Review





Similar Products

superdex 200 increase 10 300 column  (Cytiva Europe)
99
Cytiva Europe superdex 200 increase 10 300 column
Superdex 200 Increase 10 300 Column, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/superdex+200+increase+10/pm42001940-309-11-16?v=Cytiva+Europe
Average 99 stars, based on 1 article reviews
superdex 200 increase 10 300 column - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier
superdex 200 increase 10 30 column  (Cytiva Europe)
99
Cytiva Europe superdex 200 increase 10 30 column
Superdex 200 Increase 10 30 Column, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/superdex+200+increase+10/pm41965334-238-22-27?v=Cytiva+Europe
Average 99 stars, based on 1 article reviews
superdex 200 increase 10 30 column - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier
superdex 200 increase 10 300 gl  (Cytiva Europe)
99
Cytiva Europe superdex 200 increase 10 300 gl
The second Calypso/Asx heterodimer facilitates efficient nucleosome processing (A) Comparison of the electron density maps of Calypso/Asx/NCP-ub and BAP1/ASXL1/NCP-ub, with the nucleosome positioned at the same angle. The resolution of BAP1/ASXL1/NCP-ub has been low-pass filtered. (B) Previously proposed ubiquitin-binding site and key residues are shown (doi, https://doi.org/10.1038/s41467-018-06186-1 ). (C) A cartoon representation illustrates that, building upon the established binding mode of Calypso-1/Asx-1 with nucleosome-ub-1, a second nucleosome-ub-2 was modeled onto the catalytic center of Calypso-2/Asx-2 using the binding configuration observed for Calypso-1/Asx-1 with nucleosome-ub-1. This modeling results in pronounced steric clashes in the nucleosomal region (indicated by red dashed lines). Subunit coloring is maintained consistently with the previous figures. (D) A close-up view showing the key amino acids of the two Calypso coiled-coil hairpins, with the model referenced from PDB: 6CGA . (E) SEC-MALS analysis of wild-type Calypso/Asx (1–340) (dimer) and mutant Calypso/Asx (1–340) (monomer), with the following mutations in Calypso: M288R, N292R, L340R. The gel filtration column is <t>Superdex</t> <t>200</t> 5/150. (F) Michaelis-Menten analysis of wild-type and mutant Calypso/Asx proteins cleavage of ubiquitin-AMC. Error bars indicate ±SEM ( n = 3 independent experiments). (G) Activity assays comparing the ability of wild-type (dimer), mutant (monomer) Calypso/Asx complexes to remove ubiquitin from nucleosomes mono-ubiquitinated at H2AK119. The H3 band was run on the same gel as a control.
Superdex 200 Increase 10 300 Gl, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/superdex+200+increase+10/pmc12955571-77-0-6?v=Cytiva+Europe
Average 99 stars, based on 1 article reviews
superdex 200 increase 10 300 gl - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier
superdex 200 increase 10 300 gl column  (Cytiva Europe)
99
Cytiva Europe superdex 200 increase 10 300 gl column
The second Calypso/Asx heterodimer facilitates efficient nucleosome processing (A) Comparison of the electron density maps of Calypso/Asx/NCP-ub and BAP1/ASXL1/NCP-ub, with the nucleosome positioned at the same angle. The resolution of BAP1/ASXL1/NCP-ub has been low-pass filtered. (B) Previously proposed ubiquitin-binding site and key residues are shown (doi, https://doi.org/10.1038/s41467-018-06186-1 ). (C) A cartoon representation illustrates that, building upon the established binding mode of Calypso-1/Asx-1 with nucleosome-ub-1, a second nucleosome-ub-2 was modeled onto the catalytic center of Calypso-2/Asx-2 using the binding configuration observed for Calypso-1/Asx-1 with nucleosome-ub-1. This modeling results in pronounced steric clashes in the nucleosomal region (indicated by red dashed lines). Subunit coloring is maintained consistently with the previous figures. (D) A close-up view showing the key amino acids of the two Calypso coiled-coil hairpins, with the model referenced from PDB: 6CGA . (E) SEC-MALS analysis of wild-type Calypso/Asx (1–340) (dimer) and mutant Calypso/Asx (1–340) (monomer), with the following mutations in Calypso: M288R, N292R, L340R. The gel filtration column is <t>Superdex</t> <t>200</t> 5/150. (F) Michaelis-Menten analysis of wild-type and mutant Calypso/Asx proteins cleavage of ubiquitin-AMC. Error bars indicate ±SEM ( n = 3 independent experiments). (G) Activity assays comparing the ability of wild-type (dimer), mutant (monomer) Calypso/Asx complexes to remove ubiquitin from nucleosomes mono-ubiquitinated at H2AK119. The H3 band was run on the same gel as a control.
Superdex 200 Increase 10 300 Gl Column, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/superdex+200+increase+10/pmc12988193-22-0-7?v=Cytiva+Europe
Average 99 stars, based on 1 article reviews
superdex 200 increase 10 300 gl column - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier
10 300 superdex 200 increase column  (Cytiva Europe)
99
Cytiva Europe 10 300 superdex 200 increase column
The second Calypso/Asx heterodimer facilitates efficient nucleosome processing (A) Comparison of the electron density maps of Calypso/Asx/NCP-ub and BAP1/ASXL1/NCP-ub, with the nucleosome positioned at the same angle. The resolution of BAP1/ASXL1/NCP-ub has been low-pass filtered. (B) Previously proposed ubiquitin-binding site and key residues are shown (doi, https://doi.org/10.1038/s41467-018-06186-1 ). (C) A cartoon representation illustrates that, building upon the established binding mode of Calypso-1/Asx-1 with nucleosome-ub-1, a second nucleosome-ub-2 was modeled onto the catalytic center of Calypso-2/Asx-2 using the binding configuration observed for Calypso-1/Asx-1 with nucleosome-ub-1. This modeling results in pronounced steric clashes in the nucleosomal region (indicated by red dashed lines). Subunit coloring is maintained consistently with the previous figures. (D) A close-up view showing the key amino acids of the two Calypso coiled-coil hairpins, with the model referenced from PDB: 6CGA . (E) SEC-MALS analysis of wild-type Calypso/Asx (1–340) (dimer) and mutant Calypso/Asx (1–340) (monomer), with the following mutations in Calypso: M288R, N292R, L340R. The gel filtration column is <t>Superdex</t> <t>200</t> 5/150. (F) Michaelis-Menten analysis of wild-type and mutant Calypso/Asx proteins cleavage of ubiquitin-AMC. Error bars indicate ±SEM ( n = 3 independent experiments). (G) Activity assays comparing the ability of wild-type (dimer), mutant (monomer) Calypso/Asx complexes to remove ubiquitin from nucleosomes mono-ubiquitinated at H2AK119. The H3 band was run on the same gel as a control.
10 300 Superdex 200 Increase Column, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/superdex+200+increase+10/pm41735302-211-24-29?v=Cytiva+Europe
Average 99 stars, based on 1 article reviews
10 300 superdex 200 increase column - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier

Image Search Results


The second Calypso/Asx heterodimer facilitates efficient nucleosome processing (A) Comparison of the electron density maps of Calypso/Asx/NCP-ub and BAP1/ASXL1/NCP-ub, with the nucleosome positioned at the same angle. The resolution of BAP1/ASXL1/NCP-ub has been low-pass filtered. (B) Previously proposed ubiquitin-binding site and key residues are shown (doi, https://doi.org/10.1038/s41467-018-06186-1 ). (C) A cartoon representation illustrates that, building upon the established binding mode of Calypso-1/Asx-1 with nucleosome-ub-1, a second nucleosome-ub-2 was modeled onto the catalytic center of Calypso-2/Asx-2 using the binding configuration observed for Calypso-1/Asx-1 with nucleosome-ub-1. This modeling results in pronounced steric clashes in the nucleosomal region (indicated by red dashed lines). Subunit coloring is maintained consistently with the previous figures. (D) A close-up view showing the key amino acids of the two Calypso coiled-coil hairpins, with the model referenced from PDB: 6CGA . (E) SEC-MALS analysis of wild-type Calypso/Asx (1–340) (dimer) and mutant Calypso/Asx (1–340) (monomer), with the following mutations in Calypso: M288R, N292R, L340R. The gel filtration column is Superdex 200 5/150. (F) Michaelis-Menten analysis of wild-type and mutant Calypso/Asx proteins cleavage of ubiquitin-AMC. Error bars indicate ±SEM ( n = 3 independent experiments). (G) Activity assays comparing the ability of wild-type (dimer), mutant (monomer) Calypso/Asx complexes to remove ubiquitin from nucleosomes mono-ubiquitinated at H2AK119. The H3 band was run on the same gel as a control.

Journal: iScience

Article Title: Structural basis of nucleosome deubiquitination by the bidentate Calypso/Asx complex

doi: 10.1016/j.isci.2026.114958

Figure Lengend Snippet: The second Calypso/Asx heterodimer facilitates efficient nucleosome processing (A) Comparison of the electron density maps of Calypso/Asx/NCP-ub and BAP1/ASXL1/NCP-ub, with the nucleosome positioned at the same angle. The resolution of BAP1/ASXL1/NCP-ub has been low-pass filtered. (B) Previously proposed ubiquitin-binding site and key residues are shown (doi, https://doi.org/10.1038/s41467-018-06186-1 ). (C) A cartoon representation illustrates that, building upon the established binding mode of Calypso-1/Asx-1 with nucleosome-ub-1, a second nucleosome-ub-2 was modeled onto the catalytic center of Calypso-2/Asx-2 using the binding configuration observed for Calypso-1/Asx-1 with nucleosome-ub-1. This modeling results in pronounced steric clashes in the nucleosomal region (indicated by red dashed lines). Subunit coloring is maintained consistently with the previous figures. (D) A close-up view showing the key amino acids of the two Calypso coiled-coil hairpins, with the model referenced from PDB: 6CGA . (E) SEC-MALS analysis of wild-type Calypso/Asx (1–340) (dimer) and mutant Calypso/Asx (1–340) (monomer), with the following mutations in Calypso: M288R, N292R, L340R. The gel filtration column is Superdex 200 5/150. (F) Michaelis-Menten analysis of wild-type and mutant Calypso/Asx proteins cleavage of ubiquitin-AMC. Error bars indicate ±SEM ( n = 3 independent experiments). (G) Activity assays comparing the ability of wild-type (dimer), mutant (monomer) Calypso/Asx complexes to remove ubiquitin from nucleosomes mono-ubiquitinated at H2AK119. The H3 band was run on the same gel as a control.

Article Snippet: Superdex 200 Increase 10/300 GL , Cytiva , Cat#28990944.

Techniques: Comparison, Ubiquitin Proteomics, Binding Assay, Mutagenesis, Filtration, Activity Assay, Control