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human lc3b / map1lc3b protein  (Sino Biological)


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    Sino Biological human lc3b / map1lc3b protein
    Human Lc3b / Map1lc3b Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/h07e/Human+LC3B+%2F+MAP1LC3B+Protein/custom%4014555-h07e%4042607684
    Average 93 stars, based on 10 article reviews
    human lc3b / map1lc3b protein - by Bioz Stars, 2026-09
    93/100 stars

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    Related Articles

    Control:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate.
    Article Snippet: Breast cancer often manifests as solid hypoxic tumors which are associated with high levels of hypoxia-inducible factor (HIF)-α and a poor prognosis.1-4 The HIF protein consists of an oxygen-sensitive α subunit and a constitutively expressed β subunit that regulate the expression of target genes.5,6 HIF-1α and HIF-2α are the best-characterized α subunits of HIFs.. HIF-1α is ubiquitously expressed, while, HIF-2α is mainly detected in highly vascularized organs with hypoxic tissues, including kidney epithelial cells.7 Despite their extensive sequence similarity and co-expression in various cancer cell types, HIF-1α, and HIF-2α have overlapping and nonoverlapping roles in gene expression associated with Received: 11 July 2019 | Revised: 3 January 2020 | Accepted: 9 January 2020 DOI: 10.1096/fj.201901734RR

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    Binding Assay:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate.
    Article Snippet: Breast cancer often manifests as solid hypoxic tumors which are associated with high levels of hypoxia-inducible factor (HIF)-α and a poor prognosis.1-4 The HIF protein consists of an oxygen-sensitive α subunit and a constitutively expressed β subunit that regulate the expression of target genes.5,6 HIF-1α and HIF-2α are the best-characterized α subunits of HIFs.. HIF-1α is ubiquitously expressed, while, HIF-2α is mainly detected in highly vascularized organs with hypoxic tissues, including kidney epithelial cells.7 Despite their extensive sequence similarity and co-expression in various cancer cell types, HIF-1α, and HIF-2α have overlapping and nonoverlapping roles in gene expression associated with Received: 11 July 2019 | Revised: 3 January 2020 | Accepted: 9 January 2020 DOI: 10.1096/fj.201901734RR

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    Protease Inhibitor:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate.
    Article Snippet: Breast cancer often manifests as solid hypoxic tumors which are associated with high levels of hypoxia-inducible factor (HIF)-α and a poor prognosis.1-4 The HIF protein consists of an oxygen-sensitive α subunit and a constitutively expressed β subunit that regulate the expression of target genes.5,6 HIF-1α and HIF-2α are the best-characterized α subunits of HIFs.. HIF-1α is ubiquitously expressed, while, HIF-2α is mainly detected in highly vascularized organs with hypoxic tissues, including kidney epithelial cells.7 Despite their extensive sequence similarity and co-expression in various cancer cell types, HIF-1α, and HIF-2α have overlapping and nonoverlapping roles in gene expression associated with Received: 11 July 2019 | Revised: 3 January 2020 | Accepted: 9 January 2020 DOI: 10.1096/fj.201901734RR

    Recombinant:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate.
    Article Snippet: Breast cancer often manifests as solid hypoxic tumors which are associated with high levels of hypoxia-inducible factor (HIF)-α and a poor prognosis.1-4 The HIF protein consists of an oxygen-sensitive α subunit and a constitutively expressed β subunit that regulate the expression of target genes.5,6 HIF-1α and HIF-2α are the best-characterized α subunits of HIFs.. HIF-1α is ubiquitously expressed, while, HIF-2α is mainly detected in highly vascularized organs with hypoxic tissues, including kidney epithelial cells.7 Despite their extensive sequence similarity and co-expression in various cancer cell types, HIF-1α, and HIF-2α have overlapping and nonoverlapping roles in gene expression associated with Received: 11 July 2019 | Revised: 3 January 2020 | Accepted: 9 January 2020 DOI: 10.1096/fj.201901734RR

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    Article Title: Discovery and biological evaluation of a potent small molecule CRM1 inhibitor for its selective ablation of extranodal NK/T cell lymphoma
    Article Snippet: Protein , KEAP1 Protein, Human, Recombinant (His & GST Tag) , Sinobiological, Beijing, China , Cat# 11981-H20B , . .. Protein , IκB alpha Protein, Human, Recombinant (His Tag) , Sinobiological, Beijing, China , Cat# 12045-H07E , . .. Commercial assay or kit , Cell Counting Kit-8 , Beyotime, Shanghai, China , Cat# C0037 , .

