cIAP1 ligand 1 - CAS 2095244-42-9

cIAP1 ligand 1 is the LCL161 derivative based IAP ligand. cIAP1 ligand 1 can be connected to the ABL ligand for protein by a linker to form SNIPER.

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Molecular Formula
C31H42N4O6S
Molecular Weight
598.75

cIAP1 ligand 1

    • Specification
      • Solubility
        10 mM in DMSO
        Storage
        Please store the product under the recommended conditions in the Certificate of Analysis.
        Shipping
        Room temperature in continental US; may vary elsewhere
        Synonyms
        cIAP1 ligand 1; E3 ligase Ligand 12
    • Properties
      • Canonical SMILES
        OC1=CC(C(C2=CSC([C@H]3N(CCC3)C([C@@H](NC([C@@H](N(C(OC(C)(C)C)=O)C)C)=O)C4CCCCC4)=O)=N2)=O)=CC=C1
    • Reference Reading
      • 1. Bivalent Ligands for Protein Degradation in Drug Discovery
        Marcel Scheepstra, Koen F W Hekking, Luc van Hijfte, Rutger H A Folmer Comput Struct Biotechnol J. 2019 Jan 25;17:160-176.doi: 10.1016/j.csbj.2019.01.006.eCollection 2019.
        Targeting the "undruggable" proteome remains one of the big challenges in drug discovery. Recent innovations in the field of targeted protein degradation and manipulation of the ubiquitin-proteasome system open up new therapeutic approaches for disorders that cannot be targeted with conventional inhibitor paradigms. Proteolysis targeting chimeras (PROTACs) are bivalent ligands in which a compound that binds to the protein target of interest is connected to a second molecule that binds an E3 ligase via a linker. The E3 protein is usually either Cereblon or Von Hippel-Lindau. Several examples of selective PROTAC molecules with potent effect in cells and in vivo models have been reported. The degradation of specific proteins via these bivalent molecules is already allowing for the study of biochemical pathways and cell biology with more specificity than was possible with inhibitor compounds. In this review, we provide a comprehensive overview of recent developments in the field of small molecule mediated protein degradation, including transcription factors, kinases and nuclear receptors. We discuss the potential benefits of protein degradation over inhibition as well as the challenges that need to be overcome.
        2. IRF-1 inhibits NF-κB activity, suppresses TRAF2 and cIAP1 and induces breast cancer cell specific growth inhibition
        Michaele J Armstrong, Michael T Stang, Ye Liu, Jin Yan, Eva Pizzoferrato, John H Yim Cancer Biol Ther. 2015;16(7):1029-41.doi: 10.1080/15384047.2015.1046646.
        Interferon Regulatory Factor (IRF)-1, originally identified as a transcription factor of the human interferon (IFN)-β gene, mediates tumor suppression and may inhibit oncogenesis. We have shown that IRF-1 in human breast cancer cells results in the down-regulation of survivin, tumor cell death, and the inhibition of tumor growth in vivo in xenogeneic mouse models. In this current report, we initiate studies comparing the effect of IRF-1 in human nonmalignant breast cell and breast cancer cell lines. While IRF-1 in breast cancer cells results in growth inhibition and cell death, profound growth inhibition and cell death are not observed in nonmalignant human breast cells. We show that TNF-α or IFN-γ induces IRF-1 in breast cancer cells and results in enhanced cell death. Abrogation of IRF-1 diminishes TNF-α and IFN-γ-induced apoptosis. We test the hypothesis that IRF-1 augments TNF-α-induced apoptosis in breast cancer cells. Potential signaling networks elicited by IRF-1 are investigated by evaluating the NF-κB pathway. TNF-α and/or IFN-γ results in decreased presence of NF-κB p65 in the nucleus of breast cancer cells. While TNF-α and/or IFN-γ can induce IRF-1 in nonmalignant breast cells, a marked change in NF-κB p65 is not observed. Moreover, the ectopic expression of IRF-1 in breast cancer cells results in caspase-3, -7, -8 cleavage, inhibits NF-κB activity, and suppresses the expression of molecules involved in the NF-κB pathway. These data show that IRF-1 in human breast cancer cells elicits multiple signaling networks including intrinsic and extrinsic cell death and down-regulates molecules involved in the NF-κB pathway.
        3. Crosstalk between apoptosis, necrosis and autophagy
        Vassiliki Nikoletopoulou, Maria Markaki, Konstantinos Palikaras, Nektarios Tavernarakis Biochim Biophys Acta. 2013 Dec;1833(12):3448-3459.doi: 10.1016/j.bbamcr.2013.06.001.Epub 2013 Jun 13.
        Apoptosis and necrosis are the two major modes of cell death, the molecular mechanisms of which have been extensively studied. Although initially thought to constitute mutually exclusive cellular states, recent findings reveal cellular contexts that require a balanced interplay between these two modes of cellular demise. Several death initiator and effector molecules, signaling pathways and subcellular sites have been identified as key mediators in both processes, either by constituting common modules or alternatively by functioning as a switch allowing cells to decide which route to take, depending on the specific situation. Importantly, autophagy, which is a predominantly cytoprotective process, has been linked to both types of cell death, serving either a pro-survival or pro-death function. Here we review the recent literature that highlights the intricate interplay between apoptosis, necrosis and autophagy, focusing on the relevance and impact of this crosstalk in normal development and in pathology. This article is part of a Special Section entitled: Cell Death Pathways.
Bio Calculators
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L

* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2

* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O c22h30n40
g/mol
g
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