Equilibration buffer 1

Manufactured by Bio-Rad

Sourced in United States

Equilibration Buffer I is a buffer solution used in various laboratory techniques, such as protein purification and chromatography. Its core function is to maintain the desired pH and ionic environment for the effective equilibration of samples or columns prior to analysis or separation steps. The buffer composition and properties are designed to optimize the performance of the specific laboratory application.

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Lab products found in correlation

Equilibration buffer 2, by Bio-Rad (2 mentions) Gs 800 calibrated densitometer, by Bio-Rad (2 mentions) Pdquest 8, by Bio-Rad (2 mentions) Rehydration sample buffer, by Bio-Rad (2 mentions) Readyprep 2 d cleanup kit, by Bio-Rad (1 mentions) Bio safe coomassie g 250 stain, by Bio-Rad (1 mentions) Readystrip ipg strip, by Bio-Rad (1 mentions) Protean ief system, by Bio-Rad (1 mentions)

Spelling variants of this product

Equilibration buffer (2 citations) Equilibration buffers I & II (2 citations)

3 protocols using equilibration buffer 1

Two-Dimensional Gel Electrophoresis of AEs

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A 100-µg portion of the AEs was prepared with a ReadyPrep 2-D Cleanup kit (Bio-Rad
Laboratories) and used for two-dimensional gel electrophoresis (2-DE). First-dimensional
isoelectric focusing (IEF) and second dimensional SDS-PAGE were performed in accordance
with the manufacturer’s instructions (Bio-Rad Laboratories). Samples were applied to
rehydrated immobilized pH gradient (IPG) strips (7-cm long, pH range 3–10, Japan Bio-Rad
Laboratories) in a focusing tray. Then, the focusing IPG strips were run (Step 1: 250 V,
30 min; Step 2: 4,000 V, 60 min; Step 3: 4,000 V, 10,000 V-h) at 20°C under mineral oil.
After focusing, the strips were equilibrated, first in equilibration buffer I (Bio-Rad
Laboratories) for 20 min, and then in equilibration buffer II (Bio-Rad Laboratories) for
10 min. The strips were placed on top of the second-dimension gel (Bio-Rad Laboratories),
and electrophoresis was performed at 200 V for 30 min. The gel was visualized by staining
with CBB, and the other gel was transferred to NCS for Western blotting as described
above. Sera of individuals Nos. 93 and 195 working in the plant showing the highest OD in
IgG and IgA ELISA were used for detecting the recognized antigens, respectively.

TANGKONDA E., KUBO M., SEKIGUCHI S., SHINKI T., SASAKI S., YAMADA K., TANIGUCHI T., VETCHAPITAK T, & MISAWA N. (2021). Work-related increases in titer of Campylobacter jejuni antibody among workers at a chicken processing plant in Miyazaki prefecture, Japan, independent of individual ingestion of edible raw chicken meat. The Journal of Veterinary Medical Science, 83(8), 1306-1314.

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Two-Dimensional Proteome Analysis of Mitochondria and Hippocampus

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From each cortex mitochondria and hippocampus sample (n = 6/subgroup), 250 μg of protein content was precipitated in ice-cold acetone, resuspended in 0.2 mL of Rehydration/Sample buffer (163-2106, Bio-Rad Laboratories, Hercules, CA, USA), and applied to Ready Strip IPG gel (11 cm, linear gradient between pH 3–10; Bio-Rad Laboratories, Hercules, CA, USA). The first dimension of the immobilized pH gradient of the IPG gel was carried out according to the manufacturer’s instructions.
After the first dimension, the IPG gel was equilibrated with Equilibration Buffer I (163-2107; Bio-Rad Laboratories, Hercules, CA, USA) for 15 min and further equilibrated an additional 15 min with Equilibrium Buffer II (163-2108; Bio-Rad Laboratories, Hercules, CA, USA) and 0.03 g/mL of iodoacetamide. Then, the IPG gel was subjected to second-dimensional SDS-PAGE separation using 12% gel. All the gels were stained with Bio-Safe Coomassie blue G-250 and images were captured by scanning the gels using GS-800 Calibrated Densitometer and densitometrically analyzed using PDQuest 8 software (all Bio-Rad Laboratories, Hercules, CA, USA).

Lysikova T., Tomascova A., Kovalska M., Lehotsky J., Leskova Majdova K., Kaplan P, & Tatarkova Z. (2024). Dynamics in Redox-Active Molecules Following Ischemic Preconditioning in the Brain. Neurology International, 16(3), 533-550.

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2D Gel Electrophoresis Proteome Analysis

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Samples (200 µg of protein content) were precipitated with ice-cold acetone and pelleted by centrifugation (16,000 × g for 10 min). After protein reconstitution in Rehydration/ Sample buffer (163-2106, Bio-Rad), they were applied to 7 cm linear ReadyStrip IPG strips with pH 3-10 (163-2000, Bio-Rad) and let to rehydrate overnight. Isoelectric focusing (IEF) was performed using Protean IEF system (Bio-Rad) in three-step protocol (250 V for 20 min, 4000 V for 2 hours and 4000 V until the total voltage reached 10,000 Vh). Prior to the second dimension separation, the strips were equilibrated in Equilibration Buffer I (163-2107, Bio-Rad) for 15 min and in Equilibration Buffer II (163-2108, Bio-Rad) with added 0.03 g/ml iodoacetamide for 15 min. Following equilibration, the IPG strips were placed on 12% polyacrylamide gels and covered with overlay agarose (163-2111, Bio-Rad). SDS-PAGE ran for 20 min at 15 mA and at 25 mA until the bromophenol blue dye reached the bottom of the gel using a Bio-rad mini electrophoresis system in tricine electrophoresis buffer. Gels were stained using Bio-Safe Coomassie G-250 stain (161-0786, Bio-Rad), scanned by GS-800 Calibrated Densitometer (Bio-Rad) and analysed using PDQuest 8 software (Bio-Rad).

Tomascova A., Lehotsky J., Kalenska D., Baranovicova E., Kaplan P, & Tatarkova Z. (2019). A comparison of albumin removal procedures for proteomic analysis of blood plasma. General physiology and biophysics, 38(4).

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