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BioAssay: AID 504511

Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compounds

Name: Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compounds. ..more
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 Tested Compounds
 Tested Compounds
All(2)
 
 
Inactive(2)
 
 
 Tested Substances
 Tested Substances
All(2)
 
 
Inactive(2)
 
 
 Related BioAssays
 Related BioAssays
AID: 504511
Data Source: The Scripps Research Institute Molecular Screening Center (TCELLCYTOX_INH_ABSORB_4XCC50_PAFAH2)
BioAssay Type: Panel, Confirmatory, Concentration-Response Relationship Observed
Depositor Category: NIH Molecular Libraries Probe Production Network, Assay Provider
BioAssay Version:
Deposit Date: 2011-03-21
Hold-until Date: 2011-10-06
Modify Date: 2011-10-06

Data Table ( Complete ):           View All Data
Tested Compounds:
Related Experiments
Show more
AIDNameTypeProbeComment
492956Fluorescence polarization-based primary biochemical high throughput screening assay to identify inhibitors of human platelet activating factor acetylhydrolase 2 (PAFAH2)Screening depositor-specified cross reference: Primary screen (PAFAH2 inhibitors in singlicate)
492969Summary of the probe development efforts to identify inhibitors of human platelet activating factor acetylhydrolase 2 (PAFAH2)Summary1 depositor-specified cross reference: Summary (PAFAH2 inhibitors)
493030Fluorescence polarization-based biochemical high throughput confirmation assay for inhibitors of human platelet activating factor acetylhydrolase 2 (PAFAH2)Screening depositor-specified cross reference: Primary screen (PAFAH2 inhibitors in triplicate)
463082Fluorescence polarization-based primary biochemical high throughput screening assay to identify inhibitors of the plasma platelet activating factor acetylhydrolase (pPAFAH)Screening same project related to Summary assay
504483Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: Fluorescence-based biochemical gel-based Activity-Based Protein Profiling (ABPP) counterscreen assay to assess selectivity against anti-target pPAFAH in vitroOther same project related to Summary assay
504486Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: LC-MS/MS assay to assess binding of compounds to active siteOther same project related to Summary assay
504491Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: Fluorescence-based biochemical gel-based Activity-Based Protein Profiling (ABPP) inhibition and selectivity to assess carbamate vs. triazole urea scaffoldOther same project related to Summary assay
504494Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: Fluorescence-based biochemical gel-based Activity-Based Protein Profiling (ABPP) IC50Confirmatory same project related to Summary assay
504495Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: fluorescence-based cell-based gel-based Activity-Based Protein Profiling (ABPP) inhibitionOther same project related to Summary assay
504496Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: fluorescence-based cell-based gel-based Activity-Based Protein Profiling (ABPP) IC50Confirmatory same project related to Summary assay
504513Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: Fluorescence-based biochemical gel-based Activity-Based Protein Profiling (ABPP) inhibition and selectivityOther same project related to Summary assay
504519Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: LC-MS-based cell-based SILAC Activity-Based Protein Profiling (ABPP) for PAFAH2Other same project related to Summary assay
504527Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: Fluorescence-based biochemical gel-based Activity-Based Protein Profiling (ABPP) general inhibition and selectivity of serine hydrolasesOther same project related to Summary assay
504531Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: Fluorescence-based biochemical gel-based Activity-Based Protein Profiling (ABPP) assay to assess selectivity against anti-target pPAFAH in situOther same project related to Summary assay
Description:
Source (MLPCN Center Name): The Scripps Research Institute Molecular Screening Center (SRIMSC)
Center Affiliation: The Scripps Research Institute (TSRI)
Assay Provider: Benjamin Cravatt, TSRI
Network: Molecular Libraries Probe Production Centers Network (MLPCN)
Grant Proposal Number: 1R01HL084366
Grant Proposal PI: Brian Bahnson, Univ. of Delaware, Benjamin Cravatt, TSRI
External Assay ID: TCELLCYTOX_INH_ABSORB_4XCC50_PAFAH2

Name: Late stage assay provider results from the probe development effort to identify inhibitors of PAFAH2: absorbance-based cell-based dose response assay to determine cytotoxicity of inhibitor compounds.

