Log In Sign up
The largest database of trusted experimental protocols

Nucleoporin 62

Manufactured by Santa Cruz Biotechnology
Visit Supplier

Nucleoporin 62 is a protein component of the nuclear pore complex, which is a large multi-protein structure that mediates the transport of molecules between the nucleus and cytoplasm in eukaryotic cells. The Nucleoporin 62 protein plays a crucial role in the structural integrity and function of the nuclear pore complex.

Automatically generated - may contain errors

Lab products found in correlation

Tris acetate gel, by Thermo Fisher Scientific (1 mentions) Fancd2, by Santa Cruz Biotechnology (1 mentions) Supersignal west pico, by Thermo Fisher Scientific (1 mentions) α tubulin, by Merck Group (1 mentions) Nuclear extract kit, by Active Motif (1 mentions) Abcg2, by Cell Signaling Technology (1 mentions) Cd133, by Cell Signaling Technology (1 mentions) Epcam, by Cell Signaling Technology (1 mentions) Aldh1, by Cell Signaling Technology (1 mentions) Nanog, by Cell Signaling Technology (1 mentions) Mdr1 abcb1, by Cell Signaling Technology (1 mentions) Aldh1 2, by Santa Cruz Biotechnology (1 mentions) Epas 1, by Santa Cruz Biotechnology (1 mentions) Hif 1α, by Cell Signaling Technology (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Pvdf membrane, by Bio-Rad (1 mentions)

2 protocols using nucleoporin 62

1

Subcellular Fractionation and Protein Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Nuclear and cytoplasmic fractions were isolated using a Nuclear Extract Kit (Active Motif, Carlsbad, CA, version C4) per manufacturer’s instructions. This separates the fractions by hypotonic lysis of the cytoplasm, to isolate cytoplasmic proteins, followed by complete lysis of nuclei via detergent and denaturation of each fraction. Purified fractions were assayed for protein concentration using a Bradford-based method (BioRad) and prepared for electrophoretic separation of proteins in both nuclear and cytoplasmic fractions. Samples were denatured in reducing buffer, heated to 95°C for 10 minutes, and run on a 3–8% Tris-Acetate gel (Invitrogen; Carlsbad, CA). Following SDS/PAGE, proteins were transferred to nitrocellulose membranes, which were probed for FANCD2 (1:100) and nucleoporin 62 (1:200) (Santa Cruz Biotechnology; Santa Cruz, CA) or α-tubulin (1:900) (Sigma,-Aldrich, St. Louis, MO) as an additional loading control. HRP-conjugated secondary antibodies were then used for signal detection. Bands were visualized using Supersignal West Pico and West Femto chemiluminescence (ThermoScientific; Rockford IL) on Blue Basic Autorad film (BioExpress; Kaysville, UT).
Joshi S., Campbell S., Lim J.Y., McWeeney S., Krieg A., Bean Y., Pejovic N., Mhawech-Fauceglia P, & Pejovic T. (2020). Subcellular localization of FANCD2 is associated with survival in ovarian carcinoma. Oncotarget, 11(8), 775-783.
+ Open protocol
+ Expand
2

Western Blot Analysis of Stem Cell Markers

Check if the same lab product or an alternative is used in the 5 most similar protocols
Total cell lysates were obtained by adding RIPA buffer (R0728, Sigma-Aldrich) and protease inhibitor cocktail (P2714, Sigma-Aldrich). Equilibrated protein samples were loaded into a 10% SDS-Page gel, electrophoresed and then electro-transferred to a PVDF membrane (Bio-Rad). Transferred membranes were blocked with a blocking buffer containing 5% non-fat milk (Labscientific, M0841). The following monoclonal antibodies were used: Nanog (Cell Signaling, D73G4), CD133 (Cell Signaling, D2V8Q), CD44 (Cell Signaling, 8E2), ALDH1/2 (Santa Cruz, sc-166362), ALDH1 (Cell Signaling, D9J7R), MDR1/ABCB1 (Cell Signaling, E1Y7B), HIF1-α (Cell Signaling, D5F3M), ABCG2 (Cell Signaling, D5V2K), nucleoporin-62 (Santa Cruz, sc-48373), EpCAM (Cell Signaling, VU1D9) and EPAS-1 (Santa Cruz, 190B). Target proteins were visualized with the secondary mouse or rabbit IgG antibodies and a chemiluminescent substrate (Santa Cruz, sc-2048). All Western blot results were normalized by total protein (Fig. S5). All Western blot experiments were reproduced and performed three times for quantification.
Shen Q., Hill T., Cai X., Bui L., Barakat R., Hills E., Almugaiteeb T., Babu A., Mckernan P.H., Zalles M., Battiste J.D, & Kim Y.T. (2021). Physical Confinement during Cancer Cell Migration Triggers Therapeutic Resistance and Cancer Stem Cell-like Behavior. Cancer letters, 506, 142-151.
+ 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!