usp2 protein Search Results


94
R&D Systems e 322 human usp2 catalytic domain r d systems
E 322 Human Usp2 Catalytic Domain R D Systems, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e 322 human usp2 catalytic domain r d systems - by Bioz Stars, 2026-05
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91
Boston Biochem human usp2 catalytic domain protein
Cell lysates were prepared from MCF7 cells maintained at 37°C or heat‐shocked at 42°C for 1 h. Where indicated, lysate from heat‐shocked cells was incubated with recombinant <t>USP2</t> to remove polyubiquitin chains. Equal amounts of cell lysate were assayed for the levels of the indicated proteins by immunoblotting. A quantification of the levels of K48‐linked polyubiquitin is shown in the bar graph (means ± SD, n = 4, number indicates P value calculated with the two‐stage linear step‐up procedure of Benjamini, Krieger, and Yekutieli). Equal amounts of cell lysate described in (A) were fractionated by sucrose density gradient centrifugation, and K48‐linked polyubiquitin was detected by immunoblotting. Quantification of K48‐linked polyubiquitin across the gradients relative to the levels obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Trypsin‐like proteasome activity determined in the same fractions as in (B). Results are shown relative to the proteasome activity obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Source data are available online for this figure.
Human Usp2 Catalytic Domain Protein, supplied by Boston Biochem, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/human usp2 catalytic domain protein/product/Boston Biochem
Average 91 stars, based on 1 article reviews
human usp2 catalytic domain protein - by Bioz Stars, 2026-05
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94
R&D Systems recombinant usp2 catalytic domain
Cell lysates were prepared from MCF7 cells maintained at 37°C or heat‐shocked at 42°C for 1 h. Where indicated, lysate from heat‐shocked cells was incubated with recombinant <t>USP2</t> to remove polyubiquitin chains. Equal amounts of cell lysate were assayed for the levels of the indicated proteins by immunoblotting. A quantification of the levels of K48‐linked polyubiquitin is shown in the bar graph (means ± SD, n = 4, number indicates P value calculated with the two‐stage linear step‐up procedure of Benjamini, Krieger, and Yekutieli). Equal amounts of cell lysate described in (A) were fractionated by sucrose density gradient centrifugation, and K48‐linked polyubiquitin was detected by immunoblotting. Quantification of K48‐linked polyubiquitin across the gradients relative to the levels obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Trypsin‐like proteasome activity determined in the same fractions as in (B). Results are shown relative to the proteasome activity obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Source data are available online for this figure.
Recombinant Usp2 Catalytic Domain, supplied by R&D Systems, 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/recombinant usp2 catalytic domain/product/R&D Systems
Average 94 stars, based on 1 article reviews
recombinant usp2 catalytic domain - by Bioz Stars, 2026-05
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93
Boston Biochem deubiquitinase usp2
Cell lysates were prepared from MCF7 cells maintained at 37°C or heat‐shocked at 42°C for 1 h. Where indicated, lysate from heat‐shocked cells was incubated with recombinant <t>USP2</t> to remove polyubiquitin chains. Equal amounts of cell lysate were assayed for the levels of the indicated proteins by immunoblotting. A quantification of the levels of K48‐linked polyubiquitin is shown in the bar graph (means ± SD, n = 4, number indicates P value calculated with the two‐stage linear step‐up procedure of Benjamini, Krieger, and Yekutieli). Equal amounts of cell lysate described in (A) were fractionated by sucrose density gradient centrifugation, and K48‐linked polyubiquitin was detected by immunoblotting. Quantification of K48‐linked polyubiquitin across the gradients relative to the levels obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Trypsin‐like proteasome activity determined in the same fractions as in (B). Results are shown relative to the proteasome activity obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Source data are available online for this figure.
Deubiquitinase Usp2, supplied by Boston Biochem, 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/deubiquitinase usp2/product/Boston Biochem
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deubiquitinase usp2 - by Bioz Stars, 2026-05
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93
R&D Systems human recombinant
Cell lysates were prepared from MCF7 cells maintained at 37°C or heat‐shocked at 42°C for 1 h. Where indicated, lysate from heat‐shocked cells was incubated with recombinant <t>USP2</t> to remove polyubiquitin chains. Equal amounts of cell lysate were assayed for the levels of the indicated proteins by immunoblotting. A quantification of the levels of K48‐linked polyubiquitin is shown in the bar graph (means ± SD, n = 4, number indicates P value calculated with the two‐stage linear step‐up procedure of Benjamini, Krieger, and Yekutieli). Equal amounts of cell lysate described in (A) were fractionated by sucrose density gradient centrifugation, and K48‐linked polyubiquitin was detected by immunoblotting. Quantification of K48‐linked polyubiquitin across the gradients relative to the levels obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Trypsin‐like proteasome activity determined in the same fractions as in (B). Results are shown relative to the proteasome activity obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Source data are available online for this figure.
Human Recombinant, supplied by R&D Systems, 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/human recombinant/product/R&D Systems
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human recombinant - by Bioz Stars, 2026-05
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90
Human Protein Atlas bioinformatic analysis of usp2 expression
Cell lysates were prepared from MCF7 cells maintained at 37°C or heat‐shocked at 42°C for 1 h. Where indicated, lysate from heat‐shocked cells was incubated with recombinant <t>USP2</t> to remove polyubiquitin chains. Equal amounts of cell lysate were assayed for the levels of the indicated proteins by immunoblotting. A quantification of the levels of K48‐linked polyubiquitin is shown in the bar graph (means ± SD, n = 4, number indicates P value calculated with the two‐stage linear step‐up procedure of Benjamini, Krieger, and Yekutieli). Equal amounts of cell lysate described in (A) were fractionated by sucrose density gradient centrifugation, and K48‐linked polyubiquitin was detected by immunoblotting. Quantification of K48‐linked polyubiquitin across the gradients relative to the levels obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Trypsin‐like proteasome activity determined in the same fractions as in (B). Results are shown relative to the proteasome activity obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Source data are available online for this figure.
Bioinformatic Analysis Of Usp2 Expression, supplied by Human Protein Atlas, 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/bioinformatic analysis of usp2 expression/product/Human Protein Atlas
Average 90 stars, based on 1 article reviews
bioinformatic analysis of usp2 expression - by Bioz Stars, 2026-05
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N/A
Recombinant Mouse USP2 full length or partial length protein was expressed.http://www.creativebiomart.net/Recombinant-Mouse-USP2-Protein-448310.htm
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N/A
The Recombinant Human His6 USP2 Catalytic Domain Protein from R D Systems powered by Boston Biochem is derived from E coli The Recombinant Human His6 USP2 Catalytic Domain Protein has been validated for the following
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N/A
Human USP2 Protein Lysate 20ug from Innovative Research is provided as a Lyophilized powder. This is a Recombinant Protein Lysate produced in HEK293T cells. This protein lysate can be reconsituted using SDS Sample Buffer. Once
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N/A
Recombinant Human USP2(2–605 aa) fused with FLAG tag at N-terminal was expressed in Insect cells.Ubiquitin carboxyl-terminal hydrolase 2 is an enzyme that in humans is encoded by the USP2 gene.http://www.creativebiomart.net/Recombinant-Human-USP2-protein-FLAG-tagged-449005.htm
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N/A
Purified recombinant protein of Mouse ubiquitin specific peptidase 2 Usp2 with C terminal MYC DDK tag expressed in HEK293T cells 20ug
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Image Search Results