    Mutagenesis:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate.
    Article Snippet: Breast cancer often manifests as solid hypoxic tumors which are associated with high levels of hypoxia-inducible factor (HIF)-α and a poor prognosis.1-4 The HIF protein consists of an oxygen-sensitive α subunit and a constitutively expressed β subunit that regulate the expression of target genes.5,6 HIF-1α and HIF-2α are the best-characterized α subunits of HIFs.. HIF-1α is ubiquitously expressed, while, HIF-2α is mainly detected in highly vascularized organs with hypoxic tissues, including kidney epithelial cells.7 Despite their extensive sequence similarity and co-expression in various cancer cell types, HIF-1α, and HIF-2α have overlapping and nonoverlapping roles in gene expression associated with Received: 11 July 2019 | Revised: 3 January 2020 | Accepted: 9 January 2020 DOI: 10.1096/fj.201901734RR

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    Incubation:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate.
    Article Snippet: Breast cancer often manifests as solid hypoxic tumors which are associated with high levels of hypoxia-inducible factor (HIF)-α and a poor prognosis.1-4 The HIF protein consists of an oxygen-sensitive α subunit and a constitutively expressed β subunit that regulate the expression of target genes.5,6 HIF-1α and HIF-2α are the best-characterized α subunits of HIFs.. HIF-1α is ubiquitously expressed, while, HIF-2α is mainly detected in highly vascularized organs with hypoxic tissues, including kidney epithelial cells.7 Despite their extensive sequence similarity and co-expression in various cancer cell types, HIF-1α, and HIF-2α have overlapping and nonoverlapping roles in gene expression associated with Received: 11 July 2019 | Revised: 3 January 2020 | Accepted: 9 January 2020 DOI: 10.1096/fj.201901734RR

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    Article Title: An extracellular vesicular mutant KRAS-associated protein complex promotes lung inflammation and tumor growth.
    Article Snippet: .. KRAS-Fn interaction To prove whether KRAS physically interacts with Fn1, KRAS protein 20 μg (Sino Biological; cat: 12259-H07E) was incubated with purified Fn1 (20 μg) (Sino Biological; cat: 10314-H08H) for 2 h and 30 min in 400 μl equilibrium buffer (20 mM Tris–HCl, pH 7.5, 250 mM NaCl). ..

    Article Title: An extracellular vesicular mutant KRAS‐associated protein complex promotes lung inflammation and tumor growth
    Article Snippet: .. To prove whether KRAS physically interacts with Fn1, KRAS protein 20 μg (Sino Biological; cat: 12259‐H07E) was incubated with purified Fn1 (20 μg) (Sino Biological; cat: 10314‐H08H) for 2 h and 30 min in 400 μl equilibrium buffer (20 mM Tris–HCl, pH 7.5, 250 mM NaCl). ..

    Centrifugation:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    SDS Page:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    Western Blot:

    Article Title: Regulation of hypoxia-inducible factor functions in the nucleus by sphingosine-1-phosphate
    Article Snippet: Control or S1P-coated agarose beads (Echelon Biosciences, Salt Lake City, UT, USA) equilibrated with binding buffer containing 10 mM HEPES (pH 7.8), 150 mM NaCl, 0.5% NP-40 and 1:500 protease inhibitor cocktail were mixed with nuclear extracts preincubated with or without 10 μM S1P for 25 min and rocked overnight at 4 °C ( 17 , 27 , 28 ). .. For some experiments, recombinant wildtype-HIF-1α (# ab154478, >75 % pure, Abcam) and His-tagged deletion mutant HIF-1α with the PAS domains deleted (# 11977-H07E, delta M1-L574, >95 % pure, Sino Biological US Inc., Wayne, PA, USA) proteins pretreated with or without 10 μM S1P for 25 min were mixed with control or S1P affinity beads and incubated for overnight at 4 ° C. Beads were washed 4 times with 10 volumes of binding buffer, and protein-bound S1P beads and control beads were collected by centrifugation at 1000 RPM at 4 ° C. After removing the supernatant, the beads were boiled in SDS-PAGE sample buffer and bound proteins analyzed by Western blotting ( 17 , 27 , 28 ), as explained in the Figure legend. ..

    other:

    Article Title: Non-orthosteric inhibition of enolase 1 impedes growth of triple-negative breast cancer
    Article Snippet: ENO3 protein , Sino Biological , Cat. No. # 14270-H07E.

