ubr5 (Proteintech)
Proteintech is a verified supplier 
94
Structured Review
Proteintech
ubr5
Ubr5, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ubr5/UBR5+Antibody/pmc12765265-67-8-9
Average 94 stars, based on 21 article reviews
Ubr5, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ubr5/UBR5+Antibody/pmc12765265-67-8-9
Average 94 stars, based on 21 article reviews
ubr5 - by Bioz Stars,
2026-09
94/100 stars
Images
1) Product Images from "UBR5 regulates the progression of colorectal cancer cells through Snail-induced epithelial–mesenchymal transition"
Article Title: UBR5 regulates the progression of colorectal cancer cells through Snail-induced epithelial–mesenchymal transition
Journal: Genes & Diseases
doi: 10.1016/j.gendis.2025.101679
Figure Legend Snippet: UBR5 interacted with Snail. (A) UBR5 was positively correlated with Snail in colon adenocarcinoma and rectal adenocarcinoma. Correlation analysis for TCGA and GTEx on the GEPIA website showed a correlation coefficient of R = 0.26, P = 4.4e-13. P < 0.01 denoted statistical significance. (B) The expression levels of UBR5 and Snail correlated with colorectal cancer (CRC) stages. The UBR5 and Snail mRNA levels based on pathological stages were analyzed using the GEPIA2 violin-plots in colorectal tumors. (C) Co-immunoprecipitation assay showed that UBR5 interacted with Snail. HEK293T cells were transfected with Myc-tagged UBR5 and Flag-tagged Snail and treated with MG132 as indicated. Cell lysates were immunoprecipitated with either anti-Myc or anti-Flag antibodies and immunoblotted with anti-Snail and anti-UBR5 antibodies. (D) Co-localization of UBR5 and Snail in the nucleus. Immunofluorescence assay probe co-localization of UBR5 (red) and Snail (green). Scale bar: 50 μm. (E) UBR5 interacted with Snail through the HECT domain. A schematic of various UBR5 truncations that are fused to His. Coomassie blue staining image of a PAGE gel, confirming the expression of pET28a and various UBR5 truncations. (F) Snail interacted with UBR5 through the zinc-figure domain. A schematic of various Snail truncations that are fused to His. Coomassie blue staining image of a PAGE gel, confirming the expression of pET28a and various Snail truncations. (G) Molecular docking of Snail zinc-figure domain (amino acids 151–264) and UBR5 HECT domain (amino acids 2453–2799) truncation protein. (H) The HECT domain of UBR5 interacted with Snail in the co-immunoprecipitation assay. HEK293T cells were transfected with wild-type and truncated Myc-tagged UBR5, as well as Flag-tagged Snail, and treated with MG132 as indicated. Cell lysates were immunoprecipitated with either anti-Myc or anti-Flag antibodies and immunoblotted with anti-Snail or anti-UBR5 antibodies.
Techniques Used: Expressing, Co-Immunoprecipitation Assay, Transfection, Immunoprecipitation, Immunofluorescence, Staining
Figure Legend Snippet: UBR5 promoted the degradation and polyubiquitination of Snail. (A) UBR5 promoted the proteasomal degradation of Snail. HEK293T cells were transfected with Snail-Flag, Snail 6SA-Flag, UBR5-Myc, GFP, or empty vector and treated with DMSO, chloroquine, MG132, or CT99021 as indicated. The expression of Snail and GFP was assessed by western blotting. (B) UBR5 degraded Snail protein in a concentration-dependent manner. HEK293T cells were transfected with Snail-Flag, GFP, or in combination with different concentrations of wild-type and truncated UBR5-Myc for 48 h. Cell lysates were immunoblotted with anti-Snail antibodies. (C) UBR5 promoted K48 polyubiquitinated chain generation of Snail protein. In cellular ubiquitination assays, UBR5-Myc were co-transfected with Snail-Flag plasmids or with HA-Ub-K63 and HA-Ub-K48 plasmids. Western blotting was performed on cell lysates immunoprecipitated with an anti-Flag antibody, followed by the detection of polyubiquitination levels using an anti-Ub antibody. (D) UBR5 accelerated the Snail protein turnover through the HECT domain. HEK293T cells were transfected with corresponding plasmids. Cells were treated with cycloheximide (CHX) and harvested at indicated time points for immunoblotting with anti-Snail or anti-GFP antibody. The graph shows the quantification of Snail protein levels (based on the band intensity from the gels) normalized to those of GFP over the time course. Snail protein expression at the 0 h time point of treatment with CHX was set as 100 %. Experiments were performed in triplicate, and a representative experiment is presented.
