplasm, membrane and nucleus protein which belongs to the protein kinase superfamily, AGC Ser/Thr protein kinase family and PKC subfamily. PRKCI contains one AGC-kinase C-terminal domain, one OPR domain, one phorbol-ester/DAG-type zinc finger and one protein kinase domain. PRKCI is predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. It is highly expressed in non-small cell lung cancers. PRKCI is a calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. It may play a role in the secretory response to nutrients. PRKCI is involved in cell polarization processes and the formation of epithelial tight junctions. It is implicated in the activation of several signaling pathways including Ras, c-Src and NF-kappa-B pathways. PRKCI functions in both pro- and anti-apoptotic pathways. It functions in the RAC1/ERK signaling required for transformed growth. PRKCI plays a role in microtubule dynamics through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). PRKCI might be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion.
|
|||||
TMPJ-01261 | PPP1R14A Protein, Human, Recombinant (His) | Human | E. coli | ||
Protein Phosphatase 1 Regulatory Subunit 14A (PPP1R14A) belongs to the PP1 inhibitor family. PPP1R14A is mapped to chromosome 19q13.13-q13.2. PPP1R14A binds directly to protein kinase C and casein kinase I. Meantime, PPP1R14A is a phosphorylation-dependent inhibitor of smooth muscle myosin phosphatase. PPP1R14A is the inhibitor of PPP1CA. When phosphorylated, PPP1R14A has over 1000-fold higher inhibitory activity, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. In addition, inhibition of PPP1R14A also enhances contraction of smooth muscle in the absence of increment of intracellular Ca2+ concentration.
|
|||||
TMPY-00808 | FKBP12 Protein, Human, Recombinant (His) | Human | E. coli | ||
FKBP12 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 12.9 kDa and the accession number is P62942.
|
|||||
TMPY-04406 | Protein Kinase D2/PRKD2 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
Serine/threonine-protein kinase D2, also known as PRKD2 and PKD2, is a cytoplasm and membrane protein that belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family and PKD subfamily. PRKD2 / PKD2 is widely expressed. It contains one PH domain, two phorbol-ester/DAG-type zinc fingers and one protein kinase domain. PRKD2 / PKD2 is activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-71 and phosphorylation of Ser-76 by PKC relieves auto-inhibition by the PH domain. PRKD2 / PKD2 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress.
|
|||||
TMPH-01581 | KRT1 Protein, Human, Recombinant (His) | Human | E. coli | ||
May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK. KRT1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 69.9 kDa and the accession number is P04264.
|
|||||
TMPY-02761 | Rack1 Protein, Human, Recombinant (His & MBP) | Human | E. coli | ||
The scaffolding protein, Rack1, is a seven-WD-domain-containing protein that has been implicated in binding to integrin beta subunit cytoplasmic domains and to members of two kinase families (src and protein kinase C, PKC) that mediate integrin bidirectional signaling.Rack1 may link protein kinase C directly to integrins and participate in the regulation of integrin functions.Rack1 regulates the localization of an essential PCP protein and acts as a molecular switch to promote PCP signaling.
|
|||||
TMPJ-01307 | PACSIN1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Protein Kinase C and Casein Kinase Substrate in Neurons Protein 1 (PACSIN1) belongs to the PACSIN family. PACSIN1 contains one FCH domain and one SH3 domain. PACSIN1 is highly expressed in the brain and at lower leves in the heart, pancreas, and liver. PACSIN1 may play a role in vesicle formation and transport. PACSIN1 has been shown to interact with DNM1, PACSIN3, Huntingtin, and PACSIN2. In addition, PACSIN1 is phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC).
