Log In Sign up
The largest database of trusted experimental protocols

One step blue protein gel stain

Manufactured by Biotium
Visit Supplier
Sourced in United States

One-Step Blue Protein Gel Stain is a ready-to-use solution for staining proteins in polyacrylamide gels. It provides a simple and efficient method for visualizing protein bands after electrophoresis.

Automatically generated - may contain errors

Lab products found in correlation

Methionine, by Thermo Fisher Scientific (2 mentions) Cystine, by Thermo Fisher Scientific (2 mentions) Anisomycin, by Cell Signaling Technology (2 mentions) Hrp conjugated streptavidin, by Thermo Fisher Scientific (2 mentions) Dialyzed fbs, by Thermo Fisher Scientific (2 mentions) Biotin alkyne, by Vector Laboratories (2 mentions) L azidohomoalanine, by Vector Laboratories (2 mentions) Click go click chemistry reaction buffer kit, by Vector Laboratories (2 mentions) L methionine, by Merck Group (2 mentions) Penicillin streptomycin, by Thermo Fisher Scientific (2 mentions) Glutamax, by Thermo Fisher Scientific (2 mentions) L cysteine, by Merck Group (2 mentions) Mops sds running buffer, by Thermo Fisher Scientific (1 mentions) Lds sample buffer, by Thermo Fisher Scientific (1 mentions) Nupage bis tris gel, by Thermo Fisher Scientific (1 mentions) Pngase f, by New England Biolabs (1 mentions) Bolt 4 to 12 bis tris gel, by Thermo Fisher Scientific (1 mentions) Human antibody capture kit, by Cytiva (1 mentions) Hp1100 system, by Agilent Technologies (1 mentions) Biacore t200, by Cytiva (1 mentions)

8 protocols using one step blue protein gel stain

1

Topoisomerase Charging Assay with Mutants

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

Example 1

Topoisomerase (30 pmoles) is incubated with 20 pmoles of ShuBT cassette, 50 mM Tris, pH=7.4, and the designated concentration of NaCl in a 20 ul volume for 15 minutes at 37.C. Five microliters of LDS Sample Buffer (Thermo-Fisher) is added to quench the reaction, and all of the sample is loaded onto a 4-12% Bis-Tris PAGE gel with 1× MOPS SDS running buffer (Thermo-Fisher). The gel is stained overnight with 1× One-Step Blue Protein Gel Stain (Biotium) and imaged.

FIG. 2 depicts this charging reaction with various vaccinia topoisomerases (wild type, Q69A/R80A double mutant, R67A/Q69A/R80A and R67A/Y70A/R80A triple mutants at varying concentrations of NaCl. These results demonstrate that wild type topoisomerase can charge a cassette in >250 mM NaCl, whereas the mutants are more sensitive to NaCl concentrations (69/80-150 mM NaCl; 67/69/80-<100 mM NaCl; 67/70/80-<100 mM NaCl).

US11655465B1. Enzymes and systems for synthesizing DNA (2023-05-23). IRIDIA, INC. [US]. Inventors: Paul F. Predki [US], Stefen Boehme [US].
+ Open protocol
+ Expand
2

Deglycosylation of SARS-CoV-2 Spike Protein

Check if the same lab product or an alternative is used in the 5 most similar protocols
To deglycosylate S protein of virions, 20 μg purified virion sample was treated with 500 units PNGase F (New England Biolabs, Ipswich, MA) at 37°C for 1 hour. 20 μg of treated and untreated samples were kept at 100°C for 15 min. Deglycosylation of S protein was characterized by 4 to 12% NuPAGE Bis-Tris gel (Invitrogen,Carlsbad, CA). The protein band was stained by One-Step Blue Protein Gel Stain (Biotium, Fremont, CA).
Yao H., Song Y., Chen Y., Wu N., Xu J., Sun C., Zhang J., Weng T., Zhang Z., Wu Z., Cheng L., Shi D., Lu X., Lei J., Crispin M., Shi Y., Li L, & Li S. (2020). Molecular Architecture of the SARS-CoV-2 Virus. Cell, 183(3), 730-738.e13.
+ Open protocol
+ Expand
3