Description:

Oxidative stress has been implicated as an underlying inflammatory factor in several disease pathologies, including cancer, atherosclerosis, aging, and various neurodegenerative disorders (1-5). Phospholipids in particular are susceptible to oxidative damage, and (per)oxidized phospholipids can have deleterious effects, including disruption of membrane bilayers and production of toxic byproducts (4, 6-8). One hypothesized pathway for removal of oxidatively damaged species involves hydrolysis by phospholipase A2-type enzymes. Candidate hydrolytic enzymes include the platelet-activating factor acetylhydrolases (PAFAHs) (4,9). The initial role assigned to the PAFAHs was the hydrolysis of platelet activating factor (PAF) (10,11), a potent pro-inflammatory phospholipid signaling molecule (12), which plays a role in myriad physiological processes including inflammation, anaphylaxis, fetal development, and reproduction (4,13). The PAFAHs are subdivided into three classes: plasma (p)PAFAH, and intracellular types 1 and 2. In terms of sequence homology, pPAFAH and PAFAH2 are close homologs and show little similarity to type 1 enzymes. This project aims to develop specific inhibitors for pPAFAH and three counterscreen enzymes: PAFAH2, PAFAH1b2, and PAFAH1b3.

pPAFAH is associated with inflammatory pathways involved in atherosclerosis, asthma, anaphylactic shock, and other allergic reactions (14,15). Numerous studies have also linked increases in pPAFAH concentration and/or activity to an increased risk of various cardiovascular diseases (16,17); however, the biological function of pPAFAH in the development of coronary heart diseases is controversial, with both anti- and proinflammatory roles attributed to it (18,19). Dr. Bahnson and colleagues recently reported the first high-resolution crystal structure of pPAFAH (20), and would like to expand their studies to co-crystallize pPAFAH with substrate-mimetic inhibitors to further define the active site and substrate specificity of pPAFAH. While one selective pPAFAH inhibitor has been reported (21), its properties are not suitable for the proposed studies.

PAFAH2 has also been shown to play a role in inflammatory processes via hydrolysis of oxidized phospholipids. Over-expression of PAFAH2 has been shown to reduce oxidative stress-induced cell death (22,23) and to mediate repair of oxidative-stress induced tissue injury (4). The enzyme also undergoes N-terminal myristoylation and subsequent translocation to the membrane under conditions of oxidative stress (22,23). This evidence suggests that PAFAH2 functions as an important, and perhaps primary, antioxidant enzyme in certain tissues (4); however, its substrate specificity and pathway involvement are far from being fully elucidated. Currently no suitable inhibitors exist for co-crystallization or biochemical studies of PAFAH2.

Given the complex biology of the PAFAH enzymes, chemical tools capable of interrogating enzyme architecture and providing precise temporal control over PAFAH activity are necessary for complete characterization of patho/physiological roles of the PAFAHs in phospholipid metabolism and inflammatory disease processes. Towards that goal, we developed a HTS assay for inhibitor discovery for four PAFAH enzymes: pPAFAH, PAFAH2, PAFAH1b2, and PAFAH1b3, based on their reactivity with the serine-hydrolase-specific fluorophosphonate (FP) (24) activity-based protein profiling (ABPP) probe. This reactivity can be exploited for inhibitor discovery using a competitive-ABPP platform, whereby small molecule enzyme inhibition is assessed by the ability to out-compete ABPP probe labeling (25). Competitive ABPP has also been configured to operate in a high-throughput manner via fluorescence polarization readout, FluoPol-ABPP (26). Following the HTS campaign, top inhibitors for each enzyme will be characterized and medchem optimized with the goal of delivering key reagents for elucidating the biology of the PAFAH enzymes.

References:

1. Ames, B.N., Dietary carcinogens and anticarcinogens. Oxygen radicals and degenerative diseases. Science, 1983. 221(4617): p. 1256-64.
2. Halliwell, B. and J.M. Gutteridge, Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol., 1990. 186: p. 1-85.
3. Harman, D., The aging process. Proc. Natl. Acad. Sci. U. S. A., 1981. 78(11): p. 7124-8.
4. Kono, N., et al., Protection against oxidative stress-induced hepatic injury by intracellular type II platelet-activating factor acetylhydrolase by metabolism of oxidized phospholipids in vivo. J. Biol. Chem., 2008. 283(3): p. 1628-36.
5. Southorn, P.A. and G. Powis, Free radicals in medicine. II. Involvement in human disease. Mayo. Clin. Proc., 1988. 63(4): p. 390-408.
6. Kinnunen, P.K., On the principles of functional ordering in biological membranes. Chem. Phys. Lipids, 1991. 57(2-3): p. 375-99.
7. Uchida, K., 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog. Lipid Res., 2003. 42(4): p. 318-43.
8. Fruhwirth, G.O., A. Loidl, and A. Hermetter, Oxidized phospholipids: from molecular properties to disease. Biochim. Et Biophys. Acta, 2007. 1772(7): p. 718-36.
9. Nigam, S. and T. Schewe, Phospholipase A(2)s and lipid peroxidation. Biochim. Et Biophys. Acta, 2000. 1488(1-2): p. 167-81.
10. Blank, M.L., et al., A specific acetylhydrolase for 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (a hypotensive and platelet-activating lipid). J. Biol. Chem., 1981. 256(1): p. 175-8.
11. Farr, R.S., et al., Preliminary studies of an acid-labile factor (ALF) in human sera that inactivates platelet-activating factor (PAF). Clin. Immunol. Immunopathol., 1980. 15(3): p. 318-330.
12. Zimmerman, G.A., et al., The platelet-activating factor signaling system and its regulators in syndromes of inflammation and thrombosis. Crit. Care Med., 2002. 30(5 Suppl): p. S294-301.
13. Prescott, S.M., et al., Platelet-activating factor and related lipid mediators. Annu. Rev. Biochem., 2000. 69: p. 419-45.
14. Karasawa, K., et al., Plasma platelet activating factor-acetylhydrolase (PAF-AH). Prog. Lipid Res., 2003. 42(2): p. 93-114.
15. Leitinger, N., Oxidized phospholipids as triggers of inflammation in atherosclerosis. Mol. Nutr. Food Res., 2005. 49(11): p. 1063-71.
16. Anderson, J.L., Lipoprotein-associated phospholipase A2: an independent predictor of coronary artery disease events in primary and secondary prevention. Am. J. Cardiol., 2008. 101(12A): p. 23F-33F.
17. Sudhir, K., Clinical review: Lipoprotein-associated phospholipase A2, a novel inflammatory biomarker and independent risk predictor for cardiovascular disease. J. Clin. Endocrinol. Metab., 2005. 90(5): p. 3100-5.
18. Wilensky, R.L. and C.H. Macphee, Lipoprotein-associated phospholipase A(2) and atherosclerosis. Curr. Opin. Lipidol., 2009. 20(5): p. 415-20.
19. Karabina, S.A. and E. Ninio, Plasma PAF-acetylhydrolase: an unfulfilled promise? Biochim. Et Biophys. Acta, 2006. 1761(11): p. 1351-8.
20. Samanta, U. and B.J. Bahnson, Crystal structure of human plasma platelet-activating factor acetylhydrolase: structural implication to lipoprotein binding and catalysis. J. Biol. Chem., 2008. 283(46): p. 31617-24.
21. Blackie, J.A., et al., The identification of clinical candidate SB-480848: a potent inhibitor of lipoprotein-associated phospholipase A2. Bioorg. Med. Chem. Lett., 2003. 13(6): p. 1067-70.
22. Matsuzawa, A., et al., Protection against oxidative stress-induced cell death by intracellular platelet-activating factor-acetylhydrolase II. J. Biol. Chem., 1997. 272(51): p. 32315-20.
23. Marques, M., et al., Identification of platelet-activating factor acetylhydrolase II in human skin. J. Invest. Dermatol., 2002. 119(4): p. 913-9.
24. Jessani, N., et al., Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness. Proc. Natl. Acad. Sci. U. S. A., 2002. 99(16): p. 10335-40.
25. Leung, D., et al., Discovering potent and selective reversible inhibitors of enzymes in complex proteomes. Nat. Biotechnol., 2003. 21(6): p. 687-91.
26. Bachovchin, D.A., et al., Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes. Nat. Biotechnol., 2009. 27(4): p. 387-94.

Keywords:

late stage, late stage AID, assay provider, powders, platelet-activating factor acetylhydrolase, PAFAH, PAF-AH, plasma platelet-activating factor acetylhydrolase, pPAFAH, platelet-activating factor acetylhydrolase type II, PAFAH2, PAFAHII, cancer, inflammation, atherosclerosis, serine hydrolase, counterscreen, inhibitor, cytotoxicity, CC50, activity-based protein profiling, ABPP, gel-based ABPP, fluorophosphonate rhodamine, FP-Rh, BW5147, murine T cells, T cells, Scripps, Scripps Research Institute Molecular Screening Center, SRIMSC, Molecular Libraries Probe Production Centers Network, MLPCN
Panel Information
Assays (see Protocol for details)
PID§NameSubstancePanel TargetsDescription
ActiveInactive
1Assay 1: % Surviving cells, serum-free media2
2Assay 2: % Surviving cells, media plus FCS2