    Article Title: SDCBP/Syntenin-1 stabilizes BACH1 by disassembling the SCF FBXO22 –BACH1 complex in triple-negative breast cancer
    Article Snippet: Biological Human Syntenin-1 protein , Sino Biological , Cat15640-H07E.

    Purification:

    Article Title: An extracellular vesicular mutant KRAS-associated protein complex promotes lung inflammation and tumor growth.
    Article Snippet: .. KRAS-Fn interaction To prove whether KRAS physically interacts with Fn1, KRAS protein 20 μg (Sino Biological; cat: 12259-H07E) was incubated with purified Fn1 (20 μg) (Sino Biological; cat: 10314-H08H) for 2 h and 30 min in 400 μl equilibrium buffer (20 mM Tris–HCl, pH 7.5, 250 mM NaCl). ..

    Article Title: An extracellular vesicular mutant KRAS‐associated protein complex promotes lung inflammation and tumor growth
    Article Snippet: .. To prove whether KRAS physically interacts with Fn1, KRAS protein 20 μg (Sino Biological; cat: 12259‐H07E) was incubated with purified Fn1 (20 μg) (Sino Biological; cat: 10314‐H08H) for 2 h and 30 min in 400 μl equilibrium buffer (20 mM Tris–HCl, pH 7.5, 250 mM NaCl). ..



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    94
    Sino Biological sox2 protein
    GAC binds <t>HSPA8</t> to induce ferroptosis in HCC. (A) Schematic diagram of the drug Affinity responsive Target stability (DARTS) assay workflow. (B) Representative coomassie blue-stained SDS-PAGE gel of DARTS samples. (C) Bubble plot summarizing MS results: x-axis shows δsequence coverage (GAC vs. control), bubble size represents protein score. (D) Protein-protein interaction (PPI) network of DARTS-identified targets; nodes are colored by DMNC algorithm score (red = high centrality, yellow = low). (E–F) Cellular thermal shift assay (CETSA) confirms GAC binding stabilizes HSPA8. Representative immunoblots (E) of HSPA8 levels in lysates from HCCLM3 cells treated with GAC or DMSO and subjected to a temperature gradient (37-65 °C) and quantification (F) of relative HSPA8 levels at each temperature, data were assessed by the repeated-measures ANOVA, n = 3 in each group. (G–H) Microscale thermophoresis (MST): representative MST traces (G); dose-response curve showing GAC binding to recombinant HSPA8 (H). (I–J) molecular docking pose(I) of GAC bound to HSPA8 and magnified view of the molecular docking pose (J) focusing on the interactions between GAC and key residues (Tyr15, Gly201, Arg272, Asp366). (K–M) molecular dynamics (MD) simulations of GAC bound to HSPA8: RMSD of HSPA8 backbone over 100 ns (K); RMSF per residue(L); per-residue energy decomposition identifying key interacting residues (M). (N) Schematic of HSPA8 point mutations generated at predicted GAC-binding residues. (O-P) CETSA validation of HSPA8 mutants: Western blots (O) and quantification (P) demonstrate loss of thermal stabilization by GAC in HSPA8 MUT , n = 3 in each group. (Q–R) Flow cytometry histogram of Bodipy665/676 intensity and quantification of the percentage of oxidized cells in shHSPA8 vs. scramble cells treated with GAC or not, n = 3 in each group. (S–T) Knock down HSPA8 restores redox homeostasis: Quantified MDA levels, data were assessed by the Mann-Whitney test. (S) and GSH/GSSG ratio (T), n = 3 in each group. (U-V) Flow cytometry plots (U) and quantification (V) of the percentage of Annexin V + cells in shHSPA8 vs. scramble cells treated with GAC or not, n = 3 in each group. (W-X) Knock down HSPA8 ameliorates clonogenic capacity: Representative colony formation images(W) and quantified colony counts (X), n = 3 in each group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.
    Sox2 Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/h07e/Human+SOX2+Protein/pm41824786-346-10-20
    Average 94 stars, based on 1 article reviews
    sox2 protein - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier
    human il 15  (Sino Biological)
    94
    Sino Biological human il 15
    Liposome coated scaffolds are suitable substrates for cells and enable cytokine presentation: (A) live HEK293 cell counts were measured from multiple time points on unpoled scaffolds with and without cationic liposome coating. Data is presented as mean ± SEM from 3 independent wells at each time point. Statistical significance was assessed by two-way ANOVA with Sidak's multiple comparisons test, comparing coated to uncoated scaffold at each time point. P values reflect differences between groups at individual time points, and all error bars are present on graph although some are too small to see. (B) Unpoled scaffolds were coated with fluorescent Cy5-labeled liposomes and imaged with confocal microscopy. Jurkat T cells were stained with calcein, cultured on Cy5 liposome-coated scaffolds, and imaged at 60× resolution 3 days after plating. (C) Jurkat T cells were fixed on day 4 and stained intracellularly with ActinProbe555 and DAPI. Arrows indicate punctate actin (yellow) or liposome uptake (magenta). Scale bars are 50 µm or 10 µm. (D) Activating the JAK-STAT Pathway <t>with</t> <t>IL-15</t> Liposomes on Scaffolds: (i) unpoled scaffolds were coated with 2 mg mL −1 of IL-15-tethered liposomes in optimized HEPES-NaCl buffer conditions and SEAP is produced in response to IL-15 recognition. (ii) IL-15 reporter cells were plated on unpoled scaffolds, and absorbance was read daily, correlating to the downstream SEAP production from activation of the JAK-STAT pathway with n = 3 samples per group. Data is presented as relative fold change from uncoated scaffold control, with mean ± SD. Significance is conducted with an Ordinary Two-Way Anova with multiple comparisons using Šídák's multiple comparisons test.
    Human Il 15, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/h07e/Human+IL-15+%2F+IL15+%2F+Interleukin+15+Protein/pmc12989790-248-6-8
    Average 94 stars, based on 1 article reviews
    human il 15 - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier

    Image Search Results


    GAC binds HSPA8 to induce ferroptosis in HCC. (A) Schematic diagram of the drug Affinity responsive Target stability (DARTS) assay workflow. (B) Representative coomassie blue-stained SDS-PAGE gel of DARTS samples. (C) Bubble plot summarizing MS results: x-axis shows δsequence coverage (GAC vs. control), bubble size represents protein score. (D) Protein-protein interaction (PPI) network of DARTS-identified targets; nodes are colored by DMNC algorithm score (red = high centrality, yellow = low). (E–F) Cellular thermal shift assay (CETSA) confirms GAC binding stabilizes HSPA8. Representative immunoblots (E) of HSPA8 levels in lysates from HCCLM3 cells treated with GAC or DMSO and subjected to a temperature gradient (37-65 °C) and quantification (F) of relative HSPA8 levels at each temperature, data were assessed by the repeated-measures ANOVA, n = 3 in each group. (G–H) Microscale thermophoresis (MST): representative MST traces (G); dose-response curve showing GAC binding to recombinant HSPA8 (H). (I–J) molecular docking pose(I) of GAC bound to HSPA8 and magnified view of the molecular docking pose (J) focusing on the interactions between GAC and key residues (Tyr15, Gly201, Arg272, Asp366). (K–M) molecular dynamics (MD) simulations of GAC bound to HSPA8: RMSD of HSPA8 backbone over 100 ns (K); RMSF per residue(L); per-residue energy decomposition identifying key interacting residues (M). (N) Schematic of HSPA8 point mutations generated at predicted GAC-binding residues. (O-P) CETSA validation of HSPA8 mutants: Western blots (O) and quantification (P) demonstrate loss of thermal stabilization by GAC in HSPA8 MUT , n = 3 in each group. (Q–R) Flow cytometry histogram of Bodipy665/676 intensity and quantification of the percentage of oxidized cells in shHSPA8 vs. scramble cells treated with GAC or not, n = 3 in each group. (S–T) Knock down HSPA8 restores redox homeostasis: Quantified MDA levels, data were assessed by the Mann-Whitney test. (S) and GSH/GSSG ratio (T), n = 3 in each group. (U-V) Flow cytometry plots (U) and quantification (V) of the percentage of Annexin V + cells in shHSPA8 vs. scramble cells treated with GAC or not, n = 3 in each group. (W-X) Knock down HSPA8 ameliorates clonogenic capacity: Representative colony formation images(W) and quantified colony counts (X), n = 3 in each group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Journal: Pharmaceutical Biology

