Inhibitor SourceBook™ Second Edition

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Apoptosis Necrosis Inhibitors Product Cat. No. Comments Size Price N Necrosis Inhibitor, IM-54 480060 2-(1H-Indol-3-yl)-3-pentylamino-maleimide A cell-permeable, mono-indolylmaleimide compound that selectively blocks oxidative stress-induced necrotic cell death (~3 mM IM-54 prevented ~50% cell death in HL60 cells exposed to 00 mM H 2 O 2 ). Does not offer protection against Etoposide- (Cat. No. 34 205) induced apoptosis or display antioxidant properties. N Necrostatin- 480065 5-(Indol-3-ylmethyl)-(2-thio-3-methyl)hydantoin; Nec-1; Necroptotic Inhibitor, Nec-1 A cell-permeable, potent, and selective blocker of necroptosis, a non-apoptotic necrotic cell-death pathway mediated by death-domain receptors (DRs), in vitro (EC 50 = 494 nM in FADD-deficient Jurkat cells treated with TNF-a). Also shown to offer neuroprotection in a mouse model of ischemic brain injury. Does not disrupt normal cellular physiology or exhibit any effects on apoptosis, autophagy, or oxidative stress-induced necrosis. N Necrostatin- , Inactive Control 480066 5-(Indol-3-ylmethyl)-2-thiohydantoin, Nec-1i A cell-permeable, analog of Nec- (Cat. No. 480065) that is devoid of antinecroptotic properties and serves as a suitable inactive control. inNovations Each inNovations newsletter presents the latest Novagen® products as used in research applications. • research articles from our scientists and our customers • answers from our technical service scientists • Novagen product usage in peer-reviewed journals • detailed product descriptions 5 mg $ 39 5 mg $82 5 mg $82 NEW products, NEW applications! 68 Orders Phone 800 854 34 7 Calbiochem • Inhibitor SourceBook Fax 800 776 0999 Web www.emdbiosciences.com/calbiochem
Calbiochem • Inhibitor SourceBook Cell Division/Cell Cycle/Cell Adhesion Cell Division/Cell Cycle/Cell Adhesion Cell Adhesion Inhibitors Cell adhesion is crucial in the formation and maintenance of coherent multi-cellular structures. Two major types of cell adhesion processes are seen in multicellular organisms: cell-cell adhesion where physical bonds are formed between adjacent cells, and cell-matrix adhesion where cells bind to adhesive proteins in the extracellular matrix (ECM). A wide variety of adhesion molecules have been identified that fall into four major categories: cadherins, immunoglobulin (Ig)-like adhesion molecules, integrins, and selectins. Cell adhesion proteins are often transmembrane receptors that have domains extending into both the extracellular space and the intracellular space. Cadherins are the main mediators of Ca 2+ -dependent cellcell adhesion. Cadherin-mediated cell-cell adhesion is accomplished by homophilic protein-protein interactions between two cadherin molecules on cell surface. This interaction is mediated by interactions between the His-Ala-Val domains and between Trp residues and hydrophobic pockets in amino-terminal cadherin domains. Cadherins are critical in segregating embryonic cells into tissues. The Ig superfamily of cell adhesion molecules (CAM) is expressed in a wide variety of cell types, including neurons, leukocytes, epithelial, and endothelial cells. Collectively, they function by both homophilic and heterophilic binding. Their heterogeneous expression pattern implicates them in diverse biological processes, such as brain development, immune responses, tissue sorting, morphogenesis, and development of the vascular network. They are characterized by the presence of one or more Ig-like domain in their extracellular region. In addition, the ectodomain of Ig-CAMs may contain various numbers of fibronectin type III (FNIII) repeats, which possess the Arg-Gly-Asp (RGD) cell attachment site. Neural cell adhesion molecules (N-CAMs) and the intercellular cell adhesion molecules (ICAMs) are the beststudied members of this family. Integrins belong to a superfamily of non-covalently bound heterodimeric membrane receptor glycoproteins. They are composed of a variable a-subunit of 150-170 kDa and a conserved 95 kDa b-subunit. Although both subunits are required for adhesion, the binding specificity primarily depends on the extracellular portion of the a-subunit. While generally classified as adhesion molecules, integrins also play an important role in signal transduction. Signal transduction through integrins occurs in two directions: from the extracellular microenvironment into the cell (outside-in signaling), and from the cytoplasm to the extracellular domain of the receptor (inside-out signaling). Among the signaling molecules involved in integrinmediated cell survival is focal adhesion kinase (FAK), which is activated following integrin ligation. It activates downstream survival pathways, such as PI 3-kinase, Akt, and MAPK/ERK. In response to specific stimuli, integrins that are generally diffused over the cell surface cluster in focal contacts. Their combined affinities create a region with sufficient adhesive capacity to adhere to the ECM. This allows cells to bind to a large numbers of matrix molecules simultaneously while still maintaining their ability to explore their environment. Selectins are expressed primarily