socs2 plasmid Search Results


90
Sino Biological fluorescent protein gfp
RPE lacking <t>the</t> <t>SOCS2</t> gene exhibited impaired autophagy. (A) In vivo , autophagic flux was detected by injecting 2 μl of 1 × 10 12 vg/ml adeno-associated virus 2 <t>(AAV2)-mRFP-GFP-LC3</t> in the eyeball of adult WT and SOCS2 –/– mice subretinally. About 2-weeks later, mice were starved for 24 h before euthanasia, and RPE/choroid flat mounts were isolated from mice ( n = 8, 10-week old, including males and females). (B) The numbers of autophagosomes and autolysosomes were evaluated by counting yellow and RFP dots. Puncta dots per horizon are shown as the mean ± SEM. (C) LC3B puncta dots (green) and p62 puncta dots (green) were stained by immunofluorescence in mouse primary RPE cells that were starved and treated with or without 30 μM CQ for 24 h. One group of SOCS2 –/– RPE re-expressed SOCS2 by transient transfection. (D,E) Fluorescence intensity of LC3B and p62 were quantified by the ImageJ software. (F) Immunoblotting for LC3B and p62 was performed in mouse primary RPE with different treatments. (G) The ratio of LC3B-II/LC3B-I was quantified by ImageJ software and normalized to β-actin. (H) p62 was quantified by ImageJ software and normalized to β-actin. Values for the control were set to 1. Statistical significance was determined by using the two-tailed unpaired t -test.
Fluorescent Protein Gfp, supplied by Sino Biological, 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/socs2+plasmid/Human+SOCS2+Gene+ORF+cDNA+clone+expression+plasmid%2C+C-GFPSpark+tag/pmc08606588-48-17-32
Average 90 stars, based on 1 article reviews
fluorescent protein gfp - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier

93
Santa Cruz Biotechnology socs2 plasmid
Kaplan-Meier curve assessment of risk of death in a cohort of 89 patients with invasive breast cancer. Overall survival is shown for patients with high and low <t>SOCS2</t> and IGF-I expression, respectively. The median was taken as a cut-off. P values were determined using the log-rank test.
Socs2 Plasmid, 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/socs2+plasmid/SOCS-2+HDR+Plasmid/pmc01948006-117-14-23
Average 93 stars, based on 1 article reviews
socs2 plasmid - by Bioz Stars, 2026-09
93/100 stars
  Buy from Supplier

N/A
Full length Clone DNA of Human suppressor of cytokine signaling 2 with N terminal His tag.
  Buy from Supplier

N/A
Full length Clone DNA of Mouse suppressor of cytokine signaling 2 with C terminal GFPSpark tag.
  Buy from Supplier

N/A
Full length Clone DNA of Human suppressor of cytokine signaling 2 with C terminal GFPSpark tag.
  Buy from Supplier

N/A
Full length Clone DNA of Mouse suppressor of cytokine signaling 2 with N terminal Flag tag.
  Buy from Supplier

N/A
CRISPR/Cas9 KO Plasmids consists of SOCS-2-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double strand break (DSB)
  Buy from Supplier

N/A
Full length Clone DNA of Homo sapiens suppressor of cytokine signaling 2.
  Buy from Supplier

N/A
Full length Clone DNA of Human suppressor of cytokine signaling 2 with C terminal OFPSpark / RFP tag.
  Buy from Supplier

N/A
Full length Clone DNA of Human suppressor of cytokine signaling 2 with N terminal GFPSpark tag.
  Buy from Supplier

N/A
Full length Clone DNA of Human suppressor of cytokine signaling 2 with N terminal Myc tag.
  Buy from Supplier

N/A
Socs2 Rat 4 unique 29mer shRNA constructs in retroviral untagged vector
  Buy from Supplier

Image Search Results


RPE lacking the SOCS2 gene exhibited impaired autophagy. (A) In vivo , autophagic flux was detected by injecting 2 μl of 1 × 10 12 vg/ml adeno-associated virus 2 (AAV2)-mRFP-GFP-LC3 in the eyeball of adult WT and SOCS2 –/– mice subretinally. About 2-weeks later, mice were starved for 24 h before euthanasia, and RPE/choroid flat mounts were isolated from mice ( n = 8, 10-week old, including males and females). (B) The numbers of autophagosomes and autolysosomes were evaluated by counting yellow and RFP dots. Puncta dots per horizon are shown as the mean ± SEM. (C) LC3B puncta dots (green) and p62 puncta dots (green) were stained by immunofluorescence in mouse primary RPE cells that were starved and treated with or without 30 μM CQ for 24 h. One group of SOCS2 –/– RPE re-expressed SOCS2 by transient transfection. (D,E) Fluorescence intensity of LC3B and p62 were quantified by the ImageJ software. (F) Immunoblotting for LC3B and p62 was performed in mouse primary RPE with different treatments. (G) The ratio of LC3B-II/LC3B-I was quantified by ImageJ software and normalized to β-actin. (H) p62 was quantified by ImageJ software and normalized to β-actin. Values for the control were set to 1. Statistical significance was determined by using the two-tailed unpaired t -test.

