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rabbit antihuman smurf2  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology rabbit antihuman smurf2
    Figure 5 | Immunoblot analysis and effects of <t>Smurf2</t> immunodepletion on ubiquitination activity against SnoN and Ski. (a) Western blot analysis demonstrated that Smurf2 was weakly expressed in sham-operated kidneys. In UUO, the increases of Smurf2 were noted in almost inverse proportion to the levels of SnoN. (b) Renal extracts from obstructed or sham-operated kidneys (input) were pre-incubated with anti-Smurf2 antibody and protein G–Sepharose. After centrifugation, the remnant amounts of Smurf2 in the supernatants were checked by immunoblotting using anti-Smurf2 antibody (aSmurf2), and then subjected to the following assay. As a control, we used renal extracts that had been pre-incubated with rabbit immunoglobulin G (aIgG). (c, left panel) In obstructed kidneys, significant smeared bands were observed when HA-tagged SnoN was incubated with the control extracts that had not been immunodepleted of Smurf2 (; lanes 3 and 4); however, the bands were much weaker when HA-tagged SnoN was incubated with Smurf2-immunodepleted extracts ( þ ; lanes 5 and 6). In sham-operated kidneys, no significant bands were detected (lanes 1 and 2). (Right panel) We also performed a similar ubiquitination assay for Ski. No notable differences in the intensity of the bands were observed between the control (; lanes 9 and 10) and the Smurf2-immunodepleted extracts ( þ ; lanes 11 and 12) in obstructed kidneys.
    Rabbit Antihuman Smurf2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 87 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+antihuman+smurf2/AR+Gel+Shift+Oligonucleotides/pm16625151-91-34-38
    Average 93 stars, based on 87 article reviews
    rabbit antihuman smurf2 - by Bioz Stars, 2026-09
    93/100 stars

    Images

    1) Product Images from "Ubiquitin-dependent degradation of SnoN and Ski is increased in renal fibrosis induced by obstructive injury."

    Article Title: Ubiquitin-dependent degradation of SnoN and Ski is increased in renal fibrosis induced by obstructive injury.

    Journal: Kidney international

    doi: 10.1038/sj.ki.5000261

    Figure 5 | Immunoblot analysis and effects of Smurf2 immunodepletion on ubiquitination activity against SnoN and Ski. (a) Western blot analysis demonstrated that Smurf2 was weakly expressed in sham-operated kidneys. In UUO, the increases of Smurf2 were noted in almost inverse proportion to the levels of SnoN. (b) Renal extracts from obstructed or sham-operated kidneys (input) were pre-incubated with anti-Smurf2 antibody and protein G–Sepharose. After centrifugation, the remnant amounts of Smurf2 in the supernatants were checked by immunoblotting using anti-Smurf2 antibody (aSmurf2), and then subjected to the following assay. As a control, we used renal extracts that had been pre-incubated with rabbit immunoglobulin G (aIgG). (c, left panel) In obstructed kidneys, significant smeared bands were observed when HA-tagged SnoN was incubated with the control extracts that had not been immunodepleted of Smurf2 (; lanes 3 and 4); however, the bands were much weaker when HA-tagged SnoN was incubated with Smurf2-immunodepleted extracts ( þ ; lanes 5 and 6). In sham-operated kidneys, no significant bands were detected (lanes 1 and 2). (Right panel) We also performed a similar ubiquitination assay for Ski. No notable differences in the intensity of the bands were observed between the control (; lanes 9 and 10) and the Smurf2-immunodepleted extracts ( þ ; lanes 11 and 12) in obstructed kidneys.
    Figure Legend Snippet: Figure 5 | Immunoblot analysis and effects of Smurf2 immunodepletion on ubiquitination activity against SnoN and Ski. (a) Western blot analysis demonstrated that Smurf2 was weakly expressed in sham-operated kidneys. In UUO, the increases of Smurf2 were noted in almost inverse proportion to the levels of SnoN. (b) Renal extracts from obstructed or sham-operated kidneys (input) were pre-incubated with anti-Smurf2 antibody and protein G–Sepharose. After centrifugation, the remnant amounts of Smurf2 in the supernatants were checked by immunoblotting using anti-Smurf2 antibody (aSmurf2), and then subjected to the following assay. As a control, we used renal extracts that had been pre-incubated with rabbit immunoglobulin G (aIgG). (c, left panel) In obstructed kidneys, significant smeared bands were observed when HA-tagged SnoN was incubated with the control extracts that had not been immunodepleted of Smurf2 (; lanes 3 and 4); however, the bands were much weaker when HA-tagged SnoN was incubated with Smurf2-immunodepleted extracts ( þ ; lanes 5 and 6). In sham-operated kidneys, no significant bands were detected (lanes 1 and 2). (Right panel) We also performed a similar ubiquitination assay for Ski. No notable differences in the intensity of the bands were observed between the control (; lanes 9 and 10) and the Smurf2-immunodepleted extracts ( þ ; lanes 11 and 12) in obstructed kidneys.