Techniques Used: Transfection, Plasmid Preparation, Expressing, Western Blot, Concentration Assay, Ubiquitin Proteomics, Immunoprecipitation
Figure Legend Snippet: UBR5 affected the expression of epithelial–mesenchymal transition (EMT)-related factors. (A) Endogenous UBR5 knockdown changed the expression of Snail and EMT marker genes in colorectal cancer cells. Cells were collected and subjected to immunoblotting analysis and quantitative reverse transcription PCR analysis for indicated epithelial and mesenchymal markers. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. (B) Immunofluorescence analysis of Snail and E-cadherin protein expression in control and shUBR5 of HCT116 cells (Snail, green; E-cadherin, red; DAPI, blue). Scale bar: 50 μm. (C) Depletion of UBR5 induced the EMT phenotype in colorectal cancer cells. Morphology of HCT116 cells after transfection with lentiviral shRNAs targeting either control or UBR5. Scale bar: 100 μm. (D) Reduction of UBR5 enhanced cell migration in vitro . Wound-healing experiments were performed to analyze changes in the migratory capacity of HCT116 control and shUBR5 cells. The histogram shows the quantitation of the relative degree of healing ( n = 3). Scale bars: 100 μm. (E) Depletion of UBR5 facilitated cell invasiveness in vitro . Transwell assay was used to analyze changes in the invasive capacity of HCT116 control and shUBR5 cells. Scale bar: 100 μm. The number of cells crossing the basement membrane was counted. The histogram shows the quantitation of the relative numbers of cells that invaded and migrated through the matrix layer ( n = 3). Scale bars: 100 μm. (F) Knockdown of UBR5 increased tumor volumes and weights. The photographs show the excised tumors from HCT116 control (left) and HCT116 shUBR5 (right) models ( n = 3). The tumor sizes (tumor volumes and weights) were subjected to comparison. ∗ P < 0.05 and ∗∗∗ P < 0.001. (G) The knockdown of UBR5 promoted tumor cell infiltration. The effect on the xenograft model in HCT116 control and shUBR5 cells was assessed by hematoxylin-eosin staining. Scale bars: 50 μm.
Techniques Used: Expressing, Knockdown, Marker, Western Blot, Reverse Transcription, Immunofluorescence, Control, Transfection, Migration, In Vitro, Quantitation Assay, Transwell Assay, Membrane, Comparison, Staining
Figure Legend Snippet: UBR5 C2768S mutation abrogated the interaction with Snail. (A) His pull-down assays showed the abolished interactions between Snail and the UBR5 C2768S. A schematic representation of the UBR5 wild-type and C2768S mutation. (B) Co-immunoprecipitation assay showed that the interaction between the Snail and the UBR5 C2768S mutation was eliminated. HEK293T cells were transfected with UBR5-Myc, UBR5 C2768S-Myc, and Snail-Flag as indicated. Cell lysates were immunoprecipitated with either anti-Myc or anti-Flag antibodies and immunoblotted with anti-Snail and anti-UBR5 antibodies. (C) UBR5 C2768S abolished the UBR5-mediated degradation of Snail. HEK293T cells were transfected with Snail-Flag, UBR5-Myc, and UBR5 C2768S-Myc as indicated. Cell lysates were subjected to western blotting analysis with anti-Snail and anti-GFP antibodies. (D) UBR5 C2768S did not accelerate Snail protein turnover. HEK293T cells were transfected with Snail-Flag, UBR5-Myc, and UBR5 C2768S-Myc and treated with cycloheximide (CHX) as indicated. Cell lysates were subjected to western blotting analysis with anti-Snail and anti-GFP antibodi.
