hif 1 α (MedChemExpress)

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MedChemExpress hif 1 α

ATG5 enhances <t>HSP90‐HIF‐1</t> α interaction to <t>promote</t> <t>HIF‐1</t> <t>α</t> stabilization. A) HK‐2 cells were transfected with ATG5 siRNA or control siRNA and then incubated with or without 800 µM UA for 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of ATG5 and HIF‐1 α . B) HK‐2 cells, after being transfected with ATG5 siRNA or control siRNA, were administered with CHX (10 µg mL −1 ) and harvested at the indicated times, followed by immunoblotting and quantitative analysis. C) 800 µM UA‐treated HK‐2 cells, after being transfected with ATG5 siRNA or control siRNA, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. D) HK‐2 cells were transfected with HSP90 siRNA or control siRNA and then incubated with or without UA (800 µM) for an additional 36 h. Western blot analyses showing the expression of HSP90 and HIF‐1 α . E) HK‐2 cells were transfected with HSP90 siRNA or control siRNA and then incubated with or without 800 µM UA for 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of HIF‐1 α . F) HK‐2 cells, after being transfected with HSP90 siRNA or control siRNA, were administered with CHX (10 µg mL −1 ) and harvested at the indicated times, followed by immunoblotting and quantitative analysis. G) 800 µM UA‐treated HK‐2 cells, after being transfected with HSP90 siRNA or control siRNA, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. H,I) 800 µM UA‐treated HK‐2 cell lysates were subjected to immunoprecipitation with IgG or HSP90, HIF‐1 α antibodies followed by HSP90 and HIF‐1 α immunoblotting. J) HK‐2 cells were transfected with HSP90 siRNA or control siRNA for 36 h, and then transfected with ATG5 pcDNA3.0 for an additional 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of ATG5, HSP90, and HIF‐1 α . K) HK‐2 cells, after being transfected with HSP90 siRNA and ATG5 pcDNA3.0, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. L) HK‐2 cells were transfected with ATG5 siRNA or control siRNA for 36 h, and then transfected with HSP90 pcDNA3.0 for an additional 36 h. Western blot analyses showing the expression of ATG5, HSP90, and HIF‐1 α . M) HK‐2 cells, after being transfected with ATG5 siRNA and HSP90 pcDNA3.0, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. n = 3 per group. Data are expressed as mean ± SEM. * p <0.05, ** p <0.01, *** p <0.001, **** p <0.0001, and N.S. denote statistically not significant.

Hif 1 α, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hy-p1888/HIF-1+alpha/pmc12061336-247-42-65
Average 94 stars, based on 5 article reviews

hif 1 α - by Bioz Stars, 2026-10

94/100 stars

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1) Product Images from "Autophagy Related 5 Promotes Mitochondrial Fission and Inflammation via HSP90‐HIF‐1 α ‐Mediated Glycolysis in Kidney Fibrosis"

Article Title: Autophagy Related 5 Promotes Mitochondrial Fission and Inflammation via HSP90‐HIF‐1 α ‐Mediated Glycolysis in Kidney Fibrosis