on leukocytes and endothelial cells. They play an important role in host defense mechanisms. In contrast to other CAMs, selectins bind to carbohydrate ligands. Hence, the resulting binding forces are relatively weak. This allows selectin-mediated interactions between leukocytes and endothelial cells and promotes rolling of the leukocytes along the endothelium. L-selectins are expressed on most leukocytes, E-selectins are inducible on vascular endothelium upon stimulation with cytokines, and P-selectins are found on activated platelets and vascular endothelium. Dysregulation of several CAMs, particularly the Ig- CAMs, has been linked to tumor progression and metastasis, making them a suitable target for therapeutic intervention. Also, increased expression of CAMs on the vascular endothelium is postulated to play an important role in atherogenesis. CAMs also play critical roles in the recruitment and migration of cells to sites of inflammation. Hence, these molecules have become targets for the development of drugs for treatment of cancer, inflammation, and autoimmune diseases. References: Cavallaro, U., and Christofori, G. 2004. Nat. Rev. Cancer 4, 8. Aplin, A.E., et al. 999. Curr. Opin. Cell Biol. 11, 737. Meredith, J.E., et al. 997. Trends Cell Biol. 7, 46. Ruoslahti, E., and Obrink, B. 996. Exp. Cell Res. 227, . Law, D.A., et al. 996. J. Biol. Chem. 271, 08 . Flores, M.E., et al. 996. Exp. Cell Res. 227, 40. More online... www.calbiochem.com/inhibitors/ca Technical Support Phone 800 628 8470 E-mail calbiochem@emdbiosciences.com 69
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Inhibitor SourceBook Second Editio
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Calbiochem • Inhibitor SourceBook
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Akt (Protein Kinase B) Inhibitors,
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Calmodulin-Dependent Protein Kinase
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Casein Kinase (CK) Inhibitors Casei
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Checkpoint Kinase Inhibitors Eukary
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Cyclin-Dependent Kinase (Cdk) Inhib
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Cyclin-Dependent Kinase (Cdk) Inhib
Page 19 and 20: 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 and 34: Phosphatidylinositol 3-Kinase (PI 3
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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: 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 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
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Matrix Metalloproteinase (MMP) Inhi
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Matrix Metalloproteinase Inhibitors
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Tissue Inhibitors of Matrix Metallo
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Protease Inhibitors The proper func
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Protease Inhibitors, continued Calb
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Protease Inhibitors, continued Calb
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Protease Inhibitors, continued Sele
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Protease Inhibitor Cocktails, conti
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N Animal-Free Protease Inhibitor Co
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Proteasome and Ubiquitination Pathw
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Transmembrane receptors of various
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Angiotensin-Converting Enzyme (ACE)
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ATPase Inhibitors, continued Calbio
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Inhibitors of Glycoprotein Processi
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Heat Shock Protein Inhibitors Heat
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Inhibitors of Mitochondrial Functio
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NF-kB Activation Inhibitors NF-kB,
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NF-kB Activation Inhibitors, contin
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Phosphodiesterase (PDE) Inhibitors
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Plasminogen Activator Inhibitors Ti
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Protein Synthesis Inhibitors, conti
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Sonic Hedgehog Signaling Inhibitors
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Why can’t I make serial dilutions
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Calpastatin, Human, Recombinant, Do
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InSolution Microcystin-LR, Microcys
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RNA Polymerase III Inhibitor ......
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324875 ............................
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Trademarks CALBIOCHEM®
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Your #1 Resource for Inhibitors! We
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