socs1 (OriGene)

OriGene is a verified supplier

OriGene manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

OriGene socs1

NOS1-derived NO mediates S-nitrosation of <t>SOCS1</t> and prevents SOCS1-mediated proteasomal degradation of p65 . (A) Immunoblot analysis of p65 and SOCS1 in WT, NOS1 −/− , NOS2 −/− , and NOS3 −/− BMDM treated with LPS (250 ng/ml) for the indicated times. (B) SOCS1 S-nitrosation was detected using the biotin switch method on protein from WT and NOS1 −/− BMDMs pretreated with MG132 (50 µM) for 1 h before treatment with LPS (250 ng/ml) for the indicated times, followed by immunoblotting for SOCS1. (C) NOS2 −/− and NOS3 −/− BMDMs analyzed by biotin switch method, as in B. (D) Co-immunoprecipitation of SOCS1 and p65 in WT and NOS1 −/− BMDMs, pretreated with MG132 (50 µM, 1 h) before LPS (250 ng/ml) for the indicated time intervals. (E) Immunoblot analysis of p65 and SOCS1 total protein levels in NOS1 −/− BMDM treated with DEANO (NO donor, 5 µM) and LPS (250 ng/ml). All blots shown are representative of at least two (C and D) or three (A, B, and E) independent experiments.

Socs1, supplied by OriGene, 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/product/ssim+function/Socs1+(NM_009896)+Mouse+Tagged+ORF+Clone/pmc04577833-194-10-7
Average 90 stars, based on 1 article reviews

socs1 - by Bioz Stars, 2026-09

90/100 stars

Images

1) Product Images from "NOS1-derived nitric oxide promotes NF-κB transcriptional activity through inhibition of suppressor of cytokine signaling-1"

Article Title: NOS1-derived nitric oxide promotes NF-κB transcriptional activity through inhibition of suppressor of cytokine signaling-1

Journal: The Journal of Experimental Medicine

doi: 10.1084/jem.20140654

NOS1-derived NO mediates S-nitrosation of SOCS1 and prevents SOCS1-mediated proteasomal degradation of p65 . (A) Immunoblot analysis of p65 and SOCS1 in WT, NOS1 −/− , NOS2 −/− , and NOS3 −/− BMDM treated with LPS (250 ng/ml) for the indicated times. (B) SOCS1 S-nitrosation was detected using the biotin switch method on protein from WT and NOS1 −/− BMDMs pretreated with MG132 (50 µM) for 1 h before treatment with LPS (250 ng/ml) for the indicated times, followed by immunoblotting for SOCS1. (C) NOS2 −/− and NOS3 −/− BMDMs analyzed by biotin switch method, as in B. (D) Co-immunoprecipitation of SOCS1 and p65 in WT and NOS1 −/− BMDMs, pretreated with MG132 (50 µM, 1 h) before LPS (250 ng/ml) for the indicated time intervals. (E) Immunoblot analysis of p65 and SOCS1 total protein levels in NOS1 −/− BMDM treated with DEANO (NO donor, 5 µM) and LPS (250 ng/ml). All blots shown are representative of at least two (C and D) or three (A, B, and E) independent experiments.

Figure Legend Snippet: NOS1-derived NO mediates S-nitrosation of SOCS1 and prevents SOCS1-mediated proteasomal degradation of p65 . (A) Immunoblot analysis of p65 and SOCS1 in WT, NOS1 −/− , NOS2 −/− , and NOS3 −/− BMDM treated with LPS (250 ng/ml) for the indicated times. (B) SOCS1 S-nitrosation was detected using the biotin switch method on protein from WT and NOS1 −/− BMDMs pretreated with MG132 (50 µM) for 1 h before treatment with LPS (250 ng/ml) for the indicated times, followed by immunoblotting for SOCS1. (C) NOS2 −/− and NOS3 −/− BMDMs analyzed by biotin switch method, as in B. (D) Co-immunoprecipitation of SOCS1 and p65 in WT and NOS1 −/− BMDMs, pretreated with MG132 (50 µM, 1 h) before LPS (250 ng/ml) for the indicated time intervals. (E) Immunoblot analysis of p65 and SOCS1 total protein levels in NOS1 −/− BMDM treated with DEANO (NO donor, 5 µM) and LPS (250 ng/ml). All blots shown are representative of at least two (C and D) or three (A, B, and E) independent experiments.