Journal: Advanced Science

doi: 10.1002/advs.202414673

ATG5 enhances HSP90‐HIF‐1 α interaction to promote HIF‐1 α stabilization. A) HK‐2 cells were transfected with ATG5 siRNA or control siRNA and then incubated with or without 800 µM UA for 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of ATG5 and HIF‐1 α . B) HK‐2 cells, after being transfected with ATG5 siRNA or control siRNA, were administered with CHX (10 µg mL −1 ) and harvested at the indicated times, followed by immunoblotting and quantitative analysis. C) 800 µM UA‐treated HK‐2 cells, after being transfected with ATG5 siRNA or control siRNA, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. D) HK‐2 cells were transfected with HSP90 siRNA or control siRNA and then incubated with or without UA (800 µM) for an additional 36 h. Western blot analyses showing the expression of HSP90 and HIF‐1 α . E) HK‐2 cells were transfected with HSP90 siRNA or control siRNA and then incubated with or without 800 µM UA for 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of HIF‐1 α . F) HK‐2 cells, after being transfected with HSP90 siRNA or control siRNA, were administered with CHX (10 µg mL −1 ) and harvested at the indicated times, followed by immunoblotting and quantitative analysis. G) 800 µM UA‐treated HK‐2 cells, after being transfected with HSP90 siRNA or control siRNA, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. H,I) 800 µM UA‐treated HK‐2 cell lysates were subjected to immunoprecipitation with IgG or HSP90, HIF‐1 α antibodies followed by HSP90 and HIF‐1 α immunoblotting. J) HK‐2 cells were transfected with HSP90 siRNA or control siRNA for 36 h, and then transfected with ATG5 pcDNA3.0 for an additional 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of ATG5, HSP90, and HIF‐1 α . K) HK‐2 cells, after being transfected with HSP90 siRNA and ATG5 pcDNA3.0, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. L) HK‐2 cells were transfected with ATG5 siRNA or control siRNA for 36 h, and then transfected with HSP90 pcDNA3.0 for an additional 36 h. Western blot analyses showing the expression of ATG5, HSP90, and HIF‐1 α . M) HK‐2 cells, after being transfected with ATG5 siRNA and HSP90 pcDNA3.0, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. n = 3 per group. Data are expressed as mean ± SEM. * p <0.05, ** p <0.01, *** p <0.001, **** p <0.0001, and N.S. denote statistically not significant.

Figure Legend Snippet: ATG5 enhances HSP90‐HIF‐1 α interaction to promote HIF‐1 α stabilization. A) HK‐2 cells were transfected with ATG5 siRNA or control siRNA and then incubated with or without 800 µM UA for 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of ATG5 and HIF‐1 α . B) HK‐2 cells, after being transfected with ATG5 siRNA or control siRNA, were administered with CHX (10 µg mL −1 ) and harvested at the indicated times, followed by immunoblotting and quantitative analysis. C) 800 µM UA‐treated HK‐2 cells, after being transfected with ATG5 siRNA or control siRNA, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. D) HK‐2 cells were transfected with HSP90 siRNA or control siRNA and then incubated with or without UA (800 µM) for an additional 36 h. Western blot analyses showing the expression of HSP90 and HIF‐1 α . E) HK‐2 cells were transfected with HSP90 siRNA or control siRNA and then incubated with or without 800 µM UA for 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of HIF‐1 α . F) HK‐2 cells, after being transfected with HSP90 siRNA or control siRNA, were administered with CHX (10 µg mL −1 ) and harvested at the indicated times, followed by immunoblotting and quantitative analysis. G) 800 µM UA‐treated HK‐2 cells, after being transfected with HSP90 siRNA or control siRNA, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. H,I) 800 µM UA‐treated HK‐2 cell lysates were subjected to immunoprecipitation with IgG or HSP90, HIF‐1 α antibodies followed by HSP90 and HIF‐1 α immunoblotting. J) HK‐2 cells were transfected with HSP90 siRNA or control siRNA for 36 h, and then transfected with ATG5 pcDNA3.0 for an additional 36 h, followed by treatment with 5 µM MG132 for 4 h before being harvested. Western blot analyses showing the expression of ATG5, HSP90, and HIF‐1 α . K) HK‐2 cells, after being transfected with HSP90 siRNA and ATG5 pcDNA3.0, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. L) HK‐2 cells were transfected with ATG5 siRNA or control siRNA for 36 h, and then transfected with HSP90 pcDNA3.0 for an additional 36 h. Western blot analyses showing the expression of ATG5, HSP90, and HIF‐1 α . M) HK‐2 cells, after being transfected with ATG5 siRNA and HSP90 pcDNA3.0, were subjected to immunoprecipitation with HIF‐1 α antibody, followed by ubiquitin immunoblotting. n = 3 per group. Data are expressed as mean ± SEM. * p <0.05, ** p <0.01, *** p <0.001, **** p <0.0001, and N.S. denote statistically not significant.