Journal: Frontiers in Neuroscience

Article Title: Suppressor of Cytokine Signaling 2 Regulates Retinal Pigment Epithelium Metabolism by Enhancing Autophagy

doi: 10.3389/fnins.2021.738022

Figure Lengend Snippet: RPE lacking the SOCS2 gene exhibited impaired autophagy. (A) In vivo , autophagic flux was detected by injecting 2 μl of 1 × 10 12 vg/ml adeno-associated virus 2 (AAV2)-mRFP-GFP-LC3 in the eyeball of adult WT and SOCS2 –/– mice subretinally. About 2-weeks later, mice were starved for 24 h before euthanasia, and RPE/choroid flat mounts were isolated from mice ( n = 8, 10-week old, including males and females). (B) The numbers of autophagosomes and autolysosomes were evaluated by counting yellow and RFP dots. Puncta dots per horizon are shown as the mean ± SEM. (C) LC3B puncta dots (green) and p62 puncta dots (green) were stained by immunofluorescence in mouse primary RPE cells that were starved and treated with or without 30 μM CQ for 24 h. One group of SOCS2 –/– RPE re-expressed SOCS2 by transient transfection. (D,E) Fluorescence intensity of LC3B and p62 were quantified by the ImageJ software. (F) Immunoblotting for LC3B and p62 was performed in mouse primary RPE with different treatments. (G) The ratio of LC3B-II/LC3B-I was quantified by ImageJ software and normalized to β-actin. (H) p62 was quantified by ImageJ software and normalized to β-actin. Values for the control were set to 1. Statistical significance was determined by using the two-tailed unpaired t -test.

Article Snippet: Plasmid cytomegalovirus 3 (pCMV3)-Human-SOCS2-orange fluorescent protein (OFP) expression plasmid (HG11285-ACR), control vector OFP expression plasmids (CV025), pCMV3-Human-SOCS2-green fluorescent protein (GFP) (HG11285-ACG), and control vectors GFP expression plasmids (CV026) were purchased from the Sino Biological Incorporation (Wayne, PA, United States).

Techniques: In Vivo, Isolation, Staining, Immunofluorescence, Transfection, Fluorescence, Software, Western Blot, Two Tailed Test

SOCS2 promoted autophagy in ARPE-19 cells. (A) The mRNA expression of SOCS2 was detected by real-time quantitative PCR in ARPE-19 after transient transfection with pCMV3-Human-SOCS2-OFP expression plasmids or control vectors. The two-tailed unpaired t -test was used. (B,C) Western blot images of SOCS2-OFP and SOCS2-GFP were detected by the SOCS2 antibody to check the overexpression of SOCS2. (D) LC3B puncta dots (green) and p62 puncta dots (green) were stained by immunofluorescence in ARPE-19 cells transfected with pCMV3-Human-SOCS2-OFP expression plasmids or control vectors for 24 h, then cells were starved and treated with or without 30 μM CQ for 24 h. (E,F) Fluorescence intensity of LC3B and p62 was quantified by ImageJ software. (G) Western blot detected the expression of LC3B and p62 in SOCS2 overexpressing ARPE-19 cells that were treated with or without 30 μM CQ for 24 h. (H) The ratio of LC3B-II/LC3B-I was quantified by ImageJ software and normalized to β-actin. Values for the control were set to 1. (I) p62 was quantified by ImageJ software and normalized to β-actin. Values for the control were set to 1. Statistical significance was determined by using the two-tailed unpaired t -test.

Journal: Frontiers in Neuroscience

Article Title: Suppressor of Cytokine Signaling 2 Regulates Retinal Pigment Epithelium Metabolism by Enhancing Autophagy