§ Panel component ID.
Protocol
Assay Overview:
The purpose of this assay is to determine cytotoxicity of inhibitor compounds belonging to the urea triazole scaffold. In this assay, BW5147-derived murine T-cells in either serum-free media (Assay 1) or media containing FCS (Assay 2) are incubated with test compounds, followed by determination of cell viability. The assay utilizes the WST-1 substrate which is converted into colorimetric formazan dye by the metabolic activity of viable cells. The amount of formed formazan directly correlates to the number of metabolically active cells in the culture. As designed, compounds that reduce cell viability will result in decreased absorbance of the dye. Compounds were tested in quadruplicate in a 7-point 1:5 dilution series starting at a nominal test concentration of 50 uM.
Protocol Summary:
This assay was started by dispensing BW5147-derived murine T cells in RPMI media (100 uL, 10E4 cells/well) into a 96-well plate. Both serum-free media (Assay 1) and media supplemented with fetal calf serum (FCS) (Assay 2) were tested. Compound (5 uL of 0-1000 uM in media containing 5% DMSO) was added to each well, giving final compound concentrations of 0-50 uM. Cells were incubated for 48 hours at 37 degrees Celsius in a humidified incubator and cell viability was determined by the WST-1 assay (Roche) according to manufacturer instructions.
The % cell viability for each well was then calculated as follows:
%_Cell_Viability = ( ABS_Test_Compound - MedianABS_Low_Control ) / ( MedianABS_High_Control - MedianABS_Low_Control ) * 100
Where:
Test_Compound is defined as wells containing cells in the presence of test compound.
High_Control is defined as wells containing cells treated with media only (no compound).
Low_Control is defined as wells containing no cells (media only).
For each test compound, percent cell viability was plotted against the log of the compound concentration. The CC50 is reported as ">X uM" (where X = the highest concentration tested for which >50% cell survival was observed).
PubChem Activity Outcome and Score:
The following applies to each panel in this assay:
Compounds with a CC50 value of less than 5 uM were considered active (cytotoxic). Compounds with a CC50 value greater than or equal to 5 uM were considered inactive (non-cytotoxic).
Any compound with a percent cell viability value < 50% at all test concentrations was assigned an activity score of zero. Any compound with a percent cell viability value >= 50% at any test concentration was assigned an activity score greater than zero.
Activity score was then ranked by the potency of the compounds with fitted curves, with the most potent compounds assigned the highest activity scores.
Assay 1 Score: The PubChem Activity Score range for inactive compounds is 100-1. There are no active compounds.
Assay 2 Score: The PubChem Activity Score range for inactive compounds is 0-0. There are no active compounds.
Overall Outcome and Score:
The overall outcome was active if the compound was active in at least one panel, inactive otherwise.
The overall score is 0 if the compound was inactive, otherwise the score is taken as the fraction of panels where the compound is active, multiplied by 100.
The PubChem Activity Score range for inactive compounds is 0-0. There are no active compounds.
List of Reagents:
BW5147-derived murine T-cells (provided by Assay Provider)
RPMI Media (CellGro 10-040-CV)
FCS (Omega Scientific, FB-01)
WST-1 reagent (Roche)
96-well plates (Corning)
Comment
This assay was performed by the assay provider with powder samples of compounds.
Categorized Comment - additional comments and annotations
From PubChem:
Assay Format: Cell-based
Assay Type: Toxicity
Assay Cell Type: BW5147
Result Definitions
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TIDNameDescriptionPID§Panel TargetsHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Outcome [Assay 1]One of Active, Inactive, or Not Tested1Outcome
2Score [Assay 1]The BioAssay activity ranking score1Integer
3CC50 [Assay 1]*The value for concentration at which 50% of surviving cells are observed; CC50 shown in micromolar.1FloatμM
4Cell Viability at 0.0032 uM [1, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate one.1Integer%
5Cell Viability at 0.0032 uM [2, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate two.1Integer%
6Cell Viability at 0.0032 uM [3, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate three.1Integer%
7Cell Viability at 0.0032 uM [4, Assay 1] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate four.1Integer%
8Cell Viability at 0.016 uM [1, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate one.1Integer%
9Cell Viability at 0.016 uM [2, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate two.1Integer%
10Cell Viability at 0.016 uM [3, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate three.1Integer%
11Cell Viability at 0.016 uM [4, Assay 1] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate four.1Integer%
12Cell Viability at 0.08 uM [1, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate one.1Integer%
13Cell Viability at 0.08 uM [2, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate two.1Integer%
14Cell Viability at 0.08 uM [3, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate three.1Integer%
15Cell Viability at 0.08 uM [4, Assay 1] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate four.1Integer%
