DiscoveryProbe™ Proteases/Proteasome-related Compounds Panel

Compound Panel Contents

Catalog No.	Product Name	Summary	Targets	CAS Number	Smiles
A2603	Calpain Inhibitor II, ALLM	Calpain inhibitor	Proteases/Proteasome|Calpains	136632-32-1	CC(C)CC(C(=O)NC(CC(C)C)C(=O)NC(CCSC)C=O)NC(=O)C
A8165	Q-VD(OMe)-OPh	Pan-caspase inhibitor	Proteases/Proteasome|Caspase		O=C(N[C@@H](C(C)C)C(N[C@@H](CC(OC)=O)C(COC1=C(F)C=CC=C1F)=O)=O)C2=NC3=CC=CC=C3C=C2
A2576	E-64	Cysteine protease inhibitor,irriversible	Proteases/Proteasome|Cathepsin	66701-25-5	CC(C)CC(C(=O)NCCCCN=C(N)N)NC(=O)C1C(O1)C(=O)O
A4005	RO4929097	γ secretase inhibitor	Proteases/Proteasome|Gamma Secretase	847925-91-1	CC(C)(C(=O)NCC(C(F)(F)F)(F)F)C(=O)NC1C2=CC=CC=C2C3=CC=CC=C3NC1=O
A3820	Simeprevir	Potent inhibitor of HCV NS3/4A protease	Proteases/Proteasome|HCV Protease	923604-59-5	COC1=CC=C(C(O[C@H]2CC(C(N(C)CCCC/C=C\[C@H]3C[C@@]3(C(NS(=O)(C4CC4)=O)=O)NC5=O)=O)[C@H]5C2)=CC(C6=NC(C(C)C)=CS6)=N7)C7=C1C
A8204	Lopinavir	HIV protease inhibitor,highly potent	Proteases/Proteasome|HIV Protease	192725-17-0	CC1=C(C(=CC=C1)C)OCC(=O)NC(CC2=CC=CC=C2)C(CC(CC3=CC=CC=C3)NC(=O)C(C(C)C)N4CCCNC4=O)O
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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 proteases/proteasome, including cathepsin, DUB and gamma secretase, MMP and HCV protease etc. Facilitate your research towards the insights of apoptosis, cell cycle, viral infection and immune response 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. Rodriguez DA, Weinlich R, Brown S, Guy C, Fitzgerald P, Dillon CP, Oberst A, Quarato G, Low J, Cripps JG, Chen T, Green DR. Characterization of RIPK3-mediated phosphorylation of the activation loop of MLKL during necroptosis. Cell Death Differ. 2016 Jan;23(1):76-88. 
Abstract 
The activation of MLKL occurs in a multimolecular complex, within this complex, RIPK3 phosphorylates the activation loop of MLKL, promoting conformational changes and allowing the formation of MLKL oligomers. Here we examine the role of each of these residues and found that the phosphorylation of Ser345 is critical for RIPK3-mediated necroptosis, Ser347 has a minor accessory role and Thr349 seems to be irrelevant. We demonstrate that the phosphorylation of Ser345 is not required for the interaction between RIPK3 and MLKL in the necrosome, but is essential for MLKL translocation, accumulation in the plasma membrane, and consequent necroptosis.