Precision plus protein ladder

Manufactured by Bio-Rad

The Precision Plus Protein Ladder is a pre-stained molecular weight standard used for the identification and estimation of protein molecular weights in SDS-PAGE. It consists of 10 recombinant proteins, ranging from 10 to 250 kDa, that are covalently coupled to a blue or orange dye.

Automatically generated - may contain errors

Lab products found in correlation

Ecl plus chemiluminescent substrate, by GE Healthcare (2 mentions) Criterion polyacrylamide gel, by Bio-Rad (2 mentions) Pvdf membrane, by GE Healthcare (2 mentions) Nupage lds buffer, by Thermo Fisher Scientific (1 mentions) Chemidoc touch imager, by Bio-Rad (1 mentions) Nupage reducing agent 10, by Thermo Fisher Scientific (1 mentions) Mes buffer, by Thermo Fisher Scientific (1 mentions) Simplyblue safestain, by Thermo Fisher Scientific (1 mentions) Image lab software, by Bio-Rad (1 mentions) Collagen 1, by Merck Group (1 mentions) Imagequant tl software, by GE Healthcare (1 mentions) Criterion xt bis tris precast gel, by Bio-Rad (1 mentions) Xt mops buffer, by Bio-Rad (1 mentions) Ge image scanner 3, by GE Healthcare (1 mentions) Xt reducing agent, by Bio-Rad (1 mentions) Bio safe coomassie, by Bio-Rad (1 mentions) Xt sample buffer, by Bio-Rad (1 mentions) Phenol chloroform isoamyl alcohol, by Thermo Fisher Scientific (1 mentions) Pierce ecl 2 western blotting substrate, by Thermo Fisher Scientific (1 mentions) Actin 1 19, by Santa Cruz Biotechnology (1 mentions)

7 protocols using precision plus protein ladder

Protein Sample Preparation and Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

Protein samples were prepared for analysis by adding water, NuPage Reducing Agent (10×) (Invitrogen, Carlsbad, CA), and NuPage LDS Buffer (4×) (Invitrogen) for a total of 10 μL per well. Non-reduced samples were prepared similarly, substituting 1 μL of water for the reducing agent. Each sample was put into a NuPage™ 4–12% Bis-Tris PAGE gel (Invitrogen) along with a PrecisionPlus™ protein ladder (Biorad, Hercules, CA). Gels were run in MES buffer (Invitrogen). After electrophoresis, gels were rinsed three times with 18 MΩ water for 5 min each. Gels were then treated with SimplyBlue™ Safestain (Invitrogen) for at least one hour, and then rinsed with water overnight. Images of stained gels were taken using a Chemidoc Touch Imager (BioRad). Densitometry measurements were performed using ImageLab software (BioRad). Densitometry readings of >96% were considered to be pure enough to proceed with animal trials.

Gillam F, & Zhang C. (2018). Epitope selection and their placement for increased virus neutralization in a novel vaccination strategy for porcine epidemic diarrhea virus utilizing the Hepatitis B virus core antigen. Vaccine, 36(30), 4507-4516.

+ Open protocol

+ Expand

Comparative Analysis of dECM Composition

Check if the same lab product or an alternative is used in the 5 most similar protocols

SDS-PAGE was used to compare the compositions of the dECMs. Protein extracts were prepared using the Pierce Protein Assay Kit according to manufacturer instructions and resuspended in 7.5 μL XT sample buffer/1.5 μL XT reducing agent (Bio-Rad), placed in a 95°C heating block for 10 min, and centrifuged for 2 min at 14,000 g. Samples were loaded into 1.0 mm 4–12% gradient Bis-Tris Criterion XT Precast Gel (Bio-Rad), with collagen I (Sigma Aldrich) and Precision Plus protein ladder (Bio-Rad) used as controls. Loaded gels were placed into XT MOPS buffer (Bio-Rad) and electrophoresed at 150 V for ~100 min. Gels were then stained with BioSafe Coomassie (Bio-Rad) for at least 2 h and washed with deionized water three times for 5 min each. Bands were visualized using a GE Image Scanner III, with images taken using ImageQuant TL software (GE Healthcare).

Yang M.C., O'Connor A.J., Kalionis B, & Heath D.E. (2022). Improvement of Mesenchymal Stromal Cell Proliferation and Differentiation via Decellularized Extracellular Matrix on Substrates With a Range of Surface Chemistries. Frontiers in Medical Technology, 4, 834123.