    Article Title: Ginkgolic acid targets HSPA8 to trigger ferroptosis in hepatocellular carcinoma via chaperone-mediated autophagy-dependent GPX4 degradation

    doi: 10.1080/13880209.2026.2646350

    Figure Lengend Snippet: GAC binds HSPA8 to induce ferroptosis in HCC. (A) Schematic diagram of the drug Affinity responsive Target stability (DARTS) assay workflow. (B) Representative coomassie blue-stained SDS-PAGE gel of DARTS samples. (C) Bubble plot summarizing MS results: x-axis shows δsequence coverage (GAC vs. control), bubble size represents protein score. (D) Protein-protein interaction (PPI) network of DARTS-identified targets; nodes are colored by DMNC algorithm score (red = high centrality, yellow = low). (E–F) Cellular thermal shift assay (CETSA) confirms GAC binding stabilizes HSPA8. Representative immunoblots (E) of HSPA8 levels in lysates from HCCLM3 cells treated with GAC or DMSO and subjected to a temperature gradient (37-65 °C) and quantification (F) of relative HSPA8 levels at each temperature, data were assessed by the repeated-measures ANOVA, n = 3 in each group. (G–H) Microscale thermophoresis (MST): representative MST traces (G); dose-response curve showing GAC binding to recombinant HSPA8 (H). (I–J) molecular docking pose(I) of GAC bound to HSPA8 and magnified view of the molecular docking pose (J) focusing on the interactions between GAC and key residues (Tyr15, Gly201, Arg272, Asp366). (K–M) molecular dynamics (MD) simulations of GAC bound to HSPA8: RMSD of HSPA8 backbone over 100 ns (K); RMSF per residue(L); per-residue energy decomposition identifying key interacting residues (M). (N) Schematic of HSPA8 point mutations generated at predicted GAC-binding residues. (O-P) CETSA validation of HSPA8 mutants: Western blots (O) and quantification (P) demonstrate loss of thermal stabilization by GAC in HSPA8 MUT , n = 3 in each group. (Q–R) Flow cytometry histogram of Bodipy665/676 intensity and quantification of the percentage of oxidized cells in shHSPA8 vs. scramble cells treated with GAC or not, n = 3 in each group. (S–T) Knock down HSPA8 restores redox homeostasis: Quantified MDA levels, data were assessed by the Mann-Whitney test. (S) and GSH/GSSG ratio (T), n = 3 in each group. (U-V) Flow cytometry plots (U) and quantification (V) of the percentage of Annexin V + cells in shHSPA8 vs. scramble cells treated with GAC or not, n = 3 in each group. (W-X) Knock down HSPA8 ameliorates clonogenic capacity: Representative colony formation images(W) and quantified colony counts (X), n = 3 in each group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Article Snippet: Purified HSPA8 (11329-H07E, sinoBiological) served as a target and was labeled with fluorescence by Monolith Labeling Kit RED-tris-NTA (MO-L018, NanoTemper Technologies).

    Techniques: Staining, SDS Page, Control, Thermal Shift Assay, Binding Assay, Western Blot, Microscale Thermophoresis, Recombinant, Residue, Generated, Biomarker Discovery, Flow Cytometry, Knockdown, MANN-WHITNEY

