disodium Search Results


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Gold Biotechnology Inc c 103 sl
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Frontier Specialty Chemicals Inc protoporphyrin ix disodium salt
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Valiant Co Ltd g 980
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Valiant Co Ltd eosin y right supplemental information eosin y disodium salt
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Gold Biotechnology Inc m edta
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Valiant Co Ltd γ 32p atp
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Gold Biotechnology Inc lb plates
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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91
Valiant Co Ltd gα o
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Gold Biotechnology Inc 5 triphosphate
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
5 Triphosphate, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MedChemExpress disodium succinate
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Selleck Chemicals atp disodium s1985
Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) <t>protoporphyrin-IX</t> (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.
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Santa Cruz Biotechnology anthracene 9 10 dipropionic acid disodium salt adpa
Reactive oxygen species (ROS) generation by Ce6 ethosomes. ( A ) Determination of 1 O 2 production kinetics by 0.3 µM of Ce6 (red) and Ce6 ethosomes (black), as analyzed by <t>ADPA</t> sensor fluorescence decay at Ex 378 nm and Em 400–420 nm. The rate constants for 1 O 2 production for Ce6 and Ce6 ethosomes are non-significantly different ( p > 0.05). ( B ) A431 squamous cell carcinoma cells were treated with Ce6 ethosomes (2 µM) for 24 h then irradiated with laser light at 12 J/cm 2 . At 4 h after photodynamic therapy (PDT), the collected cells were stained with 5 μM MitoSOX, a mitochondrial peroxide sensor, and the labelled cells were analyzed by flow cytometry (Ex/Em 490/580 nm). Data are the mean ± SD; n = 4, *** p < 0.001 vs. controls.
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Image Search Results


Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) protoporphyrin-IX (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

Article Title: Metalloporphyrins inactivate caspase-3 and -8.

doi: 10.1096/fj.04-3259com

Figure Lengend Snippet: Figure 1. The influence of metalloporphyrins on caspase-3- like activity, HO-1 protein expression, and PARP cleavage in intact Jurkat T-lymphocytes. A) Cells were either left un- treated (Co) or treated with Fas ligand (FasL, 100 ng/mL, 16 h). The HO-1 inducer cobalt(III) protoporphyrin-IX (CoPP, 10 M) and the HO-1 inhibitors tin and zinc(II) protoporphyrin-IX (SnPP, ZnPP, 10 M each) were added 30 min before the cells were lysed. Caspase-3-like activity was determined. Bars represent means se of 3 independent experiments performed in triplicates and values of untreated cells were set as 1. ***P 0.001 represents significant differences compared with Co. P 0.001 represents significant differences compared with cells treated with FasL alone. B) To detect HO-1 protein expression by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL, 16 h) or with the different porphyrins (CoPP, SnPP, ZnPP, 10 M each, 30 min). Human umbilical vein endothe- lial cells (HUVEC) treated with CoPP (10 M, 30 min) served as a positive control (P) for induction of HO-1 protein expression. One representative blot of three is shown. C) To detect PARP cleavage by Western blot, cells were either left untreated (Co) or treated with FasL (100 ng/mL) alone or together with CoPP (10 M) for 6 h. Experiments were performed 3 times with consistent results and 1 representative blot is shown.

Article Snippet: Protoporphyrin IX disodium salt was from Frontier Scientific Porphyrin Products (Carnforth/ Lancashire, UK).

Techniques: Activity Assay, Expressing, Western Blot, Positive Control

Figure 4. Metalloporphyrins and protoporphyrin sodium salt influence the activity of recombinant caspase-3. CoPP (0.001–10 M), SnPP (0.001–100 M), ZnPP (0.001–100 M (A), or protoporphyrin-IX disodium salt (PP, 10 M) (C) were added to recombinant caspases-3 (C-3) immediately before measurement of caspase activity. In further experi- ments, CoPP (10 M) was added to recombinant caspase-3 with increasing amounts of the caspase-3 substrate (B). Data represent means se of 3 independent experiments per- formed in triplicates and activity of caspase-3 in the absence of the porphyrins was taken as 100%. ***P 0.001 represents significant differences compared with the respective C-3 group.

