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anti trap1  (Absolute Biotech Inc)

 
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    Absolute Biotech Inc anti trap1
    Anti Trap1, supplied by Absolute Biotech Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+trap1/anti+trap1/pmc12582411-61-9-12
    Average 86 stars, based on 1 article reviews
    anti trap1 - by Bioz Stars, 2026-09
    86/100 stars

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    Western Blot:

    Article Title: Restricting metabolic plasticity enhances stress adaptation through the modulation of PDH and HIF1A in TRAP1-depleted colon cancer.
    Article Snippet: Metabolic plasticity allows cancer cells to survive under adverse conditions.. To investigate the role of mitochondrial chaperone tumor necrosis factor receptor-associated protein 1 (TRAP1) in this process, we used CRISPR/Cas9 mediated genetic deletion to knock out (KO) TRAP1 in colon cancer cells.. Depletion of TRAP1 triggered a series of events: induced metabolic reprogramming, increased glycolytic flux, downregulation of mitochondrial complex I, and elevated ROS generation.

    Article Title: Restricting metabolic plasticity enhances stress adaptation through the modulation of PDH and HIF1A in TRAP1-depleted colon cancer
    Article Snippet: Nuclear part and cytoplasm part were separated by NE-PER TM Nuclear and Cytoplasmic Extraction kit (Thermo Fisher, Waltham, MA, USA) according to the manufacturer’s protocol. .. Western blot analysis was performed using the following antibodies: anti-TRAP1 (1:1000) from LSBio (Lynnwood, WA, USA), anti-MCT1 (1:500), anti-NDUFA10 (1:500), anti-NDUFS2 (1:500) from Santa Cruz (Dallas, TX, USA), anti-GLUT1 (1:1000), anti-HIF1A (1:1000), anti-PDH (1:1000), anti-pPDH (S293) (1:1000), anti-pPDH (S232) (1:1000), anti-Lamin B1 (1:1000), anti-PARP (1:1000), anti-CHOP (1:1000), anti-tubulin (1:5000) and anti-actin (1:5000) were obtained from Cell Signaling (Danvers, MA, USA). .. Acrylamide gel was purchased from Bio-Rad (Hercules, CA, USA).



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    a Sequence alignment of the C-terminal regions of human FATE1 and Mff generated with Jalview using the T-Coffee algorithm under default settings. Amino acid numbering corresponds to Mff. b Coiled coil domain prediction of FATE1 using the COILS program. Mff and Bnip3 were included as positive and negative controls, respectively. Predicted probabilities for coiled coil formation are shown for scanning windows of 14, 21 and 28 residues. c Schematic comparison of the domain architecture of Mff and FATE1, highlighting sequence homologies, including the predicted coiled coil domain and transmembrane region. R1 and R2 indicate the short repeat motifs in Mff involved in Drp1 recruitment. d Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with RFP-KDEL (ER marker) for 24 h in HeLa cells. Blue arrows, ER-localized FATE1 at perinuclear regions. e Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with mito-RFP (mitochondrial marker) for 24 h in HeLa cells. f Subcellular fractionation of HeLa cells transfected with GFP-tagged constructs as indicated. Fractionation yielded cytosolic (S1), rest-mitochondrial (P1) and purified mitochondrial (P2) fractions, analyzed by immunoblotting. g Representative widefield images of MCF-7 cells expressing GFP-FATE1 or GFP-Mff for 24 h and IF stained for mitochondrial matrix protein <t>TRAP1.</t> Plot profiles along yellow lines in zoom images show fluorescence intensity of GFP and TRAP1 signals. h STED super-resolution microscopy of HeLa cells expressing pcDNA-FATE1 and IF stained for FATE1 in combination with Cox IV (IMM marker) or Tom20 (OMM marker). Plot profiles show fluorescence intensity of FATE1 and Cox IV or Tom20. Scale bars, 10 µm
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    a Sequence alignment of the C-terminal regions of human FATE1 and Mff generated with Jalview using the T-Coffee algorithm under default settings. Amino acid numbering corresponds to Mff. b Coiled coil domain prediction of FATE1 using the COILS program. Mff and Bnip3 were included as positive and negative controls, respectively. Predicted probabilities for coiled coil formation are shown for scanning windows of 14, 21 and 28 residues. c Schematic comparison of the domain architecture of Mff and FATE1, highlighting sequence homologies, including the predicted coiled coil domain and transmembrane region. R1 and R2 indicate the short repeat motifs in Mff involved in Drp1 recruitment. d Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with RFP-KDEL (ER marker) for 24 h in HeLa cells. Blue arrows, ER-localized FATE1 at perinuclear regions. e Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with mito-RFP (mitochondrial marker) for 24 h in HeLa cells. f Subcellular fractionation of HeLa cells transfected with GFP-tagged constructs as indicated. Fractionation yielded cytosolic (S1), rest-mitochondrial (P1) and purified mitochondrial (P2) fractions, analyzed by immunoblotting. g Representative widefield images of MCF-7 cells expressing GFP-FATE1 or GFP-Mff for 24 h and IF stained for mitochondrial matrix protein <t>TRAP1.</t> Plot profiles along yellow lines in zoom images show fluorescence intensity of GFP and TRAP1 signals. h STED super-resolution microscopy of HeLa cells expressing pcDNA-FATE1 and IF stained for FATE1 in combination with Cox IV (IMM marker) or Tom20 (OMM marker). Plot profiles show fluorescence intensity of FATE1 and Cox IV or Tom20. Scale bars, 10 µm
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    a Sequence alignment of the C-terminal regions of human FATE1 and Mff generated with Jalview using the T-Coffee algorithm under default settings. Amino acid numbering corresponds to Mff. b Coiled coil domain prediction of FATE1 using the COILS program. Mff and Bnip3 were included as positive and negative controls, respectively. Predicted probabilities for coiled coil formation are shown for scanning windows of 14, 21 and 28 residues. c Schematic comparison of the domain architecture of Mff and FATE1, highlighting sequence homologies, including the predicted coiled coil domain and transmembrane region. R1 and R2 indicate the short repeat motifs in Mff involved in Drp1 recruitment. d Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with RFP-KDEL (ER marker) for 24 h in HeLa cells. Blue arrows, ER-localized FATE1 at perinuclear regions. e Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with mito-RFP (mitochondrial marker) for 24 h in HeLa cells. f Subcellular fractionation of HeLa cells transfected with GFP-tagged constructs as indicated. Fractionation yielded cytosolic (S1), rest-mitochondrial (P1) and purified mitochondrial (P2) fractions, analyzed by immunoblotting. g Representative widefield images of MCF-7 cells expressing GFP-FATE1 or GFP-Mff for 24 h and IF stained for mitochondrial matrix protein <t>TRAP1.</t> Plot profiles along yellow lines in zoom images show fluorescence intensity of GFP and TRAP1 signals. h STED super-resolution microscopy of HeLa cells expressing pcDNA-FATE1 and IF stained for FATE1 in combination with Cox IV (IMM marker) or Tom20 (OMM marker). Plot profiles show fluorescence intensity of FATE1 and Cox IV or Tom20. Scale bars, 10 µm
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    a Sequence alignment of the C-terminal regions of human FATE1 and Mff generated with Jalview using the T-Coffee algorithm under default settings. Amino acid numbering corresponds to Mff. b Coiled coil domain prediction of FATE1 using the COILS program. Mff and Bnip3 were included as positive and negative controls, respectively. Predicted probabilities for coiled coil formation are shown for scanning windows of 14, 21 and 28 residues. c Schematic comparison of the domain architecture of Mff and FATE1, highlighting sequence homologies, including the predicted coiled coil domain and transmembrane region. R1 and R2 indicate the short repeat motifs in Mff involved in Drp1 recruitment. d Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with RFP-KDEL (ER marker) for 24 h in HeLa cells. Blue arrows, ER-localized FATE1 at perinuclear regions. e Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with mito-RFP (mitochondrial marker) for 24 h in HeLa cells. f Subcellular fractionation of HeLa cells transfected with GFP-tagged constructs as indicated. Fractionation yielded cytosolic (S1), rest-mitochondrial (P1) and purified mitochondrial (P2) fractions, analyzed by immunoblotting. g Representative widefield images of MCF-7 cells expressing GFP-FATE1 or GFP-Mff for 24 h and IF stained for mitochondrial matrix protein TRAP1. Plot profiles along yellow lines in zoom images show fluorescence intensity of GFP and TRAP1 signals. h STED super-resolution microscopy of HeLa cells expressing pcDNA-FATE1 and IF stained for FATE1 in combination with Cox IV (IMM marker) or Tom20 (OMM marker). Plot profiles show fluorescence intensity of FATE1 and Cox IV or Tom20. Scale bars, 10 µm

