Inhibitor SourceBook™ Second Edition

More documents

Recommendations

Info

Phosphorylation/Dephosphorylation Phosphatidylinositol 3-Kinase (PI 3-kinase) Inhibitors, continued Product Cat. No. Comments Size Price N PI 3-Kg Inhibitor II 528108 5-(2,2-Difluoro-benzo[1,3]dioxol-5-ylmethylene)-thiazolidine-2,4-dione A cell-permeable thiazolidinedione compound that acts as a potent and ATP-competitive inhibitor of PI 3-Kg (K i = 80 nM; IC 50 = 250 nM). Exhibits great selectivity over PI 3-Ka (IC50 = 4.5 µM), PI 3-Kb and d (IC 50 > 20 µM), and shows little effect towards a large panel of receptors, unrelated enzymes, ion channels, and 38 commonly studied kinases. Quercetin, Dihydrate 551600 (3,3´,4´,5,7-Pentahydroxyflavone) An inhibitor of PI 3-kinase (IC 50 = 3.8 mM) and phospholipase A 2 (IC 50 = 2 mM). Also inhibits mitochondrial ATPase, phosphodiesterases, and PKC. Wortmannin 681675 (KY 12420) A fungal metabolite that acts as a potent, selective, cell-permeable and irreversible inhibitor of PI 3-kinase in purified preparations and cytosolic fractions (IC 50 = 5 nM). Blocks the catalytic activity of PI 3-kinase without affecting the upstream signaling events. Call us or visit our website 5 mg $ 35 00 mg $33 mg $76 www.calbiochem.com/kinasekits 32 Orders Phone 800 854 34 7 Calbiochem • Inhibitor SourceBook Fax 800 776 0999 Web www.emdbiosciences.com/calbiochem
Calbiochem • Inhibitor SourceBook Phosphorylation/Dephosphorylation Protein Kinase A (PKA; cAMP-Dependent Protein Kinase) Inhibitors The cAMP-dependent protein kinase (protein kinase A; PKA) pathway is one of the most versatile signaling pathways in eukaryotic cells. Various extracellular signals converge on this signaling pathway through ligand binding to G protein-coupled receptors. Hence, the PKA pathway is tightly regulated at several levels to maintain specificity in the multitude of signal inputs. PKA is composed of two regulatory and two catalytic subunits. In the holoenzyme, the regulatory subunits are bound to the active site of the catalytic subunits, inactivating them. Binding of cAMP to the regulatory subunits causes a conformational change that releases and activates the two catalytic subunits. The active catalytic subunits can then phosphorylate serine and/or threonine residues on the substrates in the cytosol and in the nucleus. When the levels of cAMP begin to fall, the regulatory subunits regain their affinity towards the catalytic subunits and form the inactive holoenzyme. If cAMP levels remain persistently elevated, many cells change their behavior and may either differentiate, proliferate, or undergo apoptosis. PKA holoenzyme exists in two forms, type I and type II. They contain identical catalytic subunits; however, their regulatory subunits differ (RI or RII dimer). Type I holoenzyme is predominantly cytosolic, whereas type II holoenzyme is compartmentalized to subcellular organelles via specific anchoring proteins. The turnover rate of free type I regulatory subunit is significantly higher than that of type II subunits. When free catalytic subunit is microinjected into the cytoplasm of intact cells, it migrates to the nucleus, whereas the free regulatory subunit remains only in the cytoplasm following microinjection. When both subunits are co-injected, the regulatory subunit blocks the nuclear migration of the catalytic subunit. CREB is a major nuclear target for the catalytic subunit that binds to cAMP response elements (CREs) in the promoter regions of cAMP-responsive genes. Phosphorylation of CREB proteins alters their ability to form dimers and to interact with CREs. References: Protein Kinase A (PKA; cAMP-Dependent Protein Kinase) Inhibitors Skålhegg, B.S. et al. 2005. Curr. Drug Targets. 