Techniques Used: Transfection, Control, Incubation, Western Blot, Expressing, Immunoprecipitation, Ubiquitin Proteomics

Tubule‐specific ATG5 ablation ameliorates mitochondrial fission in AAN mice. A) The level of serum lactate from different groups of mice. B) Western blot for hexokinase 2 and PFKFB3 in kidneys from different groups of mice. C) Quantitative analyses of hexokinase 2 and PFKFB3 standardized to β ‐actin in kidneys from different groups of mice. D) Western blot for MFN1, MFN2, OPA1, DRP1 and FIS1 in kidneys from different groups of mice. E‐I) Quantitative analyses of MFN1, MFN2, OPA1, DRP1 and FIS1 standardized to β ‐actin in kidneys from different groups of mice. J) Representative transmission electron microscopy images showing the ultrastructural feature of mitochondria in kidneys from AAN‐WT and AAN‐cKO groups. Scale bar = 500 nm. K) Ratio of damaged mitochondria according to the transmission electron microscopy images. L) Quantitative analysis of the number of mitochondria per field. M) Quantitative analysis showing mitochondrial length in each group. N) Schematic depicting persistent activation of ATG5 promotes mitochondrial fission and inflammation via HSP90‐HIF‐1 α ‐mediated glycolysis in kidney fibrosis. In pathological condition, the persistent activation of ATG5 promotes HSP90‐HIF‐1 α interaction, resulting in stabilization of HIF‐1 α and subsequent activation of glycolysis. Consequently, this process contributes to mitochondrial fission and inflammation, ultimately culminating in kidney fibrosis. n = 6–7 per group. Data are expressed as mean ± SEM. * p <0.05, *** p <0.001, **** p <0.0001, and N.S. denote statistically not significant.

Figure Legend Snippet: Tubule‐specific ATG5 ablation ameliorates mitochondrial fission in AAN mice. A) The level of serum lactate from different groups of mice. B) Western blot for hexokinase 2 and PFKFB3 in kidneys from different groups of mice. C) Quantitative analyses of hexokinase 2 and PFKFB3 standardized to β ‐actin in kidneys from different groups of mice. D) Western blot for MFN1, MFN2, OPA1, DRP1 and FIS1 in kidneys from different groups of mice. E‐I) Quantitative analyses of MFN1, MFN2, OPA1, DRP1 and FIS1 standardized to β ‐actin in kidneys from different groups of mice. J) Representative transmission electron microscopy images showing the ultrastructural feature of mitochondria in kidneys from AAN‐WT and AAN‐cKO groups. Scale bar = 500 nm. K) Ratio of damaged mitochondria according to the transmission electron microscopy images. L) Quantitative analysis of the number of mitochondria per field. M) Quantitative analysis showing mitochondrial length in each group. N) Schematic depicting persistent activation of ATG5 promotes mitochondrial fission and inflammation via HSP90‐HIF‐1 α ‐mediated glycolysis in kidney fibrosis. In pathological condition, the persistent activation of ATG5 promotes HSP90‐HIF‐1 α interaction, resulting in stabilization of HIF‐1 α and subsequent activation of glycolysis. Consequently, this process contributes to mitochondrial fission and inflammation, ultimately culminating in kidney fibrosis. n = 6–7 per group. Data are expressed as mean ± SEM. * p <0.05, *** p <0.001, **** p <0.0001, and N.S. denote statistically not significant.

