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Luminata forte western blotting substrate

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Luminata Forte Western Blotting substrate is a chemiluminescent detection reagent used in Western blotting analysis. It is designed to provide a sensitive and reliable signal for the detection of target proteins.

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Lab products found in correlation

P akt thr308, by Cell Signaling Technology (2 mentions) Calsequestrin, by Abcam (2 mentions) P erk1 2 thr202 tyr204, by Cell Signaling Technology (1 mentions) P mtor ser2448, by Cell Signaling Technology (1 mentions) P 4e bp1 thr37 46, by Cell Signaling Technology (1 mentions) P stat5 tyr694, by Cell Signaling Technology (1 mentions) Immobilon p membrane, by Merck Group (1 mentions) Tween 20, by Merck Group (1 mentions) Skim milk, by Merck Group (1 mentions) Peroxidase conjugated goat anti mouse igg, by Santa Cruz Biotechnology (1 mentions) Mmp 9, by Abcam (1 mentions) Timp3, by Abcam (1 mentions) Tween 20, by Santa Cruz Biotechnology (1 mentions) Timp 2, by Abcam (1 mentions) Timp 1, by Abcam (1 mentions) Ab3516, by Abcam (1 mentions)

Close spelling variants of this product

Luminata Forte (152 citations) Luminata Forte substrate (11 citations) Luminata Forte Western substrate (2 citations) Substrates (2 citations) Luminata Forte chemiluminescence Western blotting substrate (2 citations)

5 protocols using luminata forte western blotting substrate

1

Western Blot Analysis of Protein Expression

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Qualitative analysis of protein expression and phosphorylation status was performed via standard western blotting procedures, as described previously.19 (link) Briefly, 10–30 μg protein lysate was separated on polyacrylamide gels and transferred to PVDF membranes. Membranes were probed for the following targets: p-AktThr−308 (Cell Signaling; 9275), Akt (Cell Signaling; 9272), and calsequestrin (Abcam; ab3516). A rabbit HRP-conjugated secondary antibody (Cell Signaling; 7074) was used for chemiluminescent detection with Luminata Forte Western Blotting substrate (Millipore, WBLUF0100). In order to minimize the contribution that position on the gel might have on outcomes, samples were randomized on gels; samples were re-ordered post-imaging, only for the sake of illustration of representative images (note, all bands for representative images for an individual experiment were from the same gel).
Mia S., Sonkar R., Williams L., Latimer M.N., Frayne Robillard I., Diwan A., Frank S.J., Des Rosiers C, & Young M.E. (2021). Impact of obesity on day‐night differences in cardiac metabolism. The FASEB Journal, 35(3), e21298.
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2

Quantitative Protein Expression Analysis

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Qualitative analysis of protein expression and phosphorylation status was performed via standard western blotting procedures, as described previously (Durgan et al., 2011b (link)). Briefly, 20–30 µg protein lysate was separated on polyacrylamide gels and transferred to PVDF membranes. Membranes were probed for the following targets: p-STAT5Tyr694 (Cell Signaling, 9351L), p-ERK 1/2Thr202/Tyr204 (Cell Signaling 9101), p-mTORSer−2448 (Cell Signaling, 2974), and p-4EBP1Thr−37/46 (Cell Signaling, 9459). Rabbit HRP-conjugated secondary antibodies (Cell Signaling 7076) were used for chemiluminescent detection with Luminata Forte Western Blotting substrate (Millipore, WBLUF0100). Densitometry data were normalized to total STAT5 (Santa Cruz Biotechnology, sc-835) or amido black. Importantly, in order to minimize the contribution that position on the gel might have on outcomes, samples were randomized on gels; samples were re-ordered post-imaging, only for the sake of illustration of representative images (note, all bands for representative images for an individual experiment were from the same gel; see Supplementary Figures S4, S5).
Sonkar R., Berry R., Latimer M.N., Prabhu S.D., Young M.E, & Frank S.J. (2022). Augmented Cardiac Growth Hormone Signaling Contributes to Cardiomyopathy Following Genetic Disruption of the Cardiomyocyte Circadian Clock. Frontiers in Pharmacology, 13, 836725.
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3