6, 655. Tasken, K, and Aandahl, E.M. 2004. Physiol. Rev. 84, 37. Taylor, S.S., et al. 2004. Biochim. Biophys. Acta 1697, 259. Skålhegg, B.S., and Tasken, K. 2000. Front. Biosci. 5, 678. Spaulding, S.W. 993. Endocrine Rev. 14, 632. Product Cat. No. Comments Size Price A3, Hydrochloride 100122 [N-(2-Aminoethyl)-5-chloronaphthalene-1-sulfonamide, HCl] A shorter alkyl chain derivative of W-7 (Cat. No. 68 629) that inhibits PKA (K i = 4.3 mM),) casein kinase I (K i = 80 mM), casein kinase II (K i = 5. mM), MLCK (K i = 7.4 mM), PKC (K i = 47 mM), and PKG (K i = 3.8 mM). Adenosine 3´,5´-cyclic Monophosphorothioate, Rp-Isomer, Triethylammonium Salt Adenosine 3´,5´-cyclic Monophosphorothioate, 8-Bromo-, Rp-Isomer, Sodium Salt Adenosine 3´,5´-cyclic Monophosphorothioate, 8-Bromo-2´monobutyryl-, Rp- Isomer, Sodium Salt Adenosine 3´,5´-cyclic Monophosphorothioate, 8-Chloro-, Rp-Isomer, Sodium Salt More online... www.calbiochem.com/inhibitors/PKA 116814 (Adenosine 3´,5´-cyclic Phosphorothioate-Rp; Rp-cAMPS, TEA) A cell-permeable inhibitor of protein kinase A (K i = mM). Resistant to hydrolysis by phosphodiesterases. 116816 (Rp-8-Br-cAMPS, Na) A potent, cell-permeable, metabolically-stable cAMP antagonist that inhibits cAMPdependent protein kinase and shows preference for PKA type I. More lipophilic than cAMP antagonist Rp-cAMPS (Cat. No. 68 4). 116813 (Rp-8-Br-MB-cAMPS, Na) An inhibitor of PKA that also inhibits the basal Ca 2+ -currents in smooth muscle. Reported to block the excitatory effect of 8-Bromo-cGMP (Cat No. 68 6). More lipophilic and cell-permeable than Rp-8-Br-cAMPS. 116819 (Rp-8-Cl-cAMPS, Na) A cell-permeable, metabolically stable cAMP analog that acts as a competitive inhibitor of PKA. Preferentially inhibits type I PKA (IC 50 ~50 mM). 0 mg $90 5 mmol $ 92 5 mmol $422 5 mmol $524 5 mmol $486 Technical Support Phone 800 628 8470 E-mail calbiochem@emdbiosciences.com 33
Page 1 and 2: Inhibitor SourceBook Second Editio
Page 3 and 4: Calbiochem • Inhibitor SourceBook
Page 7 and 8: Akt (Protein Kinase B) Inhibitors,
Page 9 and 10: Calmodulin-Dependent Protein Kinase
Page 11 and 12: Casein Kinase (CK) Inhibitors Casei
Page 13 and 14: Checkpoint Kinase Inhibitors Eukary
Page 15 and 16: Cyclin-Dependent Kinase (Cdk) Inhib
Page 21 and 22: Glycogen Synthase Kinase-3 (GSK-3)
Page 23 and 24: Glycogen Synthase Kinase Inhibitors
Page 25 and 26: c-Jun N-Terminal Kinase (JNK/SAP Ki
Page 27 and 28: Mitogen-Activated Protein (MAP) Kin
Page 29 and 30: MAP Kinase Inhibitors, continued Ca
Page 31 and 32: Myosin Light Chain Kinase (MLCK) In
Page 33: Phosphatidylinositol 3-Kinase (PI 3
Page 37 and 38: Protein Kinase A (PKA; cAMP-Depende
Page 39 and 40: Isozyme Specificities of Selected P
Page 41 and 42: Protein Kinase C (PKC) Inhibitors,
Page 47 and 48: Protein Tyrosine Kinase (PTK) Inhib
