eif3m antibody Search Results


anti eif3m  (Novus Biologicals)
94
Novus Biologicals anti eif3m
Anti Eif3m, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti eif3m/product/Novus Biologicals
Average 94 stars, based on 1 article reviews
anti eif3m - by Bioz Stars, 2026-03
94/100 stars
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eif3m antibody  (Bio-Techne corporation)
90
Bio-Techne corporation eif3m antibody
Eif3m Antibody, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/eif3m antibody/product/Bio-Techne corporation
Average 90 stars, based on 1 article reviews
eif3m antibody - by Bioz Stars, 2026-03
90/100 stars
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eif3m  (Proteintech)
93
Proteintech eif3m
A Complex model of Rpt5 ( P17980 , residues 166–439) and PSMD9 ( O00233 ), with full torsional freedom allowed for the linker residues (115–134) between PSMD9’s two domains. B AlphaFold model of free PSMD9, with the backbone colored according to pLDDT values (yellow, <70; orange, <50). The arrow indicates the direction of domain closure upon binding to Rpt5. C AlphaFold-modeled complex structure between Rpn5 ( O00232 ), <t>EIF3M</t> ( Q7L2H7 ), and Rpn8 ( P51665 ), shown in two different perspectives. The sequence and structure comparison between EIF3M and Rpn9 ( Q9UNM6 ) are shown in Supplementary Fig. . Dashed lines indicate experimental intermolecular cross-links, with associated Lys residues denoted.
Eif3m, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/eif3m/product/Proteintech
Average 93 stars, based on 1 article reviews
eif3m - by Bioz Stars, 2026-03
93/100 stars
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anti eif3m bethyl a304 761a  (Bethyl)
90
Bethyl anti eif3m bethyl a304 761a
A Complex model of Rpt5 ( P17980 , residues 166–439) and PSMD9 ( O00233 ), with full torsional freedom allowed for the linker residues (115–134) between PSMD9’s two domains. B AlphaFold model of free PSMD9, with the backbone colored according to pLDDT values (yellow, <70; orange, <50). The arrow indicates the direction of domain closure upon binding to Rpt5. C AlphaFold-modeled complex structure between Rpn5 ( O00232 ), <t>EIF3M</t> ( Q7L2H7 ), and Rpn8 ( P51665 ), shown in two different perspectives. The sequence and structure comparison between EIF3M and Rpn9 ( Q9UNM6 ) are shown in Supplementary Fig. . Dashed lines indicate experimental intermolecular cross-links, with associated Lys residues denoted.
Anti Eif3m Bethyl A304 761a, supplied by Bethyl, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti eif3m bethyl a304 761a/product/Bethyl
Average 90 stars, based on 1 article reviews
anti eif3m bethyl a304 761a - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


A Complex model of Rpt5 ( P17980 , residues 166–439) and PSMD9 ( O00233 ), with full torsional freedom allowed for the linker residues (115–134) between PSMD9’s two domains. B AlphaFold model of free PSMD9, with the backbone colored according to pLDDT values (yellow, <70; orange, <50). The arrow indicates the direction of domain closure upon binding to Rpt5. C AlphaFold-modeled complex structure between Rpn5 ( O00232 ), EIF3M ( Q7L2H7 ), and Rpn8 ( P51665 ), shown in two different perspectives. The sequence and structure comparison between EIF3M and Rpn9 ( Q9UNM6 ) are shown in Supplementary Fig. . Dashed lines indicate experimental intermolecular cross-links, with associated Lys residues denoted.

Journal: Nature Communications

Article Title: In-situ cross-linking mass spectrometry reveals compartment-specific proteasomal interactions and structural heterogeneity

doi: 10.1038/s41467-025-65752-6

Figure Lengend Snippet: A Complex model of Rpt5 ( P17980 , residues 166–439) and PSMD9 ( O00233 ), with full torsional freedom allowed for the linker residues (115–134) between PSMD9’s two domains. B AlphaFold model of free PSMD9, with the backbone colored according to pLDDT values (yellow, <70; orange, <50). The arrow indicates the direction of domain closure upon binding to Rpt5. C AlphaFold-modeled complex structure between Rpn5 ( O00232 ), EIF3M ( Q7L2H7 ), and Rpn8 ( P51665 ), shown in two different perspectives. The sequence and structure comparison between EIF3M and Rpn9 ( Q9UNM6 ) are shown in Supplementary Fig. . Dashed lines indicate experimental intermolecular cross-links, with associated Lys residues denoted.

Article Snippet: The following antibodies were used: EIF3M (Proteintech, 11423-1-AP), RPS5 (Santa Cruz, sc-390935), and a control IgG antibody (Proteintech, 30000-0-AP, 1:200 dilution).

Techniques: Binding Assay, Sequencing, Comparison

A Co-immunoprecipitation confirms that EIF3M interacts with Rpn11, a proteasomal subunit, and with Rps5, a component of the 48S translation initiation complex. Three biological repeats were performed, with the representative micrograph shown here (raw micrographs provided in the Source data). B Immunofluorescence microscopy reveals co-localization of EIF3M with both Rps5 and Rpn11in the cytoplasm and nucleus. Fluorescence intensity measurements indicate that EIF3M/Rpn11 levels are approximately 3–5 times higher in the cytoplasm compared to the nucleus.

Journal: Nature Communications

Article Title: In-situ cross-linking mass spectrometry reveals compartment-specific proteasomal interactions and structural heterogeneity

doi: 10.1038/s41467-025-65752-6

Figure Lengend Snippet: A Co-immunoprecipitation confirms that EIF3M interacts with Rpn11, a proteasomal subunit, and with Rps5, a component of the 48S translation initiation complex. Three biological repeats were performed, with the representative micrograph shown here (raw micrographs provided in the Source data). B Immunofluorescence microscopy reveals co-localization of EIF3M with both Rps5 and Rpn11in the cytoplasm and nucleus. Fluorescence intensity measurements indicate that EIF3M/Rpn11 levels are approximately 3–5 times higher in the cytoplasm compared to the nucleus.

Article Snippet: The following antibodies were used: EIF3M (Proteintech, 11423-1-AP), RPS5 (Santa Cruz, sc-390935), and a control IgG antibody (Proteintech, 30000-0-AP, 1:200 dilution).

Techniques: Immunoprecipitation, Immunofluorescence, Microscopy, Fluorescence