    GAC promotes CMA-dependent GPX4 degradation to induce ferroptosis. (A–B) GAC induces HSPA8-dependent KFERQ puncta formation, indicating CMA activation. Representative images of confocal images (A) detecting the KFERQ-probe (bar = 25 μm) and quantification of KFERQ puncta per cell (B) using ImageJ, n = 3 in each group. (C) CCK-8 assay assessing cytotoxicity in cells pretreated with indicated concentrations of Bafilomycin A1 (BafA1) for 12 h before GAC treatment, n = 3 in each group. (D–E) Flow cytometry histogram of Bodipy-C11 intensity (D) and quantification (E) of the percentage of oxidized cells in HCCLM3 cells pretreated with BafA1 before GAC treatment, n = 3 in each group. (F–G) Flow cytometry plots (F) and quantification (G) of the percentage of Annexin V + cells in HCCLM3 cells pretreated with BafA1 before GAC treatment, n = 3 in each group. (H) Table generated by KFERQ-finder showing the gene names, KFERQ-like motifs, and their starting positions within GPX4 and SLC7A11. (I-K) HSPA8 knockdown specifically prevents GAC-induced GPX4 degradation. Representative immunoblots (I) and quantification of GPX4 (J) and SLC7A11(K), normalized to β-actin, n = 3 in each group. (L–N) LAMP2A knockdown abolishes GAC-induced GPX4 degradation. Representative immunoblots (L) and quantification of LAMP2A (M) and GPX4 (N), normalized to β-actin, n = 3 in each group. (O–P) Flow cytometry histogram of Bodipy-C11 intensity (O) and quantification (P) of the percentage of oxidized cells in shLAMP2A vs. scramble cells treated with GAC or not, n = 3 in each group. (Q-R) Flow cytometry plots (Q) and quantification (R) of the percentage of Annexin V + cells in shLAMP2A vs. scramble cells treated with GAC or not, n = 3 in each group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Journal: Pharmaceutical Biology

    Article Title: Ginkgolic acid targets HSPA8 to trigger ferroptosis in hepatocellular carcinoma via chaperone-mediated autophagy-dependent GPX4 degradation

    doi: 10.1080/13880209.2026.2646350

    Figure Lengend Snippet: GAC promotes CMA-dependent GPX4 degradation to induce ferroptosis. (A–B) GAC induces HSPA8-dependent KFERQ puncta formation, indicating CMA activation. Representative images of confocal images (A) detecting the KFERQ-probe (bar = 25 μm) and quantification of KFERQ puncta per cell (B) using ImageJ, n = 3 in each group. (C) CCK-8 assay assessing cytotoxicity in cells pretreated with indicated concentrations of Bafilomycin A1 (BafA1) for 12 h before GAC treatment, n = 3 in each group. (D–E) Flow cytometry histogram of Bodipy-C11 intensity (D) and quantification (E) of the percentage of oxidized cells in HCCLM3 cells pretreated with BafA1 before GAC treatment, n = 3 in each group. (F–G) Flow cytometry plots (F) and quantification (G) of the percentage of Annexin V + cells in HCCLM3 cells pretreated with BafA1 before GAC treatment, n = 3 in each group. (H) Table generated by KFERQ-finder showing the gene names, KFERQ-like motifs, and their starting positions within GPX4 and SLC7A11. (I-K) HSPA8 knockdown specifically prevents GAC-induced GPX4 degradation. Representative immunoblots (I) and quantification of GPX4 (J) and SLC7A11(K), normalized to β-actin, n = 3 in each group. (L–N) LAMP2A knockdown abolishes GAC-induced GPX4 degradation. Representative immunoblots (L) and quantification of LAMP2A (M) and GPX4 (N), normalized to β-actin, n = 3 in each group. (O–P) Flow cytometry histogram of Bodipy-C11 intensity (O) and quantification (P) of the percentage of oxidized cells in shLAMP2A vs. scramble cells treated with GAC or not, n = 3 in each group. (Q-R) Flow cytometry plots (Q) and quantification (R) of the percentage of Annexin V + cells in shLAMP2A vs. scramble cells treated with GAC or not, n = 3 in each group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Article Snippet: Purified HSPA8 (11329-H07E, sinoBiological) served as a target and was labeled with fluorescence by Monolith Labeling Kit RED-tris-NTA (MO-L018, NanoTemper Technologies).

