Luminol

Manufactured by Carl Roth

Sourced in United States, Germany, Denmark

Luminol is a chemical reagent used in forensic science for the detection of blood traces. It reacts with the iron in hemoglobin, producing a characteristic blue-green chemiluminescence that can be observed in low-light conditions.

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Lab products found in correlation

6 protocols using luminol

Detailed Reagents for Oxidative Stress

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The following chemicals
were used: calcium
chloride (CaCl₂·6H₂O), Roth #T886; Cu/Zn-SOD
from bovine liver, Sigma #S8409; Cyt c from equine
heart, Sigma #C2506 and BioChemica/Fluka #30400; DMSO, Roth # 4720;
EDTA, Aldrich #E2,628-2; FeEDDHA 138, Duchefa #F0527; ferritin, Sigma
#F4503; ferrous sulfate (Fe^IISO₄·7H₂O), Roth #P015 and Merck #3965; ferredoxin from Chlamydomonas
reinhardtii; ferric nitrate (Fe^IIINO₃·9H₂O), Fluka #44949; heminchloride, Roth#7629; Hb
from bovine blood, Sigma #H2500; hydrochloric acid (HCl), Roth #4625;
hydrogen peroxide (H₂O₂), Roth #8070 and Merck
# 1.08597; luminol, Roth # 4203; mannitol, Roth #4175; peroxidase
from horseradish (HRP), Sigma #P6140; potassium hydroxide (KOH), Roth
#5658; and Tris ultrapure, ICN Biomedicals #77861.

, & Plieth C. (2019). Peroxide-Induced Liberation of Iron from Heme Switches Catalysis during Luminol Reaction and Causes Loss of Light and Heterodyning of Luminescence Kinetics. ACS Omega, 4(2), 3268-3279.

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SDS-PAGE and Western Blotting for Lon Protein Detection

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SDS page electrophoresis and Western blotting were performed as described in [75 (link),76 ]. Then, 7.5% polyacrylamide gels were used. Briefly, the Lon protein was detected with the anti-Escherichia coli Lon rabbit antibodies (#40219-T24, Sino Biological Inc., Beijing, China) at dilution 1:2000 followed by incubation with HRP conjugated secondary anti-rabbit antibodies (#31462 Thermo Fisher) diluted 1:50,000. Chemiluminescent signal was developed using a luminol/ p-coumaric acid (Carl Roth GmbH + Co. KG) mix (4 mL of 1.41 mM luminol, 400 µL of 6.7 mM p-coumaric acid in DMSO, 4 µL of 30% H₂O₂) and was recorded by Azure Biosystems c600 (Dublin, California, USA) imaging system.

Figaj D., Czaplewska P., Przepióra T., Ambroziak P., Potrykus M, & Skorko-Glonek J. (2020). Lon Protease Is Important for Growth under Stressful Conditions and Pathogenicity of the Phytopathogen, Bacterium Dickeya solani. International Journal of Molecular Sciences, 21(10), 3687.

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Quantitative Dot Blot Analysis of Secreted Proteins

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Secreted proteins in culture supernatant were detected by dot blot, as previously described [7 (link)]. Using a 96-well dot blotter (Carl Roth, Karlsruhe, Germany), 60 μL of supernatant was transferred onto a wet nitrocellulose membrane with a vacuum pump. After being blocked with 5% bovine serum albumin in Tris-buffered saline/Tween 20 (TBS-T (9127.1, Carl Roth, Karlsruhe, Germany); 10 mM Tris-HCl at pH 7.6, 0.15 mM NaCl, and 0.1% Tween-20) for 1 h, membranes were incubated with primary antibodies at 4 °C overnight. The antibodies used are summarized in Table 2. After washing with TBS-T, the membranes were incubated with secondary antibody for 2 h. The signals were detected by chemiluminescence (100 nM TRIS, 250 mM Luminol (4203.1, Carl Roth, Karlsruhe, Germany), 90 mM p-coumaric acid (9908.1, Carl Roth, Karlsruhe, Germany), 30% v/v H₂O₂ (CP26.5, Carl Roth, Karlsruhe, Germany)) and quantified by ImageJ (NIH, Bethesda, MD, USA).

Guo H., Weng W., Zhang S., Rinderknecht H., Braun B., Breinbauer R., Gupta P., Kumar A., Ehnert S., Histing T., Nussler A.K, & Aspera-Werz R.H. (2022). Maqui Berry and Ginseng Extracts Reduce Cigarette Smoke-Induced Cell Injury in a 3D Bone Co-Culture Model. Antioxidants, 11(12), 2460.

