Log In Sign up
The largest database of trusted experimental protocols

Horseradish peroxidase conjugated igg antibodies

Manufactured by Bio-Rad
Visit Supplier
Sourced in Germany

Horseradish peroxidase-conjugated IgG antibodies are laboratory reagents that consist of immunoglobulin G (IgG) antibodies covalently linked to the enzyme horseradish peroxidase. These conjugated antibodies are used as detection tools in various immunoassay techniques, such as enzyme-linked immunosorbent assays (ELISAs), Western blots, and immunohistochemistry.

Automatically generated - may contain errors

Lab products found in correlation

Enhanced chemiluminescent substrate, by Thermo Fisher Scientific (4 mentions) Primary phospho antibodies, by Cell Signaling Technology (3 mentions) Primary full length antibodies, by Santa Cruz Biotechnology (3 mentions) Sds page, by Bio-Rad (2 mentions) Versadoc system, by Bio-Rad (1 mentions) C3 33, by Merck Group (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Smad1 5 8, by Santa Cruz Biotechnology (1 mentions) P erk 1 2, by Bio-Rad (1 mentions)

5 protocols using horseradish peroxidase conjugated igg antibodies

1

Protein Expression Profiling in Tissue Engineering

Check if the same lab product or an alternative is used in the 5 most similar protocols
Lysates for western blot analysis were prepared from scaffolds at 0, 3, 7, 14, and 24 days of culture using Phosphosafe lysis buffer (Novagen, Madison, WI). Equal amounts of protein lysates were subjected to 4–20% (Bio-Rad) SDS-PAGE. Western analysis was carried out with antibodies against phosphorylated-Smad1/5 (p-Smad1/5), total Smad1/5/8, phosphorylated-ERK1/2 (p-ERK1/2), total ERK1/2, phosphorylated-Smad2/3 (p-Smad2/3), total Smad2/3, phosphorylated-p38 (p-p38), total p38, Akt, phosphorylated-Akt (p-Akt) and β-actin followed by 1:4000 dilutions of horseradish peroxidase-conjugated IgG antibodies (Bio-Rad, Hercules, CA) and an enhanced chemiluminescent substrate (Thermo Scientific, Rockford, IL). For detection of p-Smad1/5 and total Smad1/5/8, 40 µg of lysate was loaded per lane. For detection of p-ERK1/2 and total ERK1/2, 60 µg of lysate was loaded per lane. For detection p-p38, total p38, p-Smad2/3, total Smad2/3, 50 µg of lysate was loaded per lane. All primary phospho antibodies were obtained from Cell Signaling Technologies (Beverly, MA) and all primary full length antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, CA). Imaging was carried out using ImageJ (NIH, Bethesda, MD).
Ren X., Tu V., Bischoff D., Weisgerber D.W., Lewis M.S., Yamaguchi D.T., Miller T.A., Harley B.A, & Lee J.C. (2016). Nanoparticulate Mineralized Collagen Scaffolds Induce In Vivo Bone Regeneration Independent of Progenitor Cell Loading or Exogenous Growth Factor Stimulation. Biomaterials, 89, 67-78.
+ Open protocol
+ Expand
2

Signaling Pathway Analysis of Cell Scaffolds

Check if the same lab product or an alternative is used in the 5 most similar protocols
Lysates for western blot analysis were prepared from scaffolds at 7 and 14 days of culture using Phosphosafe lysis buffer (Novagen, USA). Equal amounts of protein lysates were subjected to 4–20% (Bio-Rad) SDS-PAGE. Western blot analysis was carried out with antibodies against phosphorylated-Smad1/5/8 (P-Smad1/5), total Smad1/5/8, phosphorylated-Smad2/3 (P-Smad2/3), total Smad2/3, phosphorylated-p38 (P-p38), total p38, phosphorylated-GSK3β (P-GSK3β), total GSK3β, phosphorylated β-catenin (P-β-catenin), and β-actin followed by 1 : 4000 dilutions of horseradish peroxidase-conjugated IgG antibodies (Bio-Rad) and an enhanced chemiluminescent substrate (Thermo Scientific, Rockford, IL). For detection of P-Smad1/5/8 and total Smad1/5/8, 40 mg of lysate was loaded per lane. For detection P-p38, total p38, P-Smad2/3, total Smad2/3, P-GSK3β, total GSK3β, P-β-catenin, 50 mg of lysate was loaded per lane. All primary phospho antibodies were obtained from Cell Signaling Technology (Beverly, MA), and all primary full-length antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, CA). Images were analyzed using ImageJ (NIH, Bethesda, MD).
Liang B., Huang J., Xu J., Li X, & Li J. (2018). Local delivery of a novel PTHrP via mesoporous bioactive glass scaffolds to improve bone regeneration in a rat posterolateral spinal fusion model. RSC Advances, 8(22), 12484-12493.
+ Open protocol
+ Expand
3