    Techniques Used: Western Blot, Immunodepletion, Ubiquitin Proteomics, Activity Assay, Incubation, Centrifugation, Control

    Related Articles

    Nucleic Acid Electrophoresis:

    Article Title: Ubiquitin-dependent degradation of SnoN and Ski is increased in renal fibrosis induced by obstructive injury.
    Article Snippet: .. Equal amounts of proteins (40 mg) were loaded for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as described previously.29–31 The primary antibodies were goat anti-human SnoN (Santa Cruz Biotechnology), rabbit anti-human c-Ski (Santa Cruz Biotechnology), rabbit antihuman Smurf2 (sc-25511; Santa Cruz Biotechnology), and mouse monoclonal anti-b-actin (Sigma, St Louis, MO, USA). b-Actin was used as an internal control. ..

    Control:

    Article Title: Ubiquitin-dependent degradation of SnoN and Ski is increased in renal fibrosis induced by obstructive injury.
    Article Snippet: .. Equal amounts of proteins (40 mg) were loaded for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as described previously.29–31 The primary antibodies were goat anti-human SnoN (Santa Cruz Biotechnology), rabbit anti-human c-Ski (Santa Cruz Biotechnology), rabbit antihuman Smurf2 (sc-25511; Santa Cruz Biotechnology), and mouse monoclonal anti-b-actin (Sigma, St Louis, MO, USA). b-Actin was used as an internal control. ..