    Techniques: Activation Assay, CCK-8 Assay, Flow Cytometry, Generated, Knockdown, Western Blot

    GAC binds HSPA8 to promote HSPA8-GPX4 interaction via KFERQ-like motif. (A) GAC enhances the endogenous HSPA8-GPX4 interaction. Co-immunoprecipitation (co-IP) of GPX4 followed by immunoblotting for HSPA8 in HCCLM3 (left panel) and HepG2 (right panel) cells, n = 3 in each group. (B-D) GAC increases HSPA8-GPX4 co-localization. Representative immunofluorescence confocal microscopy images (B) showing endogenous GPX4 (red) and HSPA8 (green). Nuclei were stained with DAPI (blue). Scale bar: 25 μm. Line-scan intensity profiles (C) across representative regions of interest (ROIs) from (B), demonstrating correlated fluorescence signals of HSPA8 and GPX4 at subcellular resolution. Quantification (D) of co-localization using Pearson’s correlation coefficient (analyzed with the JACoP plugin in ImageJ), n = 3 in each group. (E) Co-IP of GPX4 in cells expressing wild-type HSPA8 (HSPA8 WT ) or binding-deficient mutant HSPA8 (HSPA8 MUT ); GAC enhances HSPA8-GPX4 interaction only in the presence of HSPA8 WT .(F) schematic of GPX4 highlighting two critical KFERQ-like motifs (AAKFD and LIDAA) targeted for mutagenesis to generate GPX4 AAKFD and GPX4 LIDAA . (G, H) Immunoblotting (G) and quantification (H) showing that GAC induces degradation of wild-type GPX4 but not KFERQ-mutant GPX4 in HCCLM3 cells. (I) Co-IP assay demonstrating loss of interaction between HSPA8 and KFERQ-mutant GPX4 upon GAC treatment. (J, K) Overexpression of HSPA8 promotes degradation of Myc-GPX4 WT but not Myc-GPX4 AAKFD : representative immunoblots (J) and quantification (K) of GPX4, normalized to β-actin, n = 3 in each group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Journal: Pharmaceutical Biology

    Article Title: Ginkgolic acid targets HSPA8 to trigger ferroptosis in hepatocellular carcinoma via chaperone-mediated autophagy-dependent GPX4 degradation

    doi: 10.1080/13880209.2026.2646350

    Figure Lengend Snippet: GAC binds HSPA8 to promote HSPA8-GPX4 interaction via KFERQ-like motif. (A) GAC enhances the endogenous HSPA8-GPX4 interaction. Co-immunoprecipitation (co-IP) of GPX4 followed by immunoblotting for HSPA8 in HCCLM3 (left panel) and HepG2 (right panel) cells, n = 3 in each group. (B-D) GAC increases HSPA8-GPX4 co-localization. Representative immunofluorescence confocal microscopy images (B) showing endogenous GPX4 (red) and HSPA8 (green). Nuclei were stained with DAPI (blue). Scale bar: 25 μm. Line-scan intensity profiles (C) across representative regions of interest (ROIs) from (B), demonstrating correlated fluorescence signals of HSPA8 and GPX4 at subcellular resolution. Quantification (D) of co-localization using Pearson’s correlation coefficient (analyzed with the JACoP plugin in ImageJ), n = 3 in each group. (E) Co-IP of GPX4 in cells expressing wild-type HSPA8 (HSPA8 WT ) or binding-deficient mutant HSPA8 (HSPA8 MUT ); GAC enhances HSPA8-GPX4 interaction only in the presence of HSPA8 WT .(F) schematic of GPX4 highlighting two critical KFERQ-like motifs (AAKFD and LIDAA) targeted for mutagenesis to generate GPX4 AAKFD and GPX4 LIDAA . (G, H) Immunoblotting (G) and quantification (H) showing that GAC induces degradation of wild-type GPX4 but not KFERQ-mutant GPX4 in HCCLM3 cells. (I) Co-IP assay demonstrating loss of interaction between HSPA8 and KFERQ-mutant GPX4 upon GAC treatment. (J, K) Overexpression of HSPA8 promotes degradation of Myc-GPX4 WT but not Myc-GPX4 AAKFD : representative immunoblots (J) and quantification (K) of GPX4, normalized to β-actin, n = 3 in each group. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Article Snippet: Purified HSPA8 (11329-H07E, sinoBiological) served as a target and was labeled with fluorescence by Monolith Labeling Kit RED-tris-NTA (MO-L018, NanoTemper Technologies).