doi: 10.3389/fnins.2021.738022

Figure Lengend Snippet: SOCS2 promoted autophagy in ARPE-19 cells. (A) The mRNA expression of SOCS2 was detected by real-time quantitative PCR in ARPE-19 after transient transfection with pCMV3-Human-SOCS2-OFP expression plasmids or control vectors. The two-tailed unpaired t -test was used. (B,C) Western blot images of SOCS2-OFP and SOCS2-GFP were detected by the SOCS2 antibody to check the overexpression of SOCS2. (D) LC3B puncta dots (green) and p62 puncta dots (green) were stained by immunofluorescence in ARPE-19 cells transfected with pCMV3-Human-SOCS2-OFP expression plasmids or control vectors for 24 h, then cells were starved and treated with or without 30 μM CQ for 24 h. (E,F) Fluorescence intensity of LC3B and p62 was quantified by ImageJ software. (G) Western blot detected the expression of LC3B and p62 in SOCS2 overexpressing ARPE-19 cells that were treated with or without 30 μM CQ for 24 h. (H) The ratio of LC3B-II/LC3B-I was quantified by ImageJ software and normalized to β-actin. Values for the control were set to 1. (I) p62 was quantified by ImageJ software and normalized to β-actin. Values for the control were set to 1. Statistical significance was determined by using the two-tailed unpaired t -test.

Article Snippet: Plasmid cytomegalovirus 3 (pCMV3)-Human-SOCS2-orange fluorescent protein (OFP) expression plasmid (HG11285-ACR), control vector OFP expression plasmids (CV025), pCMV3-Human-SOCS2-green fluorescent protein (GFP) (HG11285-ACG), and control vectors GFP expression plasmids (CV026) were purchased from the Sino Biological Incorporation (Wayne, PA, United States).

Techniques: Expressing, Real-time Polymerase Chain Reaction, Transfection, Two Tailed Test, Western Blot, Over Expression, Staining, Immunofluorescence, Fluorescence, Software

Ubiquitylated proteins recognized by SOCS2 were transferred into autophagosomes and autolysosomes. (A) The endogenous detection of protein interaction between SOCS2 and ubiquitin was detected in starved ARPE-19 by Duolink in situ fluorescence. The red fluorescence indicated the interaction of SOCS2 and ubiquitin. (B) Immunofluorescence staining with ubiquitin (red) and DAPI (blue) was performed in starved ARPE-19 with transient transfection of GFP control vectors or SOCS2-GFP plasmids. The yellow dots indicated the colocalization of SOCS2 and ubiquitin in merged pictures. (C) Immunofluorescence staining with the antibody p62 (red) and DAPI (blue) in ARPE-19 with the same treatment of B. The yellow dots indicated the colocalization of SOCS2 and p62 in merged pictures. (D) The immunoprecipitation of p62 and SOCS2 was detected in ARPE-19 with the same treatment of B. (E) Immunofluorescence staining was performed with the antibodies against p62 (green) and ubiquitin (red) in starved ARPE-19. (F) Immunofluorescence staining with the antibody LC3B (red) in ARPE-19 with the same treatment of B. (G) The immunoprecipitation of LC3B and SOCS2 was detected in ARPE-19 with the same treatment of B. (H) The endogenous detection of protein interaction between SOCS2 and LAMP2 was detected in starved ARPE-19 by Duolink in situ fluorescence. The red fluorescence indicated the interaction of SOCS2 and LAMP2. (I) Immunofluorescence staining with the antibody LAMP2 in ARPE-19 after transient transfection of SOCS2-OFP plasmids or OFP control vectors. (J,K) The immunoprecipitation of p62 and phosphorylated mammalian target of rapamycin (p-mTOR), SOCS2, and p-mTOR were detected in ARPE-19 with the same treatment of B.

Journal: Frontiers in Neuroscience

Article Title: Suppressor of Cytokine Signaling 2 Regulates Retinal Pigment Epithelium Metabolism by Enhancing Autophagy

doi: 10.3389/fnins.2021.738022

Figure Lengend Snippet: Ubiquitylated proteins recognized by SOCS2 were transferred into autophagosomes and autolysosomes. (A) The endogenous detection of protein interaction between SOCS2 and ubiquitin was detected in starved ARPE-19 by Duolink in situ fluorescence. The red fluorescence indicated the interaction of SOCS2 and ubiquitin. (B) Immunofluorescence staining with ubiquitin (red) and DAPI (blue) was performed in starved ARPE-19 with transient transfection of GFP control vectors or SOCS2-GFP plasmids. The yellow dots indicated the colocalization of SOCS2 and ubiquitin in merged pictures. (C) Immunofluorescence staining with the antibody p62 (red) and DAPI (blue) in ARPE-19 with the same treatment of B. The yellow dots indicated the colocalization of SOCS2 and p62 in merged pictures. (D) The immunoprecipitation of p62 and SOCS2 was detected in ARPE-19 with the same treatment of B. (E) Immunofluorescence staining was performed with the antibodies against p62 (green) and ubiquitin (red) in starved ARPE-19. (F) Immunofluorescence staining with the antibody LC3B (red) in ARPE-19 with the same treatment of B. (G) The immunoprecipitation of LC3B and SOCS2 was detected in ARPE-19 with the same treatment of B. (H) The endogenous detection of protein interaction between SOCS2 and LAMP2 was detected in starved ARPE-19 by Duolink in situ fluorescence. The red fluorescence indicated the interaction of SOCS2 and LAMP2. (I) Immunofluorescence staining with the antibody LAMP2 in ARPE-19 after transient transfection of SOCS2-OFP plasmids or OFP control vectors. (J,K) The immunoprecipitation of p62 and phosphorylated mammalian target of rapamycin (p-mTOR), SOCS2, and p-mTOR were detected in ARPE-19 with the same treatment of B.