Techniques Used: Mutagenesis, Co-Immunoprecipitation Assay, Transfection, Immunoprecipitation, Western Blot
Figure Legend Snippet: C2768S mutation abolished the effects of UBR5 on the migration and invasion of HCT116 cells. (A) C2768S mutation changed the expression of epithelial–mesenchymal transition marker genes. HCT116 cells were transfected with UBR5-Myc and UBR5 C2768S-Myc constructs. Cells were collected and subjected to immunoblotting analysis and quantitative reverse transcription PCR analysis for indicated epithelial and mesenchymal markers. ∗∗ P < 0.01 and ∗∗∗ P < 0.001. (B) Immunofluorescence analysis of Snail and E-cadherin protein expression in Mock, UBR5-Myc, and UBR5 C2768S-Myc in HCT116 cells (Snail, green; E-cadherin, red; DAPI, blue). Scale bar: 50 μm. (C) Wound-healing assays showed the migration of HCT116 cells transfected with Mock, UBR5-Myc, or UBR5 C2768S-Myc. Representative images of healing degrees at 0 and 48 h after performing the wound are shown. The histogram shows the quantitation of the relative healing degrees ( n = 3). Scale bars: 100 μm. (D) Transwell assays showed the invasiveness of HCT116 cells transfected with Mock, UBR5-Myc, or UBR5 C2768S-Myc. Representative images of the staining of the cells that invaded and migrated through the matrix layer are shown. The histogram shows the quantitation of the relative numbers of cells that invaded and migrated through the matrix layer ( n = 3). Scale bars: 100 μm. (E) Wild-type UBR5 tumors were smaller in volume and weight than the HCT116 Mock and C2768S mutant groups. The photographs show the excised tumors from HCT116 Mock, UBR5, and UBR5 C2768S models ( n = 4). The tumor sizes (tumor volumes and weights) were subjected to comparison. (F) The UBR5 C2768S mutation disrupted the UBR5-Snail axis, eliminating its regulatory effect on tumor cell invasion. Hematoxylin-eosin staining of xenograft tumors derived from HCT116 Mock, UBR5-Myc, and UBR5 C2768S-Myc cells. Scale bar: 50 μm.
Techniques Used: Mutagenesis, Migration, Expressing, Marker, Transfection, Construct, Western Blot, Reverse Transcription, Immunofluorescence, Quantitation Assay, Staining, Comparison, Derivative Assay
Figure Legend Snippet: UBR5 was a favorable prognostic factor in human colorectal cancer. (A) Snail was highly expressed in samples obtained from patients with colorectal cancer. Immunohistochemical analysis of Snail expression levels in normal colorectum and tumors in the Human Protein Atlas website. Representative images are shown. ∗∗∗ P < 0.001; student's t -test. (B) GEPIA revealed that UBR5 had higher expression in normal tissue samples compared with tumor samples. Dark and light gray indicate tumor and normal tissues, respectively. (C) High expression of UBR5 was associated with a favorable prognosis. Kaplan–Meier analysis of 20-year overall survival of rectum adenocarcinoma cancer patients with UBR5 ( n = 165). Log-rank P -values are shown. (D) Diagram of the pattern of UBR5 regulation of epithelial–mesenchymal transition (EMT) in colorectal cancer. UBR5 inhibited the invasive migration of tumor cells by regulating the ubiquitination and transcriptional activity of Snail, and UBR5 C2768S eliminated the inhibitory effect of UBR5 on EMT.
Techniques Used: Immunohistochemical staining, Expressing, Migration, Ubiquitin Proteomics, Activity Assay
Related Articles
Concentration Assay:Article Title: Response of UBR-box E3 ubiquitin ligases and protein quality control pathways to perturbations in protein synthesis and skeletal muscle size. Article Snippet: .. The following antibodies were used at 249 1:1000 concentration unless otherwise stated: Total Ubiquitin (Millipore, 250 RRID:AB_2043482 and Cell Signaling, RRID:AB_2799235), UBR1 (ProteinTech, Cat no. 251 260069), UBR2 (Abcam, Cat no. 217069), UBR4 (Abcam, Cat no. 86738), Article Title: Response of UBR-box E3 ubiquitin ligases and protein quality control pathways to perturbations in protein synthesis and skeletal muscle size Article Snippet: .. The following antibodies were used at 1:1000 concentration unless otherwise stated: Total Ubiquitin FK2 (RRID:AB_2931782), UBR1 (ProteinTech, Cat no. 260069), UBR2 (Abcam, Cat no. 217069), UBR4 (Abcam, Cat no. 86738), Article Title: Response of UBR-box E3 ubiquitin ligases and protein quality control pathways to perturbations in protein synthesis and skeletal muscle size Article Snippet: .. The following antibodies were used at 1:1000 concentration unless otherwise stated: Total Ubiquitin (Millipore, RRID:AB_2043482 