16Cell Viability at 0.4 uM [1, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate one.1Integer%
17Cell Viability at 0.4 uM [2, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate two.1Integer%
18Cell Viability at 0.4 uM [3, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate three.1Integer%
19Cell Viability at 0.4 uM [4, Assay 1] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate four.1Integer%
20Cell Viability at 2 uM [1, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate one.1Integer%
21Cell Viability at 2 uM [2, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate two.1Integer%
22Cell Viability at 2 uM [3, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate three.1Integer%
23Cell Viability at 2 uM [4, Assay 1] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate four.1Integer%
24Cell Viability at 10 uM [1, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate one.1Integer%
25Cell Viability at 10 uM [2, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate two.1Integer%
26Cell Viability at 10 uM [3, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate three.1Integer%
27Cell Viability at 10 uM [4, Assay 1] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate four.1Integer%
28Cell Viability at 50 uM [1, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate one.1Integer%
29Cell Viability at 50 uM [2, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate two.1Integer%
30Cell Viability at 50 uM [3, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate three.1Integer%
31Cell Viability at 50 uM [4, Assay 1] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate four.1Integer%
32Outcome [Assay 2]One of Active, Inactive, or Not Tested2Outcome
33Score [Assay 2]The BioAssay activity ranking score2Integer
34Qualifier [CC50, Assay 2]Activity Qualifier identifies if the resultant data CC50 came from a fitted curve or was determined manually to be less than or greater than its listed CC50 concentration.2String
35CC50 [Assay 2]*The value for concentration at which 50% of surviving cells are observed; CC50 shown in micromolar.2FloatμM
36Cell Viability at 0.0032 uM [1, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate one.2Integer%
37Cell Viability at 0.0032 uM [2, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate two.2Integer%
38Cell Viability at 0.0032 uM [3, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate three.2Integer%
39Cell Viability at 0.0032 uM [4, Assay 2] (0.0032μM**)Value of % Surviving cells at 0.0032 uM inhibitor concentration; replicate four.2Integer%
40Cell Viability at 0.016 uM [1, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate one.2Integer%
41Cell Viability at 0.016 uM [2, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate two.2Integer%
42Cell Viability at 0.016 uM [3, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate three.2Integer%
43Cell Viability at 0.016 uM [4, Assay 2] (0.016μM**)Value of % Surviving cells at 0.016 uM inhibitor concentration; replicate four.2Integer%
44Cell Viability at 0.08 uM [1, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate one.2Integer%
45Cell Viability at 0.08 uM [2, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate two.2Integer%
46Cell Viability at 0.08 uM [3, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate three.2Integer%
47Cell Viability at 0.08 uM [4, Assay 2] (0.08μM**)Value of % Surviving cells at 0.08 uM inhibitor concentration; replicate four.2Integer%
48Cell Viability at 0.4 uM [1, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate one.2Integer%
49Cell Viability at 0.4 uM [2, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate two.2Integer%
50Cell Viability at 0.4 uM [3, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate three.2Integer%
51Cell Viability at 0.4 uM [4, Assay 2] (0.4μM**)Value of % Surviving cells at 0.4 uM inhibitor concentration; replicate four.2Integer%
52Cell Viability at 2 uM [1, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate one.2Integer%
53Cell Viability at 2 uM [2, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate two.2Integer%
54Cell Viability at 2 uM [3, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate three.2Integer%
55Cell Viability at 2 uM [4, Assay 2] (2μM**)Value of % Surviving cells at 2 uM inhibitor concentration; replicate four.2Integer%
56Cell Viability at 10 uM [1, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate one.2Integer%
57Cell Viability at 10 uM [2, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate two.2Integer%
58Cell Viability at 10 uM [3, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate three.2Integer%
59Cell Viability at 10 uM [4, Assay 2] (10μM**)Value of % Surviving cells at 10 uM inhibitor concentration; replicate four.2Integer%
60Cell Viability at 50 uM [1, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate one.2Integer%
61Cell Viability at 50 uM [2, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate two.2Integer%
62Cell Viability at 50 uM [3, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate three.2Integer%
63Cell Viability at 50 uM [4, Assay 2] (50μM**)Value of % Surviving cells at 50 uM inhibitor concentration; replicate four.2Integer%

* Activity Concentration. ** Test Concentration. § Panel component ID.
Additional Information
Grant Number: TCELLCYTOX_INH_ABSORB_4XCC50_PAFAH2

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