+ Open protocol

+ Expand

Reagents and Antibodies for Protein Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

Unless otherwise noted, all chemicals were purchased from Sigma/Aldrich Chemical Co (St. Louis, MO & Milwaukee, WI). DNA extraction solvents were from Life Technologies (Grand Island, NY). Criterion polyacrylamide gels and Precision Plus protein ladder were purchased from BioRad Laboratories (Richmond, CA). PVDF membrane and ECL Plus chemiluminescent substrate were from GE Healthcare (Piscataway, NJ). Pierce® ECL 2 Western Blotting Substrate was from Thermo Scientific (Rockford, IL). Sodium phenylbutyrate (PBA) was from Enzo Life Sciences. Saturated phenol and phenol/chloroform/isoamyl alcohol were from Life Technologies (Grand Island, NY). The synthesis of 2-succinocysteamine (2SCEA) and preparation of polyclonal anti-2SC antibody has been described previously (Nagai 2007).

Tanis R.M., Piroli G.G., Day S.D, & Frizzell N. (2014). The Effect of Glucose Concentration and Sodium Phenylbutyrate Treatment on Mitochondrial Bioenergetics and ER Stress in 3T3-L1 Adipocytes. Biochimica et biophysica acta, 1853(1), 213-221.

+ Open protocol

+ Expand

Antibody and Tubulin Detection Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols

Unless otherwise noted, all chemicals were purchased from Sigma/Aldrich Chemical Co (St. Louis, MO & Milwaukee, WI). Criterion polyacrylamide gels and Precision Plus protein ladder were purchased from BioRad Laboratories (Richmond, CA). PVDF membrane and ECL Plus chemiluminescent substrate were from GE Healthcare (Piscataway, NJ). The synthesis of 2-succinocysteamine and preparation of polyclonal anti-2SC antibody has been described previously [2 (link)]. The following commercial antibodies were used: α-tubulin B-7 from Santa Cruz Biotechnology (Dallas, TX) and DM1A from Cell Signaling Technology, Inc. (Danvers, MA); β-tubulin TUB2.1 from Santa Cruz Biotechnology and D65A4 from Cell Signaling Technology, Inc.; combined αβ-tubulin ATN02 from Cytoskeleton, Inc. (Denver, CO); and actin I-19 from Santa Cruz Biotechnology.

Piroli G.G., Manuel A.M., Walla M.D., Jepson M.J., Brock J.W., Rajesh M.P., Tanis R.M., Cotham W.E, & Frizzell N. (2014). Identification of Protein Succination as a Novel Modification of Tubulin. The Biochemical journal, 462(2), 231-245.

+ Open protocol

+ Expand

SDS-PAGE Protein Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols

For initial protein characterization, an SDS-Polyacrylamide gel (SDS-PAGE) was generated using the Laemmli protocol. Briefly, 120 μg of each OPI solution was diluted in 50 μL of water and mixed with 10 μL of 6x Laemmli reducing buffer (ThermoFisher #J61337-AC). Solutions were heated to 95°C for 10 minutes, centrifuged at 13,000 g for 5 minutes, and 10 μL of solution was loaded into a 4–20% Tris-glycine gel (ThermoFisher #XP04200PK2) along with 3 μL of Precision Plus protein ladder (Bio-Rad #1610374), and gels were run at 125 V for 1.25 hours in Tris-Glycine running buffer (ThermoFisher #LC2675).

Stout A.J., Rittenberg M.L., Shub M., Saad M.K., Mirliani A.B., Dolgin J, & Kaplan D.L. (2023). A Beefy-R culture medium: replacing albumin with rapeseed protein isolates. Biomaterials, 296, 122092.

+ Open protocol

+ Expand

Western Blot Analysis of hGN Lysates

Check if the same lab product or an alternative is used in the 5 most similar protocols

hGN lysates were collected and boiled for 3 minutes in SDS sample buffer, resolved by SDS PAGE using 8–10% polyacrylamide gels and Precision Plus protein ladder (Biorad). Samples were then transferred to nitrocellulose and immunoblotted using primary antibodies (see antibodies above) at 1:1000 dilution, and then secondary 800nm DyLight-conjugated antibodies (Rockland Immunochemical 75934-472) at 1:50,000 dilution, prior to visualization and quantification with a Licor Odessy system. Original blot images provided as Supplementary Information.

Boulting G.L., Durresi E., Ataman B., Sherman M.A., Mei K., Harmin D.A., Carter A.C., Hochbaum D.R., Granger A.J., Engreitz J.M., Hrvatin S., Blanchard M.R., Yang M.G., Griffith E.C, & Greenberg M.E. (2021). Activity-dependent regulome of human GABAergic neurons reveals new patterns of gene regulation and neurological disease heritability. Nature neuroscience, 24(3), 437-448.

+ Open protocol

+ Expand

Western Blot Analysis of hGN Lysates

Check if the same lab product or an alternative is used in the 5 most similar protocols

+ 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?

Revolutionizing how scientists
search and build protocols!