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Antioxidant Enzyme Assay Protocol

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Ascorbate
(Sigma, #A7506), benzidine (Sigma
#31614), calcium chloride (CaCl₂·6H₂O;
Roth #T886), coumaric acid (Sigma #C9008), Cu/Zn-superoxide dismutase
from bovine liver (Sigma #S8409), cytochrome c from
equine heart (Sigma #C2506 and BioChemica/Fluka #30400), DMSO (Roth
#4720), dithiothreitol (Roth#6908), ethylenediaminetetraacetic acid
(Aldrich #E2,628-2), FeEDDHA (Duchefa #F0527), ferrous sulfate (Fe^IISO₄·7H₂O; Roth #P015 and Merck
#3965), ferric nitrate (Fe^IIINO₃·9H₂O; Fluka #44949), GSH (Roth #6382), heminchlorid (Roth #7629),
hemoglobin from bovine blood (Sigma #H2500), hydrochloric acid (HCl
34%; Roth #4625), hydrogen peroxide (H₂O₂ 30%;
Roth #8070 and Merck #1.08597), IP (Fluka #58020), luminol (Roth #4203),
mannitol (Roth #4175), NADH (Roth #AE12), HRP (Sigma #P6140), potassium
hydroxide (KOH; Roth #5658), sodium sulfite (Na₂SO₃; Fluka #71988), TRIS ultrapure (ICN Biomedicals #77861),
trolox (KJ Ross-Petersen Aps; Denmark and Aldrich #23881), and uric
acid (UA, Sigma #U2625).

, & Plieth C. (2018). Redox Modulators Determine Luminol Luminescence Generated by Porphyrin-Coordinated Iron and May Repress “Suicide Inactivation”. ACS Omega, 3(9), 12295-12303.

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2D Western Blot Immunodetection Protocol

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For western blot applications, two identical gels were run. One 2DE gels was stained with FireSilver or Coomassie for preparative applications and the other gel was used for western blotting to detect the proteins by immunostaining. Blotting of 2DE gels was performed using an Immobilon-P membrane (PVDF; pore size 0.45 mm; Millipore) and a Trans-Blot SD Semi-Dry Transfer Cell (BioRad) at a constant current 5 V overnight at 4°C using a blotting buffer consisting of 25 mM Tris–HCl, 192 mM glycine, 0.1% SDS (pH 8.3) and 20% methanol. For immunodetection of proteins, membranes were washed in TBST (20 mM Tris–HCl [pH 7.5]; 154 mM NaCl, 0.1% Tween-20) and blocked in TBST containing 2% (w/v) BSA for 2 h. Membranes were incubated with the primary antibody (sc-65623; Santa Cruz Biotecnology; IgG
₁) diluted 1:1000 for 2DE blot and 1:50 for 1D-blots in TBST containing 1% (w/v) BSA overnight and then incubated with anti-mouse IgG (Fc specific–peroxidase antibody produced in goat; A0168; Sigma; diluted to 1:2000 in TBST containing 1% (w/v) BSA) for 1 h at room temperature. Finally, the bound antibody was detected by incubating with Luminol for 1s-20min (Roth). The membrane was washed in TBST (5 times for 10 min) between all incubation steps.

Lusi E.A., Maloney D., Caicci F, & Guarascio P. (2017). Questions on unusual Mimivirus-like structures observed in human cells. F1000Research, 6, 262.

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Immunoblot Analysis of Pneumococcal PnrA

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For immunoblot analysis pneumococcal cell lysates 5x10 8 bacteria were loaded per lane. Proteins were separated by SDS-PAGE and transferred onto a nitrocellulose membrane by semidry blotting (Bio-Rad Laboratories, Munich, Germany). The membrane was blocked with 5% skim milk (Roth) in Tris buffered saline (TBS).
Detection of PnrA was conducted with specific mouse anti-PnrA antibodies and goat anti-mouse IgG horseradish peroxidase conjugate (Dianova, Hamburg, Germany; 1:5000) as described [21] . The loading control protein enolase was detected with rabbit anti-enolase antibodies and a goat anti-rabbit IgG horseradish peroxidase conjugate (1:5000). Enhanced chemiluminescence (luminol and p-coumaric acid, Roth) was used for signal detection.

Abdullah M.R., Batuecas M.T., Jennert F., Voß F., Westhoff P., Kohler T.P., Molina R., Hirschmann S., Lalk M., Hermoso J.A, & Hammerschmidt S. (2021). Crystal Structure and Pathophysiological Role of the Pneumococcal Nucleoside-binding Protein PnrA. Journal of molecular biology, 433(2).

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