    Techniques: Immunoprecipitation, Co-Immunoprecipitation Assay, Western Blot, Immunofluorescence, Confocal Microscopy, Staining, Fluorescence, Expressing, Binding Assay, Mutagenesis, Over Expression

    Liposome coated scaffolds are suitable substrates for cells and enable cytokine presentation: (A) live HEK293 cell counts were measured from multiple time points on unpoled scaffolds with and without cationic liposome coating. Data is presented as mean ± SEM from 3 independent wells at each time point. Statistical significance was assessed by two-way ANOVA with Sidak's multiple comparisons test, comparing coated to uncoated scaffold at each time point. P values reflect differences between groups at individual time points, and all error bars are present on graph although some are too small to see. (B) Unpoled scaffolds were coated with fluorescent Cy5-labeled liposomes and imaged with confocal microscopy. Jurkat T cells were stained with calcein, cultured on Cy5 liposome-coated scaffolds, and imaged at 60× resolution 3 days after plating. (C) Jurkat T cells were fixed on day 4 and stained intracellularly with ActinProbe555 and DAPI. Arrows indicate punctate actin (yellow) or liposome uptake (magenta). Scale bars are 50 µm or 10 µm. (D) Activating the JAK-STAT Pathway with IL-15 Liposomes on Scaffolds: (i) unpoled scaffolds were coated with 2 mg mL −1 of IL-15-tethered liposomes in optimized HEPES-NaCl buffer conditions and SEAP is produced in response to IL-15 recognition. (ii) IL-15 reporter cells were plated on unpoled scaffolds, and absorbance was read daily, correlating to the downstream SEAP production from activation of the JAK-STAT pathway with n = 3 samples per group. Data is presented as relative fold change from uncoated scaffold control, with mean ± SD. Significance is conducted with an Ordinary Two-Way Anova with multiple comparisons using Šídák's multiple comparisons test.

    Journal: Biomaterials Science

    Article Title: Modular noncovalent functionalization of electrospun piezoelectric scaffolds with bioactive nanocarriers

    doi: 10.1039/d5bm01563d

    Figure Lengend Snippet: Liposome coated scaffolds are suitable substrates for cells and enable cytokine presentation: (A) live HEK293 cell counts were measured from multiple time points on unpoled scaffolds with and without cationic liposome coating. Data is presented as mean ± SEM from 3 independent wells at each time point. Statistical significance was assessed by two-way ANOVA with Sidak's multiple comparisons test, comparing coated to uncoated scaffold at each time point. P values reflect differences between groups at individual time points, and all error bars are present on graph although some are too small to see. (B) Unpoled scaffolds were coated with fluorescent Cy5-labeled liposomes and imaged with confocal microscopy. Jurkat T cells were stained with calcein, cultured on Cy5 liposome-coated scaffolds, and imaged at 60× resolution 3 days after plating. (C) Jurkat T cells were fixed on day 4 and stained intracellularly with ActinProbe555 and DAPI. Arrows indicate punctate actin (yellow) or liposome uptake (magenta). Scale bars are 50 µm or 10 µm. (D) Activating the JAK-STAT Pathway with IL-15 Liposomes on Scaffolds: (i) unpoled scaffolds were coated with 2 mg mL −1 of IL-15-tethered liposomes in optimized HEPES-NaCl buffer conditions and SEAP is produced in response to IL-15 recognition. (ii) IL-15 reporter cells were plated on unpoled scaffolds, and absorbance was read daily, correlating to the downstream SEAP production from activation of the JAK-STAT pathway with n = 3 samples per group. Data is presented as relative fold change from uncoated scaffold control, with mean ± SD. Significance is conducted with an Ordinary Two-Way Anova with multiple comparisons using Šídák's multiple comparisons test.

    Article Snippet: Liposomes were incubated with recombinant histidine-tagged human IL-15 (Sino Biological #10360-H07E) overnight at 4 °C to achieve a concentration of 180 ng mL −1 IL-15 on liposomes at 2 mg mL −1 , the loading concentration, in HEPES-NaCl.

    Techniques: Labeling, Liposomes, Confocal Microscopy, Staining, Cell Culture, Produced, Activation Assay, Control