|
|||||
TMPY-01659 | SDPR Protein, Mouse, Recombinant (aa 2-180, His) | Mouse | E. coli | ||
Serum deprivation-response protein, also known as Phosphatidylserine-binding protein, Cavin-2 and SDPR, is a member of the PTRF / SDPR family. SDPR is highly expressed in heart and lung, and expressed at lower levels in brain, kidney, liver, pancreas, placenta, and skeletal muscle. SDPR is a new regulator of caveolae biogenesis. SDPR is up-regulated in asynchronously growing fibroblasts following serum deprivation but not following contact inhibition and Down-regulated during synchronous cell cycle re-entry. Caveolae are plasma membrane invaginations with a characteristic flask-shaped morphology. They function in diverse cellular processes, including endocytosis. Loss of SDPR causes loss of caveolae. SDPR binds directly to PTRF and recruits PTRF to caveolar membranes. Overexpression of SDPR, unlike PTRF, induces deformation of caveolae and extensive tubulation of the plasma membrane. SDPR overexpression results in increased caveolae size and leads to the formation of caveolae-derived tubules containing Shiga toxin. SDPR is a membrane curvature inducing component of caveolae, and that STB-induced membrane tubulation is facilitated by caveolae. Pleckstrin and SDPR are phosphorylated by protein kinase C (PKC), the interaction between pleckstrin and SDPR was shown to be independent of PKC inhibition or activation. SDPR may facilitate the translocation of nonphosphorylated pleckstrin to the plasma membrane in conjunction with phosphoinositides that bind to the C-terminal PH domain.
|
|||||
TMPH-02634 | TRIM63 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
|
|||||
TMPY-01187 | Rac1 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
RAC1 is a GTPase that belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. Two transcript variants encoding different isoforms have been found for RAC1 gene. RAC1 is a plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. RAC1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophage. RAC1 is essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. RAC1's isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction. Stat3 is an important transcription factor that regulates both proinflammatory and anti-apoptotic pathways in the heart. It forms a multiprotein complex with RAC1 and PKC in an H/R-dependent manner by expression of constitutively active Rac1 mutant protein, and by RNA silencing of RAC1. Selective inhibition of PKC with calphostin C produces a marked suppression of Stat3 S727 phosphorylation. The association of Stat3 with Rax1 occurs predominantly at the cell membrane, but also inside the nucleus, and occurs through the binding of the coiled-coil domain of Stat3 to the 54 NH(2)-terminal residues of RAC1. Transfection with a peptide comprising the NH(2)-terminal 17 amino acid residues of RAC1-dependent signaling pathways resulting in a physical association between Rac1 and Stat3 and the formation of a novel multiprotein complex with PKC.
|
|||||
TMPJ-00907 | GADD45A Protein, Human, Recombinant (His) | Human | E. coli | ||
Growth Arrest and DNA Damage-Inducible Protein GADD45 α (GADD45A) is a member of the GADD45 family. GADD45A can be induced by UV irradiation, X-rays, growth arrest and alkylating agents, of which can be mediated by some kinases other than PKC. GADD45A can interact with MAPK14, GADD45GIP1, PCNA. In T-cells, GADD45A functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity. GADD45A may affect PCNA interaction with some cell division protein kinase complexes, stimulating DNA excision repair in vitro and inhibits entry of cells into S phase.
|
|||||
TMPH-01271 | TRIM63 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
|
|||||
TMPH-03282 | TRIM63 Protein, Rat, Recombinant (His & Myc) | Rat | E. coli | ||
E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
|
|||||
TMPH-01623 | GBA Protein, Human, Recombinant (His & Myc & SUMO) | Human | E. coli | ||
Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose. Thereby, plays a central role in the degradation of complex lipids and the turnover of cellular membranes. Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation. Also plays a role in cholesterol metabolism. May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol. The short chain saturated C8:0-GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction. Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide. Finally, may also hydrolyze cholesteryl-beta-D-glucoside to produce D-glucose and cholesterol.