    Similar Products

    rabbit antihuman smurf2  (Santa Cruz Biotechnology)
    93
    Santa Cruz Biotechnology rabbit antihuman smurf2
    Figure 5 | Immunoblot analysis and effects of <t>Smurf2</t> immunodepletion on ubiquitination activity against SnoN and Ski. (a) Western blot analysis demonstrated that Smurf2 was weakly expressed in sham-operated kidneys. In UUO, the increases of Smurf2 were noted in almost inverse proportion to the levels of SnoN. (b) Renal extracts from obstructed or sham-operated kidneys (input) were pre-incubated with anti-Smurf2 antibody and protein G–Sepharose. After centrifugation, the remnant amounts of Smurf2 in the supernatants were checked by immunoblotting using anti-Smurf2 antibody (aSmurf2), and then subjected to the following assay. As a control, we used renal extracts that had been pre-incubated with rabbit immunoglobulin G (aIgG). (c, left panel) In obstructed kidneys, significant smeared bands were observed when HA-tagged SnoN was incubated with the control extracts that had not been immunodepleted of Smurf2 (; lanes 3 and 4); however, the bands were much weaker when HA-tagged SnoN was incubated with Smurf2-immunodepleted extracts ( þ ; lanes 5 and 6). In sham-operated kidneys, no significant bands were detected (lanes 1 and 2). (Right panel) We also performed a similar ubiquitination assay for Ski. No notable differences in the intensity of the bands were observed between the control (; lanes 9 and 10) and the Smurf2-immunodepleted extracts ( þ ; lanes 11 and 12) in obstructed kidneys.
    Rabbit Antihuman Smurf2, 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/product/rabbit+antihuman+smurf2/AR+Gel+Shift+Oligonucleotides/pm16625151-91-34-38
    Average 93 stars, based on 1 article reviews
    rabbit antihuman smurf2 - by Bioz Stars, 2026-09
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Figure 5 | Immunoblot analysis and effects of Smurf2 immunodepletion on ubiquitination activity against SnoN and Ski. (a) Western blot analysis demonstrated that Smurf2 was weakly expressed in sham-operated kidneys. In UUO, the increases of Smurf2 were noted in almost inverse proportion to the levels of SnoN. (b) Renal extracts from obstructed or sham-operated kidneys (input) were pre-incubated with anti-Smurf2 antibody and protein G–Sepharose. After centrifugation, the remnant amounts of Smurf2 in the supernatants were checked by immunoblotting using anti-Smurf2 antibody (aSmurf2), and then subjected to the following assay. As a control, we used renal extracts that had been pre-incubated with rabbit immunoglobulin G (aIgG). (c, left panel) In obstructed kidneys, significant smeared bands were observed when HA-tagged SnoN was incubated with the control extracts that had not been immunodepleted of Smurf2 (; lanes 3 and 4); however, the bands were much weaker when HA-tagged SnoN was incubated with Smurf2-immunodepleted extracts ( þ ; lanes 5 and 6). In sham-operated kidneys, no significant bands were detected (lanes 1 and 2). (Right panel) We also performed a similar ubiquitination assay for Ski. No notable differences in the intensity of the bands were observed between the control (; lanes 9 and 10) and the Smurf2-immunodepleted extracts ( þ ; lanes 11 and 12) in obstructed kidneys.

    Journal: Kidney international

    Article Title: Ubiquitin-dependent degradation of SnoN and Ski is increased in renal fibrosis induced by obstructive injury.

    doi: 10.1038/sj.ki.5000261

    Figure Lengend Snippet: Figure 5 | Immunoblot analysis and effects of Smurf2 immunodepletion on ubiquitination activity against SnoN and Ski. (a) Western blot analysis demonstrated that Smurf2 was weakly expressed in sham-operated kidneys. In UUO, the increases of Smurf2 were noted in almost inverse proportion to the levels of SnoN. (b) Renal extracts from obstructed or sham-operated kidneys (input) were pre-incubated with anti-Smurf2 antibody and protein G–Sepharose. After centrifugation, the remnant amounts of Smurf2 in the supernatants were checked by immunoblotting using anti-Smurf2 antibody (aSmurf2), and then subjected to the following assay. As a control, we used renal extracts that had been pre-incubated with rabbit immunoglobulin G (aIgG). (c, left panel) In obstructed kidneys, significant smeared bands were observed when HA-tagged SnoN was incubated with the control extracts that had not been immunodepleted of Smurf2 (; lanes 3 and 4); however, the bands were much weaker when HA-tagged SnoN was incubated with Smurf2-immunodepleted extracts ( þ ; lanes 5 and 6). In sham-operated kidneys, no significant bands were detected (lanes 1 and 2). (Right panel) We also performed a similar ubiquitination assay for Ski. No notable differences in the intensity of the bands were observed between the control (; lanes 9 and 10) and the Smurf2-immunodepleted extracts ( þ ; lanes 11 and 12) in obstructed kidneys.

    Article Snippet: Equal amounts of proteins (40 mg) were loaded for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as described previously.29–31 The primary antibodies were goat anti-human SnoN (Santa Cruz Biotechnology), rabbit anti-human c-Ski (Santa Cruz Biotechnology), rabbit antihuman Smurf2 (sc-25511; Santa Cruz Biotechnology), and mouse monoclonal anti-b-actin (Sigma, St Louis, MO, USA). b-Actin was used as an internal control.

    Techniques: Western Blot, Immunodepletion, Ubiquitin Proteomics, Activity Assay, Incubation, Centrifugation, Control