Hybond pvdfmembranes

Manufactured by Cytiva

Sourced in United Kingdom

Hybond PVDF membranes are made of polyvinylidene fluoride (PVDF) material. They are designed for protein transfer and western blotting applications. The membranes have a high protein binding capacity and are suitable for use with a variety of detection methods.

Automatically generated - may contain errors

Lab products found in correlation

Anti h3k36me3, by Abcam (1 mentions) Anti cleaved caspase 7, by Cell Signaling Technology (1 mentions) Anti h3k4me3, by Merck Group (1 mentions) Anti egfr, by Santa Cruz Biotechnology (1 mentions) Anti phospho egfr, by Cell Signaling Technology (1 mentions) Anti idh1, by Cell Signaling Technology (1 mentions) Anti akt, by Cell Signaling Technology (1 mentions) Anti cleaved caspase 3, by Cell Signaling Technology (1 mentions) Sds page, by Thermo Fisher Scientific (1 mentions) Anti phospho akt, by Cell Signaling Technology (1 mentions) Anti hsp70, by BD (1 mentions) Anti me1, by Abcam (1 mentions) Anti histone h3, by Cell Signaling Technology (1 mentions) Anti h3k9me3, by Active Motif (1 mentions) Anti h3k27me3, by Merck Group (1 mentions) Bead mill 24, by Thermo Fisher Scientific (1 mentions) Ripa buffer, by Fujifilm (1 mentions) Imagequant las 500, by GE Healthcare (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Chemiluminescence assay, by Merck Group (1 mentions)

3 protocols using hybond pvdfmembranes

Quantitative Western Blot Analysis

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

For all Western Blot analyses, proteins were separated by
4–12% SDS/PAGE (Life Technologies), transferred to Hybond PVDF
membranes (Amersham), blocked with 5% milk in PBS with 0.1%
Tween 20 (PBS/Tween) for 1 hr, and incubated with the following antibodies:
anti-cleaved caspase-3 (Cell Signaling, 9664), anti-cleaved caspase-7 (Cell
Signaling, 9491), anti-Hsp70 (BD Pharmingen, 610607), anti-IDH1 (Cell Signaling,
8137), anti-H3K4me3 (Millipore, CS200580), anti-H3K9me3 (Active Motif, 39161),
anti-H3K27me3 (Millipore, CS200603), anti-H3K36me3 (Abcam, ab9050), anti-Histone
H3 (Cell Signaling, 4499), anti-ME1 (Abcam, ab97445), anti-FoxO6 (Thermo
Scientific PA5–35117), anti-phospho-FoxO6 (Abcam, ab154832),
anti-phospho-EGFR (Cell Signaling, 2236S), anti-EGFR (Santa Cruz, sc-373746),
anti-phospho-Akt (Cell Signaling, 4060S), and anti-Akt (Cell Signaling, 9272S).
The blots were subsequently incubated with goat anti-rabbit IgG or goat
anti-mouse IgG antibodies (Santa Cruz) in 5% milk in PBS/Tween and
developed with Supersignal West Dura ECL (enhanced chemiluminescence) substrate
(Pierce) following manufacturer’s protocol. Quantification of blots was
determined by densitometry using ImageJ software.

Calvert A.E., Chalastanis A., Wu Y., Hurley L.A., Kouri F.M., Bi Y., Kachman M., May J.L., Bartom E., Hua Y., Mishra R.K., Schiltz G.E., Dubrovskyi O., Mazar A.P., Peter M.E., Zheng H., James C.D., Burant C.F., Chandel N.S., Davuluri R.V., Horbinski C, & Stegh A.H. (2017). Cancer-associated IDH1 promotes growth and resistance to targeted therapies in the absence of mutation. Cell reports, 19(9), 1858-1873.

+ Open protocol

+ Expand

Protein Expression Analysis in Skin Tissues

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

The frozen skin tissue samples were dissolved in RIPA buffer (Wako, Osaka, Japan) containing a protease inhibitor cocktail (Sigma-Aldrich, Darmstadt, Germany), homogenized using Bead Mill 24 (Thermo Fisher Scientific), and sonicated. The solubilized sample was collected by centrifugation at 16,900g for 10 minutes. After adjusting the protein concentration (1 ng/ml) using a bicinchoninic acid protein assay kit (Pierce, Rockford, IL), the samples (20 μg/lane) were fractionated by SDS-PAGE and transferred to Hybond-PVDF membranes (Amersham Bioscience, Piscataway, NJ). The blotted membranes were blocked with Tris-buffered saline containing 0.1% Tween-20 and 10% skimmed milk and subsequently incubated overnight at 4 °C with anti-Ninj1 or anti-GAPDH antibodies (Table 1). The target protein bands were visualized using horseradish peroxidase‒conjugated secondary antibodies and quantified using ImageQuant LAS500 (GE Healthcare Life Science, Chicago, IL). ImageJ program was used for densitometry analysis.

Matsuo R., Kishibe M., Horiuchi K., Kano K., Tatsukawa T., Hayasaka T., Kabara M., Iinuma S., Eguchi R., Igawa S., Hasebe N., Ishida-Yamamoto A, & Kawabe J.I. (2022). Ninjurin1 Deletion in NG2-Positive Pericytes Prevents Microvessel Maturation and Delays Wound Healing. JID Innovations, 2(6), 100141.

+ Open protocol

+ Expand

Protein Expression Analysis of Pancreatic Tumors in Mice

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

Pancreatic tumors in mice were collected and sonicated with lysis buffer, and the protein content was determined using the Bradford assay. An aliquot of the protein solution (10 μg) in each mouse was subjected to sodium dodecyl sulfate-10% polyacrylamide gel electrophoresis (SDS-PAGE), and then electroblotted onto Hybond PVDF membranes (Amersham Bioscience, Little Chalfont, UK). The PVDF membrane was incubated with Tris-buffered saline containing 0.1% Tween 20 and 1 w/v% BSA (1% BSA/TBS-T) at room temperature for 1 h and treated with each primary antibody (diluted 1:1000) in 1% BSA/TBS-T at 4 °C overnight. Subsequently, the membranes were incubated with HRP-conjugated anti-mouse or anti-rabbit secondary antibody-HRP conjugates in 1% BSA/TBS-T at room temperature for 1 h. Protein bands were detected using a chemiluminescence assay (Millipore, Billerica, MA, USA).

Murase W., Kamakura Y., Kawakami S., Yasuda A., Wagatsuma M., Kubota A., Kojima H., Ohta T., Takahashi M., Mutoh M., Tanaka T., Maeda H., Miyashita K, & Terasaki M. (2021). Fucoxanthin Prevents Pancreatic Tumorigenesis in C57BL/6J Mice That Received Allogenic and Orthotopic Transplants of Cancer Cells. International Journal of Molecular Sciences, 22(24), 13620.

+ 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!