and Cell Signaling, RRID:AB_2799235), UBR1 (ProteinTech, Cat no. 260069), UBR2 (Abcam, Cat no. 217069), UBR4 (Abcam, Cat no. 86738), Ubiquitin Proteomics:Article Title: Response of UBR-box E3 ubiquitin ligases and protein quality control pathways to perturbations in protein synthesis and skeletal muscle size. Article Snippet: .. The following antibodies were used at 249 1:1000 concentration unless otherwise stated: Total Ubiquitin (Millipore, 250 RRID:AB_2043482 and Cell Signaling, RRID:AB_2799235), UBR1 (ProteinTech, Cat no. 251 260069), UBR2 (Abcam, Cat no. 217069), UBR4 (Abcam, Cat no. 86738), Article Title: Response of UBR-box E3 ubiquitin ligases and protein quality control pathways to perturbations in protein synthesis and skeletal muscle size Article Snippet: .. The following antibodies were used at 1:1000 concentration unless otherwise stated: Total Ubiquitin FK2 (RRID:AB_2931782), UBR1 (ProteinTech, Cat no. 260069), UBR2 (Abcam, Cat no. 217069), UBR4 (Abcam, Cat no. 86738), Article Title: Response of UBR-box E3 ubiquitin ligases and protein quality control pathways to perturbations in protein synthesis and skeletal muscle size Article Snippet: .. The following antibodies were used at 1:1000 concentration unless otherwise stated: Total Ubiquitin (Millipore, RRID:AB_2043482 and Cell Signaling, RRID:AB_2799235), UBR1 (ProteinTech, Cat no. 260069), UBR2 (Abcam, Cat no. 217069), UBR4 (Abcam, Cat no. 86738), Article Title: Phosphorylated SHMT2 Regulates Oncogenesis Through m 6 A Modification in Lung Adenocarcinoma. Article Snippet: .. For the antibodies, SHMT2 (11099-1-AP), β-actin (66009-1- Ig), SHMT1 (30192-1-AP), Myc-tag (60003-2-Ig), HUWE1 (19430-1-AP), STUB1 (55430-1-AP), Inhibition:Article Title: Proteomics-Based Trapping to Study Substrates of Histone Deacetylase 6 Catalytic Domain 1. Article Snippet: Histone deacetylase 6 (HDAC6) is linked with various cellular functions, such as gene expression and protein degradation, as well as many diseases, including breast cancers and Alzheimer’s disease.. HDAC6 removes the acetyl group of acetyllysine from histones to regulate gene expression in the nucleus.. However, with predominant localization in the cytoplasm, various cytoplasmic substrates of HDAC6 have also been identified. Transfection:Article Title: Proteomics-Based Trapping to Study Substrates of Histone Deacetylase 6 Catalytic Domain 1. Article Snippet: Histone deacetylase 6 (HDAC6) is linked with various cellular functions, such as gene expression and protein degradation, as well as many diseases, including breast cancers and Alzheimer’s disease.. HDAC6 removes the acetyl group of acetyllysine from histones to regulate gene expression in the nucleus.. However, with predominant localization in the cytoplasm, various cytoplasmic substrates of HDAC6 have also been identified. Incubation:Article Title: Proteomics-Based Trapping to Study Substrates of Histone Deacetylase 6 Catalytic Domain 1. Article Snippet: Histone deacetylase 6 (HDAC6) is linked with various cellular functions, such as gene expression and protein degradation, as well as many diseases, including breast cancers and Alzheimer’s disease.. HDAC6 removes the acetyl group of acetyllysine from histones to regulate gene expression in the nucleus.. However, with predominant localization in the cytoplasm, various cytoplasmic substrates of HDAC6 have also been identified. Lysis:Article Title: Proteomics-Based Trapping to Study Substrates of Histone Deacetylase 6 Catalytic Domain 1. Article Snippet: Histone deacetylase 6 (HDAC6) is linked with various cellular functions, such as gene expression and protein degradation, as well as many diseases, including breast cancers and Alzheimer’s disease.. HDAC6 removes the acetyl group of acetyllysine from histones to regulate gene expression in the nucleus.. However, with predominant localization in the cytoplasm, various cytoplasmic substrates of HDAC6 have also been identified. Membrane:Article Title: Proteomics-Based Trapping to Study Substrates of Histone Deacetylase 6 Catalytic Domain 1. Article Snippet: Histone deacetylase 6 (HDAC6) is linked with various cellular functions, such as gene expression and protein degradation, as well as many diseases, including breast cancers and Alzheimer’s disease.. HDAC6 removes the acetyl group of acetyllysine from histones to regulate gene expression in the nucleus.. However, with predominant localization in the cytoplasm, various cytoplasmic substrates of HDAC6 have also been identified. |