    Journal: bioRxiv

    Article Title: The Cancer/Testis Antigen FATE1 Antagonizes Fission and Preserves Mitochondrial Network Integrity under Cytotoxic Stress

    doi: 10.1101/2025.08.18.670752

    Figure Lengend Snippet: a Sequence alignment of the C-terminal regions of human FATE1 and Mff generated with Jalview using the T-Coffee algorithm under default settings. Amino acid numbering corresponds to Mff. b Coiled coil domain prediction of FATE1 using the COILS program. Mff and Bnip3 were included as positive and negative controls, respectively. Predicted probabilities for coiled coil formation are shown for scanning windows of 14, 21 and 28 residues. c Schematic comparison of the domain architecture of Mff and FATE1, highlighting sequence homologies, including the predicted coiled coil domain and transmembrane region. R1 and R2 indicate the short repeat motifs in Mff involved in Drp1 recruitment. d Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with RFP-KDEL (ER marker) for 24 h in HeLa cells. Blue arrows, ER-localized FATE1 at perinuclear regions. e Representative widefield images of GFP-Ctrl, GFP-FATE1, or GFP-Mff co-expressed with mito-RFP (mitochondrial marker) for 24 h in HeLa cells. f Subcellular fractionation of HeLa cells transfected with GFP-tagged constructs as indicated. Fractionation yielded cytosolic (S1), rest-mitochondrial (P1) and purified mitochondrial (P2) fractions, analyzed by immunoblotting. g Representative widefield images of MCF-7 cells expressing GFP-FATE1 or GFP-Mff for 24 h and IF stained for mitochondrial matrix protein TRAP1. Plot profiles along yellow lines in zoom images show fluorescence intensity of GFP and TRAP1 signals. h STED super-resolution microscopy of HeLa cells expressing pcDNA-FATE1 and IF stained for FATE1 in combination with Cox IV (IMM marker) or Tom20 (OMM marker). Plot profiles show fluorescence intensity of FATE1 and Cox IV or Tom20. Scale bars, 10 µm

    Article Snippet: Cells were then incubated with primary antibodies against Tom20 (Santa Cruz, no. sc-11415; 1:200) or FATE1 (Santa Cruz Biotechnology, no. sc-101220; 1:100) for 1 h at room temperature, or against COX IV (Cell Signaling, no. 4850S; 1:50) or TRAP1 (Novus Biologicals, no. NB300-555; 1:100) antibodies at 4°C overnight.

    Techniques: Sequencing, Generated, Comparison, Marker, Fractionation, Transfection, Construct, Purification, Western Blot, Expressing, Staining, Fluorescence, Super-Resolution Microscopy