Co-Immunoprecipitation Analysis of Cardiomyocyte Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
Co-immunoprecipitation (Co-IP) experiments were performed as described previously 28 . Lysates from both mouse whole hearts and isolated ventricular cardiomyocytes were prepared in lysis buffer. Determination of total protein was performed by the DC Protein Assay (BioRad, Hercules, CA), after which 1 mg of the supernatants were used for immunopurification. Proteins were resolved in 8% SDSpoly-acrylamide (SDS-PAGE) gel and transferred to a nitrocellulose membrane (BioRad, Hercules, CA). Blots were probed with primary antibodies against RyR2 (C3-33, Sigma-Aldrich), N-cadherin (H-63, sc-7939; Santa Cruz Biotechnology, Heidelberg, Germany), Cx43 (AB0016) and Calnexin (AB0041, Sicgen), followed by appropriate horseradish peroxidase-conjugated IgG antibodies (BioRad). The proteins of interest were visualized by chemiluminescence using a VersaDoc system (Bio-Rad).
Lissoni A., Hulpiau P., Martins-Marques T., Wang N., Bultynck G., Schulz R., Witschas K., Girao H., De Smet M, & Leybaert L. (2021). RyR2 regulates Cx43 hemichannel intracellular Ca2+-dependent activation in cardiomyocytes. Cardiovascular research, 117(1).
+ Open protocol
+ Expand
4

Quantifying Smad and MAPK Signaling in 3D Scaffolds

Check if the same lab product or an alternative is used in the 5 most similar protocols
Lysates for western blot analysis were prepared from scaffolds at 0, 3, 14, and 24 days of culture using Phosphosafe lysis buffer (Novagen, Madison, WI). Equal amounts of protein lysates were subjected to 4–20% SDS-PAGE (Bio-Rad, Hercules, CA). Western analysis was carried out with antibodies against phosphorylated Smad1/5 (p-Smad1/5), total Smad1/5/8, phosphorylated ERK1/2 (p-ERK1/2), total ERK1/2, phosphorylated Smad2/3 (p-Smad2/3), total Smad2/3, phosphorylated p38 (p-p38), total p38, and β-actin followed by 1:4000 dilutions of horseradish peroxidase-conjugated IgG antibodies (Bio-Rad, Hercules, CA) and an enhanced chemiluminescent substrate (Thermo Scientific, Rockford, IL). For detection of p-Smad1/5 and total Smad1/5/8, 40 μg of lysate was loaded per lane. For detection of p-ERK1/2 and total ERK1/2, 60 μg of lysate was loaded per lane. For detection p-p38, total p38, p-Smad2/3, total Smad2/3, 50 μg of lysate was loaded per lane. All primary phospho antibodies were obtained from Cell Signaling Technologies (Beverly, MA) and all primary full length antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, CA). Imaging was carried out using ImageJ (NIH, Bethesda, MD).
Ren X., Bischoff D., Weisgerber D.W., Lewis M.S., Tu V., Yamaguchi D.T., Miller T.A., Harley B.A, & Lee J.C. (2015). Osteogenesis on nanoparticulate mineralized collagen scaffolds via autogenous activation of the canonical BMP receptor signaling pathway. Biomaterials, 50, 107-114.
+ Open protocol
+ Expand
5

Quantifying Signaling Pathway Dynamics

Check if the same lab product or an alternative is used in the 5 most similar protocols
Lysates for western blot analysis were prepared from scaffolds at 0, 3, 7, 14, and 21 days of culture using Phosphosafe lysis buffer (Novagen, Madison, WI). Equal amounts of protein lysates were subjected to 4–20% SDS-PAGE (Bio-Rad, Hercules, CA). Western analysis was carried out with antibodies against phosphorylated-Smad1/5 (p-Smad1/5), total Smad1/5/8, phosphorylated-ERK1/2 (p-ERK1/2), total ERK1/2, phosphorylated-Smad2/3 (p-Smad2/3), total Smad2/3, phosphorylated-p38 (p-p38), total p38, and β-actin followed by 1:4000 dilutions of horseradish peroxidase-conjugated IgG antibodies (Bio-Rad, Hercules, CA) and an enhanced chemiluminescent substrate (Thermo Scientific, Rockford, IL). All primary phospho and full length antibodies were obtained from Cell Signaling Technologies (Beverly, MA) except Smad1/5/8, which was obtained from Santa Cruz Biotechnology (Santa Cruz, CA). Imaging was carried out using ImageJ (NIH, Bethesda, MD).
Ren X., Weisgerber D.W., Bischoff D., Lewis M.S., Reid R.R., He T.C., Yamaguchi D.T., Miller T.A., Harley B.A, & Lee J.C. (2016). Nanoparticulate Mineralized Collagen Scaffolds and BMP-9 Induce a Long Term Bone Cartilage Construct in Human Mesenchymal Stem Cells. Advanced healthcare materials, 5(14), 1821-1830.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!