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

Article Title: Metalloporphyrins inactivate caspase-3 and -8.

doi: 10.1096/fj.04-3259com

Figure Lengend Snippet: Figure 4. Metalloporphyrins and protoporphyrin sodium salt influence the activity of recombinant caspase-3. CoPP (0.001–10 M), SnPP (0.001–100 M), ZnPP (0.001–100 M (A), or protoporphyrin-IX disodium salt (PP, 10 M) (C) were added to recombinant caspases-3 (C-3) immediately before measurement of caspase activity. In further experi- ments, CoPP (10 M) was added to recombinant caspase-3 with increasing amounts of the caspase-3 substrate (B). Data represent means se of 3 independent experiments per- formed in triplicates and activity of caspase-3 in the absence of the porphyrins was taken as 100%. ***P 0.001 represents significant differences compared with the respective C-3 group.

Article Snippet: Protoporphyrin IX disodium salt was from Frontier Scientific Porphyrin Products (Carnforth/ Lancashire, UK).

Techniques: Activity Assay, Recombinant

Figure 7. Auto-Dock results. Caspase-3 together with 10 putative binding conformations of protoporphyrin (A). Rep- resentation of the energetically most favorable caspase-3/ protoporphyrin complex showing the major protein-ligand interactions (B).

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

Article Title: Metalloporphyrins inactivate caspase-3 and -8.

doi: 10.1096/fj.04-3259com

Figure Lengend Snippet: Figure 7. Auto-Dock results. Caspase-3 together with 10 putative binding conformations of protoporphyrin (A). Rep- resentation of the energetically most favorable caspase-3/ protoporphyrin complex showing the major protein-ligand interactions (B).

Article Snippet: Protoporphyrin IX disodium salt was from Frontier Scientific Porphyrin Products (Carnforth/ Lancashire, UK).

Techniques: Binding Assay

Reactive oxygen species (ROS) generation by Ce6 ethosomes. ( A ) Determination of 1 O 2 production kinetics by 0.3 µM of Ce6 (red) and Ce6 ethosomes (black), as analyzed by ADPA sensor fluorescence decay at Ex 378 nm and Em 400–420 nm. The rate constants for 1 O 2 production for Ce6 and Ce6 ethosomes are non-significantly different ( p > 0.05). ( B ) A431 squamous cell carcinoma cells were treated with Ce6 ethosomes (2 µM) for 24 h then irradiated with laser light at 12 J/cm 2 . At 4 h after photodynamic therapy (PDT), the collected cells were stained with 5 μM MitoSOX, a mitochondrial peroxide sensor, and the labelled cells were analyzed by flow cytometry (Ex/Em 490/580 nm). Data are the mean ± SD; n = 4, *** p < 0.001 vs. controls.

Journal: Pharmaceutics

Article Title: A Naturally Derived Carrier for Photodynamic Treatment of Squamous Cell Carcinoma: In Vitro and In Vivo Models

doi: 10.3390/pharmaceutics12060494

Figure Lengend Snippet: Reactive oxygen species (ROS) generation by Ce6 ethosomes. ( A ) Determination of 1 O 2 production kinetics by 0.3 µM of Ce6 (red) and Ce6 ethosomes (black), as analyzed by ADPA sensor fluorescence decay at Ex 378 nm and Em 400–420 nm. The rate constants for 1 O 2 production for Ce6 and Ce6 ethosomes are non-significantly different ( p > 0.05). ( B ) A431 squamous cell carcinoma cells were treated with Ce6 ethosomes (2 µM) for 24 h then irradiated with laser light at 12 J/cm 2 . At 4 h after photodynamic therapy (PDT), the collected cells were stained with 5 μM MitoSOX, a mitochondrial peroxide sensor, and the labelled cells were analyzed by flow cytometry (Ex/Em 490/580 nm). Data are the mean ± SD; n = 4, *** p < 0.001 vs. controls.

Article Snippet: Human squamous cell carcinoma, A431 (ACC 91, DSMZ German collection of microorganisms and cell cultures, Braunschweig, Germany), normal human skin fibroblasts, BJ (American Type Culture Collection, ATCC ® CRL-2522TM, Manassas, VI, USA), lecithin from soybean 90% (PanReac AppliChem, Darmstadt, Germany), chlorin e6 (Cayman Chemical, Ann Arbor, MI, USA), cremophor A25 (Sigma-Aldrich, Taufkirchen, Germany), anthracene-9,10-dipropionic acid disodium salt (ADPA) (Santa Cruz Biotechnology, Santa Cruz, CA, USA), sodium azide (99%) (Loba Chemie, Mumbai, India) were obtained as indicated.

Techniques: Fluorescence, Irradiation, Staining, Flow Cytometry