Measuring Newly Synthesized Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were grown to ~80% confluency at the time of assay. Complete medium was replaced by AHA medium formulated with DMEM, high glucose, no glutamine, no methionine, no cystine (Gibco), 10% dialyzed FBS (Gibco), 1% GlutaMAX (Gibco), 1% Penicillin-Streptomycin (Gibco), 62.6 mg/L L-Cysteine (Sigma), 250uM L-Azidohomoalanine (AHA, Click Chemistry Tools). For non-AHA control, the AHA was replaced by 30 mg/L L-methionine (Sigma). For Anisomycin (ANS) treatment, AHA medium was further added with 10 μg/mL Anisomycin (Cell Signaling). After 3 h of incubation, cells were scraped in cold DPBS, washed twice with cold DPBS and lysed in RIPA buffer. Protein concentration of the lysate was quantified by BCA and input protein concentrations were normalized to 2.1 mg/mL for downstream click chemistry. 50μL of the normalized cell lysate was used for click reaction with biotin-Alkyne (Click Chemistry Tools) by using Click-&-Go Click Chemistry Reaction Buffer Kit (Click Chemistry Tools). The reaction mixture was then methanol precipitated and was resuspended in 2xLaemmi buffer (BIO-RAD) with 2-mercaptoethanol (BIO-RAD) and denatured at 95°C for 10 min. Final protein concentration is 1 mg/mL. The sample was then resolved by SDS–PAGE, and total protein signal was detected by One-Step Blue Protein Gel Stain (Biotium). The biotin signal was detected by HRP-Conjugated Streptavidin (Thermo Scientific).
Ni C., Schmitz D.A., Lee J., Pawłowski K., Wu J, & Buszczak M. (2022). Labeling of heterochronic ribosomes reveals C1ORF109 and SPATA5 control a late step in human ribosome assembly. Cell reports, 38(13), 110597.
+ Open protocol
+ Expand
4

Tricine SDS-PAGE Protein Separation

Check if the same lab product or an alternative is used in the 5 most similar protocols
An aliquot of 20 μg proteins was dissolved with loading buffer (50 mmol/l Tris-HCl, pH 6.8, 2% SDS, 10% glycerol, 0.1% bromophenol blue, and 1% β-mercaptoethanol). After denaturation for 5 min at 95 °C, the protein samples were loaded onto homemade 10% tricine SDS-PAGE gels (15 (link)) and ran at 120 V for 80 min. The gel was stained with One-Step Blue Protein Gel Stain (BIOTIUM) and then washed with distilled water.
Zhang Q., Wu E., Tang Y., Cai T., Zhang L., Wang J., Hao Y., Zhang B., Zhou Y., Guo X., Luo J., Chen R, & Yang F. (2021). Deeply Mining a Universe of Peptides Encoded by Long Noncoding RNAs. Molecular & Cellular Proteomics : MCP, 20, 100109.
+ Open protocol
+ Expand
5

Recombinant SARS-CoV-2 RBD Production

Check if the same lab product or an alternative is used in the 5 most similar protocols
The antigen was produced in a bioreactor based on a selected stable CHO clone. A fed-batch strategy was used for high-cell-density cultivation and expression of the RBD fusion heterodimer. Upon harvest, the cell broth was clarified by depth filtration. The clarified supernatant was further purified via sequential chromatography. The purified antigen was then buffer exchanged by tangential flow filtration and filter sterilised. Purity and integrity were evaluated by SDS-PAGE with Bolt™ 4 to 12% Bis-Tris gels (Thermo Fisher, ref. NW04120BOX), stained with One-Step Blue Protein Gel Stain (Biotium, ref. 21003), and by SEC-HPLC with an Xbridge Protein BEH SEC (Waters, ref. 186009160) connected to an HP1100 system (Agilent Technologies).
The affinity test of the RBD heterodimer with human ACE2 by surface plasmon resonance (SPR) was performed by ACROBiosystems. The Fc-tagged ACE2 (AC2-H5257, ACROBiosystems) was immobilised in a Series S Sensor Chip CM5 (Cytiva) on a Biacore T200 (Cytiva) using the Human Antibody Capture Kit (Cytiva). The affinity measure was obtained using 8 different RBD heterodimer concentrations. The antigen structure simulations were performed with UCSF ChimeraX.53 (link)
Barreiro A., Prenafeta A., Bech-Sabat G., Roca M., Perozo Mur E., March R., González-González L., Madrenas L., Corominas J., Fernández A., Moros A., Cañete M., Molas M., Pentinat-Pelegrin T., Panosa C., Moreno A., Puigvert Molas E., Pol Vilarrassa E., Palmada J., Garriga C., Prat Cabañas T., Iglesias-Fernández J., Vergara-Alert J., Lorca-Oró C., Roca N., Fernández-Bastit L., Rodon J., Pérez M., Segalés J., Pradenas E., Marfil S., Trinité B., Ortiz R., Clotet B., Blanco J., Díaz Pedroza J., Ampudia Carrasco R., Rosales Salgado Y., Loubat-Casanovas J., Capdevila Larripa S., Prado J.G., Barretina J., Sisteré-Oró M., Cebollada Rica P., Meyerhans A, & Ferrer L. (2023). Preclinical evaluation of a COVID-19 vaccine candidate based on a recombinant RBD fusion heterodimer of SARS-CoV-2. iScience, 26(3), 106126.
+ Open protocol
+ Expand
6