Western Blot Analysis of TIMP and MMP

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For the detection of TIMP and MMP protein expression 15 μg of total protein was separated on a 10 % polyacrylamide gel and transferred to Immobilon-P membranes (Millipore, Schwalbach, Germany). After blocking in PBS supplemented with 5 % skim milk (Sigma-Aldrich) and 0.05 % Tween 20 (Sigma-Aldrich) membranes were incubated overnight at 4 °C with one of the following primary antibodies at the indicated dilutions: MMP2 (1:500) (Abcam, Cambridge, United Kingdom), MMP9 (1:500) (Abcam) TIMP1 (1:250) (Abcam), TIMP2 (1:250) (Abcam), TIMP3 (1:250) (Abcam). After washing three times in PBS containing 0.1 % Tween 20 membranes were incubated for 1 h at room temperature with 5000-fold diluted peroxidase conjugated goat anti-mouse IgG (Santa Cruz). Proteins recognized by the antibody were visualized with luminata forte western blotting substrate (Millipore) according to the manufacturer’s instructions. Signal intensities were quantified by densitometry using Bio-1D software version 15.01 (Vilber Lourmat, Eberhardzell, Germany).
Kunz P., Sähr H., Lehner B., Fischer C., Seebach E, & Fellenberg J. (2016). Elevated ratio of MMP2/MMP9 activity is associated with poor response to chemotherapy in osteosarcoma. BMC Cancer, 16, 223.
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4

Western Blot Analysis of Protein Signaling

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Qualitative analysis of protein expression and phosphorylation status was performed via standard western blotting procedures, as described previously (11 (link)). Briefly, 10–30 μg protein lysate was separated on polyacrylamide gels and transferred to PVDF membranes. Membranes were probed for the following targets: p-mTORSer−2448, p-P70S6KThr−389, p-S6Ser−240/244, p-4EBP1Thr−37/46, p-eIF4BSer−406, BCKDHa, p-BCKDHaSer−293, RAGA/B, RAGC, GβL, DEPTOR and RAGD (Cell Signaling; 2974, 9206, 2215, 9459, 8151, 90198, 40368, 4357, 5466, 3274, and 11816; Abcam 187679 respectively). Rabbit and mouse HRP-conjugated secondary antibodies (Cell Signaling, 7074 and 7076 respectively) were used for chemiluminescent detection with Luminata Forte Western Blotting substrate (Millipore, WBLUF0100). All densitometry data were normalized to calsequestrin (Abcam; ab3516). Importantly, due to the nature of time course studies, in order to minimize the contribution that position on the gel might have on outcomes, samples were randomized on gels; samples were re-ordered post-imaging, only for the sake of illustration of representative images (note, all bands for representative images for an individual experiment were from the same gel; original images are presented in Supplemental Figure 7).
Latimer M.N., Sonkar R., Mia S., Frayne I.R., Carter K.J., Johnson C.A., Rana S., Xie M., Rowe G.C., Wende A.R., Prabhu S.D., Frank S.J., Des Rosiers C., Chatham J.C, & Young M.E. (2021). Branched Chain Amino Acids Selectively Promote Cardiac Growth at the End of the Awake Period. Journal of molecular and cellular cardiology, 157, 31-44.
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5

Protein Expression and Phosphorylation Analysis

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Qualitative analysis of protein expression and phosphorylation status was performed via standard western blotting procedures, as described previously.19 Briefly, 10‐30 µg protein lysate was separated on polyacrylamide gels and transferred to PVDF membranes. Membranes were probed for the following targets: p‐AktThr‐308 (Cell Signaling; 9275), Akt (Cell Signaling; 9272), and calsequestrin (Abcam; ab3516). A rabbit HRP‐conjugated secondary antibody (Cell Signaling; 7074) was used for chemiluminescent detection with Luminata Forte Western Blotting substrate (Millipore, WBLUF0100). In order to minimize the contribution that position on the gel might have on outcomes, samples were randomized on gels; samples were re‐ordered postimaging, only for the sake of illustration of representative images (note, all bands for representative images for an individual experiment were from the same gel).
Mia S., Sonkar R., Williams L., Latimer M.N., Frayne Robillard I., Diwan A., Frank S.J., Des Rosiers C, & Young M.E. (2021). Impact of obesity on day‐night differences in cardiac metabolism. The FASEB Journal, 35(3), e21298.
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