Cell lysates were prepared from MCF7 cells maintained at 37°C or heat‐shocked at 42°C for 1 h. Where indicated, lysate from heat‐shocked cells was incubated with recombinant USP2 to remove polyubiquitin chains. Equal amounts of cell lysate were assayed for the levels of the indicated proteins by immunoblotting. A quantification of the levels of K48‐linked polyubiquitin is shown in the bar graph (means ± SD, n = 4, number indicates P value calculated with the two‐stage linear step‐up procedure of Benjamini, Krieger, and Yekutieli). Equal amounts of cell lysate described in (A) were fractionated by sucrose density gradient centrifugation, and K48‐linked polyubiquitin was detected by immunoblotting. Quantification of K48‐linked polyubiquitin across the gradients relative to the levels obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Trypsin‐like proteasome activity determined in the same fractions as in (B). Results are shown relative to the proteasome activity obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Source data are available online for this figure.

Journal: The EMBO Journal

Article Title: Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins

doi: 10.15252/embj.2020106183

Figure Lengend Snippet: Cell lysates were prepared from MCF7 cells maintained at 37°C or heat‐shocked at 42°C for 1 h. Where indicated, lysate from heat‐shocked cells was incubated with recombinant USP2 to remove polyubiquitin chains. Equal amounts of cell lysate were assayed for the levels of the indicated proteins by immunoblotting. A quantification of the levels of K48‐linked polyubiquitin is shown in the bar graph (means ± SD, n = 4, number indicates P value calculated with the two‐stage linear step‐up procedure of Benjamini, Krieger, and Yekutieli). Equal amounts of cell lysate described in (A) were fractionated by sucrose density gradient centrifugation, and K48‐linked polyubiquitin was detected by immunoblotting. Quantification of K48‐linked polyubiquitin across the gradients relative to the levels obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Trypsin‐like proteasome activity determined in the same fractions as in (B). Results are shown relative to the proteasome activity obtained in MCF7 cells maintained at 37°C (means ± SEM, n = 3). Source data are available online for this figure.

Article Snippet: To digest K48‐polyubiquitin chains, the lysate was incubated with 7 μg of recombinant human USP2 catalytic domain protein (Boston Biochem, E‐506) for 1 h at 25°C.

Techniques: Incubation, Recombinant, Western Blot, Gradient Centrifugation, Activity Assay

Journal: The EMBO Journal

Article Title: Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins

doi: 10.15252/embj.2020106183

Figure Lengend Snippet:

Article Snippet: To digest K48‐polyubiquitin chains, the lysate was incubated with 7 μg of recombinant human USP2 catalytic domain protein (Boston Biochem, E‐506) for 1 h at 25°C.

Techniques: Recombinant, Sequencing, Magnetic Beads, Staining, Protease Inhibitor, DNA Purification, Bicinchoninic Acid Protein Assay, Modification, Software, Imaging