|
|||||
TMPY-02682 | NELL2 Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
A brain-enriched secreting signal peptide, NELL2, has been suggested to play multiple roles in the development, survival, and activity of neurons in the mammal. NELL2 is an abundant glycoprotein containing an EGF-like domain in the neural tissues where it has multiple physiological functions by interacting with protein kinase C (PKC). There are two different splicing variant forms of NELL2 identified so far. One is secreted NELL2 (sNELL2) which is a neuron-specific variant and the other is cytosolic NELL2 (cNELL2) which is a non-secreted splicing variant of NELL2. NELL2 is strongly expressed in the brain of adults and fetuses but only weakly in the fetal kidney.
|
|||||
TMPH-01624 | GBA Protein, Human, Recombinant | Human | E. coli | ||
Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose. Thereby, plays a central role in the degradation of complex lipids and the turnover of cellular membranes. Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation. Also plays a role in cholesterol metabolism. May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol. The short chain saturated C8:0-GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction. Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide. Finally, may also hydrolyze cholesteryl-beta-D-glucoside to produce D-glucose and cholesterol.
|
|||||
TMPH-02271 | BTK Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.
|
|||||
TMPH-01282 | ELAVL4 Protein, Human, Recombinant (His & Myc & SUMO) | Human | E. coli | ||
RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs. Plays a role in the regulation of mRNA stability, alternative splicing and translation. Binds to AU-rich element (ARE) sequences in the 3' untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS, CDKN1A and ACHE mRNA. Many of the target mRNAs are coding for RNA-binding proteins, transcription factors and proteins involved in RNA processing and/or neuronal development and function. By binding to the mRNA 3'UTR, decreases mRNA deadenylation and thereby contributes to the stabilization of mRNA molecules and their protection from decay. Also binds to the polyadenylated (poly(A)) tail in the 3'UTR of mRNA, thereby increasing its affinity for mRNA binding. Mainly plays a role in neuron-specific RNA processing by stabilization of mRNAs such as GAP43, ACHE and mRNAs of other neuronal proteins, thereby contributing to the differentiation of neural progenitor cells, nervous system development, learning and memory mechanisms. Involved in the negative regulation of the proliferative activity of neuronal stem cells and in the positive regulation of neuronal differentiation of neural progenitor cells. Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone of the hippocampus by binding to and stabilizing SATB1 mRNA. Binds and stabilizes MSI1 mRNA in neural stem cells. Exhibits increased binding to ACHE mRNA during neuronal differentiation, thereby stabilizing ACHE mRNA and enhancing its expression. Protects CDKN1A mRNA from decay by binding to its 3'-UTR. May bind to APP and BACE1 mRNAS and the BACE1AS lncRNA and enhance their stabilization. Plays a role in neurite outgrowth and in the establishment and maturation of dendritic arbors, thereby contributing to neocortical and hippocampal circuitry function. Stabilizes GAP43 mRNA and protects it from decay during postembryonic development in the brain. By promoting the stabilization of GAP43 mRNA, plays a role in NGF-mediated neurite outgrowth. Binds to BDNF long 3'UTR mRNA, thereby leading to its stabilization and increased dendritic translation after activation of PKC. By increasing translation of BDNF after nerve injury, may contribute to nerve regeneration. Acts as a stabilizing factor by binding to the 3'UTR of NOVA1 mRNA, thereby increasing its translation and enhancing its functional activity in neuron-specific splicing. Stimulates translation of mRNA in a poly(A)- and cap-dependent manner, possibly by associating with the EIF4F cap-binding complex. May also negatively regulate translation by binding to the 5'UTR of Ins2 mRNA, thereby repressing its translation. Upon glucose stimulation, Ins2 mRNA is released from ELAVL4 and translational inhibition is abolished. Also plays a role in the regulation of alternative splicing. May regulate alternative splicing of CALCA pre-mRNA into Calcitonin and Calcitonin gene-related peptide 1 (CGRP) by competing with splicing regulator TIAR for binding to U-rich intronic sequences of CALCA pre-mRNA.
|