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DiscoveryProbe™ Ubiquitination-related Compounds Panel

DiscoveryProbe™ Ubiquitination-related Compounds Panel

产品编号:L1019
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Sample solution is provided at 25 µL, 10mM.

Click and Customize the Panel with your own choices of compounds/size/qtuanties/chemical forms etc.

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Related Biological Data

MG-132

Related Biological Data

MG-132

Related Biological Data

PR-619

Related Biological Data

PR-619

Related Biological Data

Carfilzomib
Synchronous trophozoites were treated with 100 nM or 1μ M carfilzomib for the indicated times followed by inhibitor wash out. Parasites were placed in fresh media, and proteasome activities of all samples were determined by MV151 labeling at 10 hr after inhibitor washout. Quantification of the putative β5 subunit labeling is shown in the graph below the gel image.

Related Biological Data

Carfilzomib (PR-171)

Signaling Pathway

Autophagy Research Area
DUB Compare Products
Proteasome Research Area

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
Download the Ubiquitination-related Compounds Panel - XLSX       Download the Ubiquitination-related Compounds Panel - SDF

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.