GelHP Protein Gel (Tris-Gly, 8%, 10 well) 

MCE GelHP Protein Gel offers a safe, convenient, and high‑performance solution for protein separation, suitable for both PAGE and Western blot analysis.

Features of MCE GelHP Protein Gel

1. Coated plastic gel plates effectively minimize non‑specific protein adsorption, delivering sharper and clearer bands.

2. Easy‑open cassette design - gel plates can be pried open effortlessly with a gel opener.

3. SDS‑free formulation, compatible with both denaturing and native PAGE.

4. Fully automated gel casting production ensures high batch‑to‑batch stability and reproducibility.

5. Compatible with most mainstream mini gel electrophoresis systems, including Bio‑Rad, Invitrogen, Tanon, Junyi Oriental, and Beijing Liuyi.

6. Available in multiple uniform concentrations (10%, 12%, 15%) and gradient concentrations (4-15%, 4-20%, 8-16%, 8-20%).

4°C, 1 year.

Do Not Freeze

Shipping at room temperature

Native‑PAGE Electrophoresis Procedure (Native-PAGE)

1. Remove the protein precast gel from the package and peel off the sealing tape at the bottom.

2. Insert the precast gel into the core of the electrophoresis tank.

3. Add 1× Tris-Glycine Native Running Buffer into the electrophoresis tank. Ensure the inner chamber is completely filled, and the outer chamber buffer covers at least 1/3 of the gel plate height, but does not exceed the top of the gel. Then carefully and slowly remove the comb in a parallel direction.

Note: If wells are slanted, gently adjust them using a fine pipette tip or needle.

4. Rinse each sample well gently with a pipette to remove any residual gel solution.

5. Sample preparation: Mix native protein samples thoroughly with native sample loading buffer.

6. Sample loading: Load the prepared samples into the wells vertically and slowly using a pipette. Avoid puncturing the gel or inserting the pipette tip too deep, which may cause gel deformation or leakage.

Note: Acidic proteins (pI < 7) can be loaded and electrophoresed under standard polarity. Basic proteins (pI > 7), being positively charged, require reversed electrode connections (red to black, black to red), in which case the sample wells become the anode and the proteins migrate downward.

7. Running: Connect the power supply and run at a constant voltage of 180 V. Stop electrophoresis when the bromophenol blue tracking dye reaches the bottom of the gel or the desired position.

8. After electrophoresis, remove the gel cassette. Use a Gel Opener (HY-K1139) to gently pry open the sides of the plates and carefully retrieve the gel.

Note: In native PAGE, protein mobility is influenced by multiple factors, including molecular weight and three‑dimensional structure.

Denaturing Electrophoresis (SDS-PAGE)

1. Remove the protein precast gel from the package and peel off the sealing tape at the bottom.

2. Insert the precast gel into the core of the electrophoresis tank.

3. Add 1× Tris‑Glycine-SDS Running Buffer to the electrophoresis tank. Ensure the inner chamber is completely filled, and the outer chamber buffer covers at least 1/3 of the gel plate height, but does not exceed the top of the gel. Then carefully and slowly remove the comb in a parallel direction.

Note: If wells are slanted, gently adjust them using a fine pipette tip or needle.

4. Rinse each sample well gently with a pipette to remove any residual gel solution.

5. Sample preparation: Mix protein samples with sample loading buffer thoroughly.

6. Sample loading: Load the prepared samples into the wells vertically and slowly using a pipette. Avoid puncturing the gel or inserting the pipette tip too deep, which may cause gel deformation or leakage.

7. Running: Connect the power supply and run at a constant voltage of 180 V. Stop electrophoresis when the bromophenol blue tracking dye reaches the bottom of the gel or the desired position.

8. After electrophoresis, remove the gel cassette. Use a Gel Opener (HY-K1139) to gently pry open the sides of the plates and carefully retrieve the gel.

1. Store the product in a cool place at ambient temperature, avoiding direct sunlight and sudden temperature fluctuations.

2. Do not store the product below 0°C. Exposure to temperatures below 0°C will cause the gel to freeze, resulting in bubbles and cracks, which will render the gel unusable.

3. Tris‑Gly gels should be used with the corresponding Tris‑Gly Running Buffer System (HY‑K1020).

4. For sharper and straighter protein bands, reduce the voltage to 150  V and extend the running time as needed.

5. When running at 180  V, the initial current is approximately 75  mA for a single gel and 150 mA for two gels, decreasing gradually during the run.

6. Reuse of running buffer is not recommended. After electrophoresis, the ionic strength and buffering capacity of the buffer will change, potentially affecting separation performance.

7. Recommended wet transfer conditions: 120  V constant voltage for 60-90 min. For optimal transfer efficiency, evaluate transfer performance using the pre‑stained marker bands on both the gel and the membrane, and adjust conditions as needed. Transfer efficiency is influenced by factors such as target protein molecular weight, gel concentration, and methanol concentration in the transfer buffer. It is recommended to use a low-percentage gel for high-molecular-weight proteins.

8. This product is for R&D use only, not for drug, household, or other uses.

9. For your safety and health, please wear a lab coat and disposable gloves to operate.