Article Snippet: Plasmid cytomegalovirus 3 (pCMV3)-Human-SOCS2-orange fluorescent protein (OFP) expression plasmid (HG11285-ACR), control vector OFP expression plasmids (CV025), pCMV3-Human-SOCS2-green fluorescent protein (GFP) (HG11285-ACG), and control vectors GFP expression plasmids (CV026) were purchased from the Sino Biological Incorporation (Wayne, PA, United States).

Techniques: In Situ, Fluorescence, Immunofluorescence, Staining, Transfection, Immunoprecipitation

Kaplan-Meier curve assessment of risk of death in a cohort of 89 patients with invasive breast cancer. Overall survival is shown for patients with high and low SOCS2 and IGF-I expression, respectively. The median was taken as a cut-off. P values were determined using the log-rank test.

Journal: BMC Cancer

Article Title: Favorable prognostic value of SOCS2 and IGF-I in breast cancer

doi: 10.1186/1471-2407-7-136

Figure Lengend Snippet: Kaplan-Meier curve assessment of risk of death in a cohort of 89 patients with invasive breast cancer. Overall survival is shown for patients with high and low SOCS2 and IGF-I expression, respectively. The median was taken as a cut-off. P values were determined using the log-rank test.

Article Snippet: To test for antibody specificity, lysates from COS7 cells transiently transfected with a myc-tagged SOCS2 plasmid were probed with an anti-c-myc antibody (9E10, Santa Cruz Biotechnology, Santa Cruz) and anti-SOCS2 antibodies.

Techniques: Expressing

Comparison of SOCS2 and IGF-I expression. (A) Box blots with data from a set of seven tumors comparing the relative mRNA expression levels in tumor (CA) and normal adjacent tissue (TA). (B) SOCS2 protein and corresponding SOCS2 mRNA expression in normal and cancerous tissue of two tumor specimens. SOCS2 protein expression was assessed by immuno-blot with an antibody directed against SOCS2. Actin was used as a loading control.

Journal: BMC Cancer

Article Title: Favorable prognostic value of SOCS2 and IGF-I in breast cancer

doi: 10.1186/1471-2407-7-136

Figure Lengend Snippet: Comparison of SOCS2 and IGF-I expression. (A) Box blots with data from a set of seven tumors comparing the relative mRNA expression levels in tumor (CA) and normal adjacent tissue (TA). (B) SOCS2 protein and corresponding SOCS2 mRNA expression in normal and cancerous tissue of two tumor specimens. SOCS2 protein expression was assessed by immuno-blot with an antibody directed against SOCS2. Actin was used as a loading control.

Article Snippet: To test for antibody specificity, lysates from COS7 cells transiently transfected with a myc-tagged SOCS2 plasmid were probed with an anti-c-myc antibody (9E10, Santa Cruz Biotechnology, Santa Cruz) and anti-SOCS2 antibodies.

Techniques: Expressing

Detection of SOCS2 in primary mammary carcinoma samples by immunohistochemistry. Representative immunohistochemical stainings of samples with low SOCS2 (A) and high SOCS2 (B) mRNA expression are shown. Note a strong cytoplasmatic epithelial staining for SOCS2 in tumors with high SOCS2 mRNA levels (B).

Journal: BMC Cancer

Article Title: Favorable prognostic value of SOCS2 and IGF-I in breast cancer

doi: 10.1186/1471-2407-7-136

Figure Lengend Snippet: Detection of SOCS2 in primary mammary carcinoma samples by immunohistochemistry. Representative immunohistochemical stainings of samples with low SOCS2 (A) and high SOCS2 (B) mRNA expression are shown. Note a strong cytoplasmatic epithelial staining for SOCS2 in tumors with high SOCS2 mRNA levels (B).

Article Snippet: To test for antibody specificity, lysates from COS7 cells transiently transfected with a myc-tagged SOCS2 plasmid were probed with an anti-c-myc antibody (9E10, Santa Cruz Biotechnology, Santa Cruz) and anti-SOCS2 antibodies.

Techniques: Immunohistochemistry, Immunohistochemical staining, Expressing, Staining