Techniques Used: Western Blot, Transmission Assay, Electron Microscopy, Activation Assay

In Vivo:

Article Title: Suppression of HIF-1α alleviates the symptoms associated with diabetic retinopathy in mice.
Article Snippet: .. In vivo PX-478 treatment and Hematoxylin and Eosin (H&E) staining To inhibit HIF-1α, PX-478 (a HIF-1α inhibitor, HY-10231, MCE, New Jersey, USA) was administered, dissolved in saline, and mice received daily intraperitoneal injections of PX-478 at a dosage of 5 mg/kg body weight. ..

H&E Stain:

Saline:

Article Title: Hypobaric hypoxia drives citrate cycle reprogramming to suppress tumor progression
Article Snippet: .. For HIF-1α related treatment, the mice were treated with saline control, 100 mg/Kg DMOG (MCE, Cat# HY-15893), or 60 mg/Kg PX-478 (MCE, Cat# HY-10231) three times a week by intraperitoneal injection. ..

Activation Assay:

Article Title: Hypoxia-inducible factor 1 protects neurons from Sarm1-mediated neurodegeneration.
Article Snippet: .. Alternative Sarm1 activation methods B/B homodimerizer (AP20187) (Medchemexpress HY-13992) was dissolved at 1 mM in anhydrous DMSO and stored at − 20 ◦ C. Vacor (Pyrinuron) (Chem Service N-13738-100MG) was dissolved at 10 mM in 0.04 M HCl and stored at − 80 ◦ C. HIF-1 alpha subunit immunofluorescence staining Mouse cortical neurons from Cas9 +/+ embryos were plated at 200,000 cells/cm 2 in 96-well black plates (μ-Plate 96 Well Black, ibidi #89626)(see above for culture method), and transduced on DIV 1 with indicated guides or constructs. ..

Immunofluorescence:

Staining:

Construct:

Immunohistochemistry:

Article Title: Hypoxia-inducible Factors Contribute to Venous Thrombosis in a Mouse Model of Myeloproliferative Neoplasms.
Article Snippet: .. We found increased HIF-1α 68 protein in the spleen of VF mice by immunohistochemistry as previously described (Figure 69 1F).11 Increased mRNA expression of LDHA and HK2 (BioRad Prime PCR Probe Assays), two 70 genes that are regulated by HIF-1α and HIF-2α was also observed (Figure 1G).12,13 We then 71 tested whether the inhibition of HIF-1α or HIF-2α activity impacted thrombus size in the model. 72 Dose-finding experiments with echinomycin (MedChem Express), a HIF-1α inhibitor, were 73 performed to determine optimal dosing. ..

Expressing:

Polymerase Chain Reaction:

Inhibition:

Activity Assay:

Control:

Article Title: HIF1A overexpression promotes osteoblast differentiation through activation of autophagy to alleviate osteoporosis.
Article Snippet: .. The primer sequences were as follows: HIF-1a -F: C T A T G T C G C T T T C T T G G A, HIF-1a -R: G T T T T C T G C T G C C T T G T A T; GAPDH -F: C A A G T T C A A C G G C A C A G, GAPDH -R: C C A G T A G A C T C C A C G A C A T. Cell grouping and processing Cells were divided into the following four groups: Control (osteoblasts induced into osteogenic differentiation), ov-NC (transfection of negative control lentivirus in osteoblasts followed by induction of osteogenic differentiation), ov-HIF-1a (transfection of HIF-1a overexpressing lentivirus in osteoblasts followed by induction of osteogenic differentiation) and ov-HIF-1a + 3-MA [after transfection of HIF-1a overexpressing lentivirus in osteoblasts, 3-MA(1 mM, HY-19312, MCE) was added and treated for 1 h, then osteogenic differentiation was induced]. ..

Article Title: GPX3 suppresses gallbladder cancer progression by modulating redox balance, glycolysis, and anti-tumor immunity.
Article Snippet: .. Briefly, sh-GPX3 cells and their corresponding control cells in the logarithmic growth phase were treated with 20 μM of the HIF-1α-specific inhibitor PX-478 (MCE, HY-10231) or an equivalent volume of DMSO for 24 hours. ..

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