Tubulin-Drug Interaction Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
Purified tubulins (20 μg) were incubated with drugs (100 μm) in reaction buffer (80 mm PIPES pH 6.9, 2 mm MgCl2, 0.5 mm EGTA, 1 mm GTP, and 10.2% glycerol) at 30 °C for 30 min. Then, tubulins and tubulin‐drug complexes were digested on ice for 20 min with 20 μg·mL−1 L‐(tosylamido‐2‐phenyl) ethyl chloromethyl ketone (TPCK)‐treated trypsin (1 : 40, w/w to tubulin). TPCK was used to inhibit contaminating chymotryptic activity. The reaction mixture was mixed with 1× SDS sample buffer and boiled for 5 min, and then resolved on 7.5% and 15% SDS/PAGE. Tubulins and drug‐tubulin complexes were visualized using the One‐Step Blue Protein Gel Stain (#21003‐1L; Biotium, Hayward, CA, USA).
Hsieh Y., Du J, & Yang P. (2023). Repositioning VU‐0365114 as a novel microtubule‐destabilizing agent for treating cancer and overcoming drug resistance. Molecular Oncology, 18(2), 386-414.
+ Open protocol
+ Expand
7

OVA-CpG Conjugation via Click Chemistry

Check if the same lab product or an alternative is used in the 5 most similar protocols
The OVA-CpG conjugate was prepared using azide-alkyne click chemistry. To a 1 mg/mL solution of OVA-2pAMF was added 2.5 eq CpG-DBCO (from the 1 mg/mL stock) at 35 °C for 48 h. Unreacted CpG-DBCO was removed by passing the crude thrice through a 30 k MWCO Amicon centrifugal filter. The purified product was characterized by SDS-PAGE gel electrophoresis. Samples were treated with 2.5% β-mercaptoethanol, heated to 90 °C, and separated by SDS-PAGE gel. Gels were stained with One-Step Blue Protein Gel Stain (Biotium), and imaged with an Azure c600 Imager (Azure Biosystems). Reaction extent was determined using ImageJ.
Weiss A.M., Ajit J., Albin T.J., Kapoor N., Maroju S., Berges A., Pill L., Fairman J, & Esser-Kahn A.P. (2021). Site-specific antigen-adjuvant conjugation using cell-free protein synthesis enhances antigen presentation and CD8+ T-cell response. Scientific Reports, 11, 6267.
+ Open protocol
+ Expand
8

Measuring Newly Synthesized Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were grown to ~80% confluency at the time of assay. Complete medium was replaced by AHA medium formulated with DMEM, high glucose, no glutamine, no methionine, no cystine (Gibco), 10% dialyzed FBS (Gibco), 1% GlutaMAX (Gibco), 1% Penicillin-Streptomycin (Gibco), 62.6 mg/L L-Cysteine (Sigma), 250uM L-Azidohomoalanine (AHA, Click Chemistry Tools). For non-AHA control, the AHA was replaced by 30 mg/L L-methionine (Sigma). For Anisomycin (ANS) treatment, AHA medium was further added with 10 μg/mL Anisomycin (Cell Signaling). After 3 h of incubation, cells were scraped in cold DPBS, washed twice with cold DPBS and lysed in RIPA buffer. Protein concentration of the lysate was quantified by BCA and input protein concentrations were normalized to 2.1 mg/mL for downstream click chemistry. 50μL of the normalized cell lysate was used for click reaction with biotin-Alkyne (Click Chemistry Tools) by using Click-&-Go Click Chemistry Reaction Buffer Kit (Click Chemistry Tools). The reaction mixture was then methanol precipitated and was resuspended in 2xLaemmi buffer (BIO-RAD) with 2-mercaptoethanol (BIO-RAD) and denatured at 95°C for 10 min. Final protein concentration is 1 mg/mL. The sample was then resolved by SDS–PAGE, and total protein signal was detected by One-Step Blue Protein Gel Stain (Biotium). The biotin signal was detected by HRP-Conjugated Streptavidin (Thermo Scientific).
Ni C., Schmitz D.A., Lee J., Pawłowski K., Wu J, & Buszczak M. (2022). Labeling of heterochronic ribosomes reveals C1ORF109 and SPATA5 control a late step in human ribosome assembly. Cell reports, 38(13), 110597.
+ 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!