β1c Search Results


rabbit anti-β1c (psmb6  (Thermo Fisher)
90
Thermo Fisher rabbit anti-β1c (psmb6
Rabbit Anti β1c (Psmb6, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
rabbit anti-β1c (psmb6 - by Bioz Stars, 2026-03
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antibody β1c e1k9o  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc antibody β1c e1k9o
Antibody β1c E1k9o, supplied by Cell Signaling Technology Inc, 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/antibody β1c e1k9o/product/Cell Signaling Technology Inc
Average 90 stars, based on 1 article reviews
antibody β1c e1k9o - by Bioz Stars, 2026-03
90/100 stars
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z-lle-2r110 (β1c)  (AAT Bioquest)
90
AAT Bioquest z-lle-2r110 (β1c)
Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, <t>β1c</t> and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).
Z Lle 2r110 (β1c), supplied by AAT Bioquest, 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/z-lle-2r110 (β1c)/product/AAT Bioquest
Average 90 stars, based on 1 article reviews
z-lle-2r110 (β1c) - by Bioz Stars, 2026-03
90/100 stars
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rabbit anti β1c  (Thermo Fisher)
86
Thermo Fisher rabbit anti β1c
Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, <t>β1c</t> and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).
Rabbit Anti β1c, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti β1c/product/Thermo Fisher
Average 86 stars, based on 1 article reviews
rabbit anti β1c - by Bioz Stars, 2026-03
86/100 stars
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β1c  (Cell Signaling Technology Inc)
94
Cell Signaling Technology Inc β1c
Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, <t>β1c</t> and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).
β1c, supplied by Cell Signaling Technology Inc, 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/β1c/product/Cell Signaling Technology Inc
Average 94 stars, based on 1 article reviews
β1c - by Bioz Stars, 2026-03
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substrates β2c/β2i, ac-kqlr110  (AAT Bioquest)
90
AAT Bioquest substrates β2c/β2i, ac-kqlr110
Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, <t>β1c</t> and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).
Substrates β2c/β2i, Ac Kqlr110, supplied by AAT Bioquest, 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/substrates β2c/β2i, ac-kqlr110/product/AAT Bioquest
Average 90 stars, based on 1 article reviews
substrates β2c/β2i, ac-kqlr110 - by Bioz Stars, 2026-03
90/100 stars
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primary antibodies  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology primary antibodies
Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, <t>β1c</t> and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).
Primary Antibodies, supplied by Santa Cruz Biotechnology, 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/primary antibodies/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
primary antibodies - by Bioz Stars, 2026-03
93/100 stars
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subunit-specific primary antibodies β5c  (Covance)
90
Covance subunit-specific primary antibodies β5c
Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, <t>β1c</t> and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).
Subunit Specific Primary Antibodies β5c, supplied by Covance, 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/subunit-specific primary antibodies β5c/product/Covance
Average 90 stars, based on 1 article reviews
subunit-specific primary antibodies β5c - by Bioz Stars, 2026-03
90/100 stars
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Image Search Results


Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, β1c and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).

Journal: Scientific Reports

Article Title: Cytotoxic unsaturated electrophilic compounds commonly target the ubiquitin proteasome system

doi: 10.1038/s41598-019-46168-x

Figure Lengend Snippet: Inhibition of proteasome deubiquitinases. ( a ) Examination of 20S proteasome inhibition by hit compounds. Cell lysates (25 μg) were exposed to 20 μM of each compound except for bortezomib (BZ; 50 nM) for 5 min in assay buffer followed by the addition of substrates. The substrates Suc-LLVY, Z-LLE and Ac-KQL were used to assay β5c, β1c and β2c proteasome activity; the substrates Ac-PAL and Ac-ANW were used to assay β1i and β5i immunoproteasome activity. ( b )19S proteasome preparations (10 nM) were incubated with ubiquitin rhodamine in the presence of the indicated compounds at 37 °C and fluorescence recorded; ( c ) 19S proteasome preparations (10 nM) were exposed to different compounds at 50 μM followed by labeling with HA-ubiquitin-vinylsulphone (HA-UbVS). The blots were probed with antibodies to HA, USP14 and UCHL5. Note the preferential loss of USP14 HA-UbVS labeling. The loss of recognition of USP14 following exposure to CB826 was observed in repeated experiments and remains unexplained (this phenomenon was not observed using extracts (see below)). The previously described DUB inhibitor b-AP15 was included as a reference. ( d ) Total cellular lysates from OPM-2 cells were incubated with ubiquitin rhodamine in the presence of 20 μM of the indicated compounds at 37 °C and fluorescence recorded. ( e ) OPM-2 cell extracts were incubated with compounds (20 μM) followed by HA-UbVS labeling. Filters were incubated with the indicated antibodies (also see Supplementary Fig. where compounds were used at 50 μM).

Article Snippet: We used the substrates Suc-LLVY-2R110 (β5c), Z-LLE-2R110 (β1c) and (Ac-KQL)2R110 (β2c) from AAT Bioquest (Sunnyvale, CA).

Techniques: Inhibition, Activity Assay, Incubation, Ubiquitin Proteomics, Fluorescence, Labeling