Techniques Used: Derivative Assay, Western Blot, Immunoprecipitation

Molecular modeling and functional testing demonstrate that Cys147 and Cys179 of SOCS1 are the targets for S-nitrosation. (A) Protein domain structure of SOCS1 illustrating the positions of all 5 candidate cysteine residues. (B) Molecular modeling was performed to predict the accessibility of cysteine residues of SOCS1 (represented as colored stick atomic models) to the likely transnitrosation donor, GSNO (represented as ball and stick atomic models). The shorter distances between the cysteine sulfur atom and the nitrogen of GSNO are predicted to permit S-nitrosation for Cys147 (4 Å, middle) and Cys179 (6 Å, right), whereas Cys43 (13 Å, left), Cys112 (11 Å, not depicted), and Cys78 (11 Å, not depicted) are predicted to be too far apart to permit the reaction. (C) Representative immunoblots of GFP-tagged constructs of SOCS1 or point mutations of each cysteine (C147S, C179S, C112S, C78S, and C43S) were transfected into HEK293 cells, which were then treated with a 15-min pulse of 20 ng/ml IL-1β. Some of the cells were pretreated with 50 µM proteasome inhibitor for 1 h (MG132 +) and some were treated with 10 µM DEANO for 1 h after IL-1β (NO donor +). Stability of SOCS1 protein levels was determined by immunoblot and (D) quantified relative to β-actin from three independent experiments (mean ± SEM). (E) The capacity of SOCS1 mutants C147S, and C179S for S-nitrosation was compared with WT SOCS1 in transiently transfected HEK293 cells using the biotin switch method. Immunoprecipitates of GFP-SOCS1 variants were assayed for biotin (S-nitrosation), and lysates were immunoblotted for total SOCS1 as control. Data are representative of two independent experiments.

Figure Legend Snippet: Molecular modeling and functional testing demonstrate that Cys147 and Cys179 of SOCS1 are the targets for S-nitrosation. (A) Protein domain structure of SOCS1 illustrating the positions of all 5 candidate cysteine residues. (B) Molecular modeling was performed to predict the accessibility of cysteine residues of SOCS1 (represented as colored stick atomic models) to the likely transnitrosation donor, GSNO (represented as ball and stick atomic models). The shorter distances between the cysteine sulfur atom and the nitrogen of GSNO are predicted to permit S-nitrosation for Cys147 (4 Å, middle) and Cys179 (6 Å, right), whereas Cys43 (13 Å, left), Cys112 (11 Å, not depicted), and Cys78 (11 Å, not depicted) are predicted to be too far apart to permit the reaction. (C) Representative immunoblots of GFP-tagged constructs of SOCS1 or point mutations of each cysteine (C147S, C179S, C112S, C78S, and C43S) were transfected into HEK293 cells, which were then treated with a 15-min pulse of 20 ng/ml IL-1β. Some of the cells were pretreated with 50 µM proteasome inhibitor for 1 h (MG132 +) and some were treated with 10 µM DEANO for 1 h after IL-1β (NO donor +). Stability of SOCS1 protein levels was determined by immunoblot and (D) quantified relative to β-actin from three independent experiments (mean ± SEM). (E) The capacity of SOCS1 mutants C147S, and C179S for S-nitrosation was compared with WT SOCS1 in transiently transfected HEK293 cells using the biotin switch method. Immunoprecipitates of GFP-SOCS1 variants were assayed for biotin (S-nitrosation), and lysates were immunoblotted for total SOCS1 as control. Data are representative of two independent experiments.

Techniques Used: Functional Assay, Western Blot, Construct, Transfection

Review

socs1 (OriGene)

Structured Review

Images

1) Product Images from "NOS1-derived nitric oxide promotes NF-κB transcriptional activity through inhibition of suppressor of cytokine signaling-1"

Similar Products

Image Search Results