Page 57 and 58: Raf Kinase Inhibitors Raf kinases a
Page 59 and 60: Rho Kinase (ROCK) Inhibitors, conti
Page 61 and 62: Protein Phosphatase Inhibitors Calb
Page 63 and 64: Protein Phosphatase Inhibitors, con
Page 65 and 66: Apoptosis Caspase Inhibitors Activa
Page 67 and 68: Caspase Inhibitors, continued Produ
Page 69 and 70: Other Selected Inhibitors of Apopto
Page 73 and 74: DNA Methyltransferase Inhibitors DN
Page 75 and 76: Histone Acetylase and Deacetylase I
Page 77 and 78: Related Products Histone Deacetylas
Page 79 and 80: Nuclear Import/Export Inhibitors, c
Page 83 and 84: Telomerase Inhibitors, continued Ca
Page 85 and 86:
Topoisomerase Related Inhibitors, c
Page 87 and 88:
Lipid Signaling Acetyl-CoA Carboxyl
Page 89 and 90:
Cyclooxygenase (COX) Inhibitors, co
Page 91 and 92:
HMG-CoA (3-Hydroxy-3-Methylglutaryl
Page 93 and 94:
Lipoxygenase (LOX) Inhibitors Lipox
Page 95 and 96:
Phospholipase Inhibitors Several si
Page 97 and 98:
Sphingomyelinase Inhibitors Ceramid
Page 99 and 100:
Amyloidogenesis Inhibitors Calbioch
Page 101 and 102:
Secretase Inhibitors Deposition of
Page 103 and 104:
Secretase Inhibitors Calbiochem •
Page 105 and 106:
Calbiochem • Inhibitor SourceBook
Page 107 and 108:
Glutathione S-Transferase (GST) Inh
Page 109 and 110:
Guanylate Cyclase Inhibitors, conti
Page 111 and 112:
Characteristics of various forms of
Page 113 and 114:
Nitric Oxide Synthase (NOS) Inhibit
Page 115 and 116:
Proteases Anthrax Lethal Factor (LF
Page 117 and 118:
the ratio of active (76 kDa) to ina
Page 119 and 120:
Collagenase Inhibitors (Also see Ma
Page 121 and 122:
Matrix Metalloproteinase (MMP) Inhi
Page 123 and 124:
Matrix Metalloproteinase Inhibitors
Page 125 and 126:
Tissue Inhibitors of Matrix Metallo
Page 127 and 128:
Protease Inhibitors The proper func
Page 129 and 130:
Protease Inhibitors, continued Calb
Page 131 and 132:
Protease Inhibitors, continued Calb
Page 133 and 134:
Protease Inhibitors, continued Sele
Page 135 and 136:
Protease Inhibitor Cocktails, conti
Page 137 and 138:
N Animal-Free Protease Inhibitor Co
Page 139 and 140:
Proteasome and Ubiquitination Pathw
Page 141 and 142:
Transmembrane receptors of various
Page 143 and 144:
Angiotensin-Converting Enzyme (ACE)
Page 145 and 146:
ATPase Inhibitors, continued Calbio
Page 147 and 148:
Calbiochem • Inhibitor SourceBook
Page 149 and 150:
Inhibitors of Glycoprotein Processi
Page 151 and 152:
Heat Shock Protein Inhibitors Heat
Page 153 and 154:
Inhibitors of Mitochondrial Functio
Page 155 and 156:
NF-kB Activation Inhibitors NF-kB,
Page 157 and 158:
NF-kB Activation Inhibitors, contin
Page 159 and 160:
Phosphodiesterase (PDE) Inhibitors
Page 161 and 162:
Plasminogen Activator Inhibitors Ti
Page 163 and 164:
Protein Synthesis Inhibitors, conti
Page 165 and 166:
Sonic Hedgehog Signaling Inhibitors
Page 167 and 168:
Why can’t I make serial dilutions
Page 169 and 170:
Calpastatin, Human, Recombinant, Do
Page 171 and 172:
InSolution Microcystin-LR, Microcys
Page 173 and 174:
RNA Polymerase III Inhibitor ......
Page 175 and 176:
324875 ............................
Page 177 and 178:
Trademarks CALBIOCHEM®
Page 179 and 180:
Your #1 Resource for Inhibitors! We
show all

Inhibitor SourceBook™ Second Edition

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?