Total protein was extracted from cells using the M-PER mammalian protein extraction reagent or from tissues using the T-PER tissue protein extraction reagent (Pierce, USA). Equal amounts of protein (15 μg) were separated by SDS-PAGE (11% gel) and transferred onto nitrocellulose membranes. The blots were incubated with primary antibodies against human KLF4 (1:400), Snai1 (1:500), α-SMA (1:200), E-cadherin (1:500), MMP2 (1:200), MMP9 (1:400), and β-actin (1:1,200) (Abcam), followed by incubation with the corresponding secondary HRP-conjugated anti-rabbit/mouse antibody (Abcam). The bands were detected by chemiluminescence and imaged with X-ray films. β-actin was used as an endogenous reference for normalization.
Hrp conjugated anti mouse rabbit antibody
Manufactured by Abcam
Sourced in United Kingdom
HRP-conjugated anti-mouse/rabbit antibody is a secondary antibody conjugated to horseradish peroxidase (HRP). It is used to detect and visualize primary antibodies raised in mouse or rabbit.
Automatically generated - may contain errors
Lab products found in correlation
Mmp 9, by Santa Cruz Biotechnology (4 mentions)
C myc, by Santa Cruz Biotechnology (4 mentions)
E cadherin, by Santa Cruz Biotechnology (4 mentions)
β actin, by Santa Cruz Biotechnology (4 mentions)
Cyclin d1, by Santa Cruz Biotechnology (4 mentions)
α sma, by Abcam (2 mentions)
E cadherin, by Abcam (2 mentions)
β actin, by Abcam (2 mentions)
Mmp 9, by Abcam (1 mentions)
Snail1, by Abcam (1 mentions)
Vimentin, by Abcam (1 mentions)
Ctnnb1, by Santa Cruz Biotechnology (1 mentions)
6 protocols using hrp conjugated anti mouse rabbit antibody
1
Protein Expression Profiling of Epithelial-Mesenchymal Transition
2
Western Blot Analysis of Epithelial-Mesenchymal Transition
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The total protein was extracted from cells using the M-PER mammalian protein extraction reagent (Pierce, Rockford, IL, USA) in accordance with the manufacturer’s instructions. Equal amounts of total protein (10 μg) were loaded onto SDS-PAGE gels (11%) and transferred onto nitrocellulose membranes. The blots were probed at 4 °C overnight with the primary antibodies against human NR2F2(1:400), Snail1 (1:500), α-SMA (1:400), Vimentin (1:450), E-cadherin (1:400), and β-actin (1:1000) (Abcam), followed by probing with the secondary HRP-conjugated anti-rabbit/mouse antibody (1:4000 dilution) at room temperature for 2 h. After washing, the bands were detected by chemiluminescence and imaged with X-ray films. β-actin was used as an endogenous reference for normalization.
3
Immunoblotting Analysis of Cell Proteins
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The total protein was extracted from the cells and tissues by using mammalian protein extraction reagent (Pierce, IL, USA). Equal amounts of protein (25 μg per lane) estimated by a bicinchoninic acid (BCA) protein assay kit (Pierce) were loaded onto (11%) SDS-PAGE gels and transferred onto nitrocellulose membranes. The blots were probed with a monoclonal antibody against human CTNNB1 (1:400), E-cadherin (1:200), C-myc (1:300), CyclinD1 (1:400), MMP-9 (1:250) and β-actin (1:1000) (Santa Cruz, USA), followed by the secondary HRP-conjugated anti-mouse/rabbit antibody (Abcam, Cambridge, UK). After washing, the bands were detected by chemiluminescence and imaged with X-ray films. β-actin was used as an endogenous reference for normalization.
4
Western Blot Protein Analysis
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The total protein was extracted from the cells and tissues by using and tissues by mammalian protein extraction reagent (Pierce, IL, USA). Equal amounts of protein (25 μg per lane) estimated by a bicinchoninic acid (BCA) protein assay kit (Pierce) were loaded onto (11%) SDS-PAGE gels and transferred onto nitrocellulose membranes. The blots were probed with a monoclonal antibody against human CTNNB1 (1:400), E-cadherin (1:200), C-myc (1:300), CyclinD1 (1:400) MMP-9 (1:250) and β-actin (1:1000) (Santa Cruz, USA), followed by the secondary HRP-conjugated anti-mouse/rabbit antibody (Abcam, Cambridge, UK). After washing, the bands were detected by chemiluminescence and imaged with X-ray lms. β-actin was used as an endogenous reference for normalization.
5
Western Blot Analysis of Protein Expression
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The total protein was extracted from the cells using M-PER mammalian protein extraction reagent (Pierce, IL, USA) or from tissues using T-PER tissue protein extraction reagent (Pierce). Equal amounts of protein (25 μg per lane) estimated by a bicinchoninic acid (BCA) protein assay kit (Pierce) were loaded onto (11%) SDS-PAGE gels and transferred onto nitrocellulose membranes. The blots were probed with a monoclonal antibody against human CTNNB1 (1:400), E-cadherin (1:200), C-myc (1:300), CyclinD1
(1:400) MMP-9 (1:250) and β-actin (1:1000) (Santa Cruz, USA), followed the secondary HRP-conjugated anti-mouse/rabbit antibody (Abcam, CA, USA). After washing, the bands were detected by chemiluminescence and imaged with X-ray lms. β-actin was used as an endogenous reference for normalization.
(1:400) MMP-9 (1:250) and β-actin (1:1000) (Santa Cruz, USA), followed the secondary HRP-conjugated anti-mouse/rabbit antibody (Abcam, CA, USA). After washing, the bands were detected by chemiluminescence and imaged with X-ray lms. β-actin was used as an endogenous reference for normalization.
6
Protein Expression Analysis Protocol
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The total protein was extracted from the cells and tissues by using mammalian protein extraction reagent (Pierce, IL, USA). Equal amounts of protein (25 μg per lane) estimated by a bicinchoninic acid (BCA) protein assay kit (Pierce) were loaded onto (11%) SDS-PAGE gels and transferred onto nitrocellulose membranes. The blots were probed with a monoclonal antibody against human CTNNB1 (1:400), E-cadherin (1:200), C-myc (1:300), CyclinD1 (1:400) MMP-9 (1:250) and β-actin (1:1000) (Santa Cruz, USA), followed by the secondary HRP-conjugated anti-mouse/rabbit antibody (Abcam, Cambridge, UK). After washing, the bands were detected by chemiluminescence and imaged with X-ray lms. β-actin was used as an endogenous reference for normalization.
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