DiscoveryProbe™ Ubiquitination-related Compounds Panel

Compound Panel Contents

Catalog No.	Product Name	Summary	Targets	CAS Number	Smiles
A8544	Wortmannin	PI3K inhibitor,selective and irreversible	Ubiquitination|Autophagy	19545-26-7	O=C1[C@](C([H])([H])[C@@]2([H])OC(C([H])([H])[H])=O)(C([H])([H])[H])[C@](C([H])([H])C1([H])[H])([H])C(C3=O)=C2[C@]4(C([H])([H])[H])C5=C3OC([H])=C5C(O[C@]4([H])C([H])([H])OC([H])([H])[H])=O
A8883	SAR405	Selective ATP-competitive inhibitor of Vps34	Ubiquitination|Autophagy	1523406-39-4	C[C@H]1N(C(N=C2N3CC[C@@H](C(F)(F)F)N2CC4=CN=CC(Cl)=C4)=CC3=O)CCOC1
A8212	PR-619	Deubiquitylating enzymes (DBUs) inhibitor	Ubiquitination|DUB	2645-32-1	C1=C(C(=NC(=C1SC#N)N)N)SC#N
B2168	NMS-873	VCP/p97 inhibitor,selective and allosteric	Ubiquitination|p97	1418013-75-8	CC1=C(C=CC(=C1)OCC2=NN=C(N2C3=CN=CC=C3)SC4CCCC4)C5=CC=C(C=C5)S(=O)(=O)C
A1933	Carfilzomib (PR-171)	Proteasome inhibitor,epoxomicin analog	Ubiquitination|Proteasome	868540-17-4	CC(C)CC(C(=O)C1(CO1)C)NC(=O)C(CC2=CC=CC=C2)NC(=O)C(CC(C)C)NC(=O)C(CCC3=CC=CC=C3)NC(=O)CN4CCOCC4
A2585	MG-132	Proteasome inhibitor, cell permeable and reversible	Ubiquitination|Proteasome	133407-82-6	CC(C)CC(C=O)NC(=O)C(CC(C)C)NC(=O)C(CC(C)C)NC(=O)OCC1=CC=CC=C1
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Advantages

• Available in stock with overnight delivery and free shipping over $500
• Cost-effective and competitive price to save your findings
• Potent, selective and cell-permeable in inhibiting or activating target molecules
• Diverse in chemical structure and route of administration (oral/i.m/i.v injection etc.)
• Detailed files describing potency, selectivity and applications etc.
• Supported by published data from top peer-reviewed journals
• Guaranteed high quality with NMR and HPLC validation

产品描述
A wide range of well-characterized bioactive molecules that covers various targets related to ubiquitination, including autophagy, proteasome and p97 etc. Facilitate your research towards the insights of cancer, diabetes, neurodegenerative and cardiovascular diseases etc. Applicable in cellular assays, animal models and drug screenings etc.
References
1. Amm I, Sommer T, Wolf DH. Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim Biophys Acta. 2014 Jan;1843(1):182-96. 
Abstract 
Misfolded proteins are mostly recognized by chaperones on the basis of their exposed hydrophobic patches and, if unable to refold them to their native state, are targeted to proteolytic pathways. A major task of this quality control system is the specific recognition and separation of the misfolded from the correctly folded protein species and the folding intermediates, respectively, In this review we focus on the recognition process and subsequent degradation of misfolded proteins via the ubiquitin-proteasome system in the different cell compartments of eukaryotic cells.
2. Boyd-Tressler A, Penuela S, Laird DW, Dubyak GR. Chemotherapeutic drugs induce ATP release via caspase-gated pannexin-1 channels and a caspase/pannexin-1-independent mechanism. J Biol Chem. 2014 Sep 26;289(39):27246-63. 
Abstract 
Diverse pro-apoptotic drugs induced functional activation of Panx1 channels via caspase-3-mediated cleavage of the Panx1 autoinhibitory C-terminal domain. Chemotherapeutic drugs also activated an alternative caspase- and Panx1-independent pathway for ATP release from Jurkat cells in the presence of benzyloxycarbonyl-VAD. These results identify chemotherapy-activated pannexin-1 channels and ATP release as possible mediators of paracrine interaction between dying tumor cells and the effector leukocytes that mediate immunogenic anti-tumor responses.