MA1-91399

antibody from Invitrogen Antibodies

Targeting: ACTB

Provider product page for MA1-91399

Western blot

Immunocytochemistry

Immunohistochemistry

Other assay

Antibody data

Antibody Data
Antigen structure
References [32]
Comments [0]
Validations
Western blot [4]
Immunocytochemistry [4]
Immunohistochemistry [1]
Other assay [25]

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Product number: MA1-91399 - Provider product page
Provider: Invitrogen Antibodies
Product name: beta Actin Monoclonal Antibody (AC-15)
Antibody type: Monoclonal
Antigen: Synthetic peptide
Description: Positive control of cultured human or chicken fibroblasts suggested.
Antibody clone number: AC-15
Concentration: 3 mg/mL

ACTB protein structure - MA1-91399 shown in red.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Western Blot analysis of beta Actin was performed by loading (1) HeLa, (2) Jurkat, (3) COS7, (4) NIH3T3, (5) PC-12, (6) RAT2, (7) CHO, (8) MDBK and (9) MDCK lysates. Proteins were transferred to a membrane and probed with a beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399) at a dilution of 1:5,000..

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Western Blot analysis of beta Actin was performed by loading (1) HeLa, (2) Jurkat, (3) COS7, (4) NIH3T3, (5) PC-12, (6) RAT2, (7) CHO, (8) MDBK and (9) MDCK lysates. Proteins were transferred to a membrane and probed with a beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399) at a dilution of 1:5,000..

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Knockout of ACTB was achieved by CRISPR-Cas9 genome editing using LentiArray™ Lentiviral sgRNA (Product # A32042, Assay ID CRISPR889078_LV) and LentiArray Cas9 Lentivirus (Product # A32064). Western blot analysis of ACTB was performed by loading 30 µg of A-375 wild type (Lane 1), A-375 Cas9 (Lane 2) and A-375 ACTB KO (Lane 3) whole cell extracts. The samples were electrophoresed using NuPAGE™ Novex™ 4-12% Bis-Tris Protein Gel (Product # NP0322BOX). Resolved proteins were then transferred onto a nitrocellulose membrane (Product # IB23001) by iBlot® 2 Dry Blotting System (Product # IB21001). The blot was probed with beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399, 1:5000 dilution) and Goat anti-Mouse IgG (H+L) Superclonal™ Recombinant Secondary Antibody, HRP (Product # A28177, 1:10,000 dilution) using the iBright™ FL1500 (Product # A44115). Chemiluminescent detection was performed usingSuperSignal™ West Dura Extended Duration Substrate (Product # 34076). Loss of signal upon CRISPR mediated knockout (KO) using the LentiArray™ CRISPR product line confirms that antibody is specific to ACTB.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Western Blot was performed using Anti-beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399) and a ~40 kDa band corresponding to Actin, cytoplasmic 1 was observed across cell lines and tissues tested. Whole cell extracts (30 µg lysate) of HeLa (Lane 1), A549 (Lane 2), A-431 (Lane 3), U-2 OS (Lane 4), Jurkat (Lane 5), PC-12 (Lane 6), NIH/3T3 (Lane 7), Mouse Spleen (Lane 8), Mouse Liver (Lane 9), Rat Spleen (Lane 10), Rat Liver (Lane 11) were electrophoresed using NuPAGE™ 4-12% Bis-Tris Protein Gel (Product # NP0321BOX). Resolved proteins were then transferred onto a Nitrocellulose membrane (Product # LC2001) by iBlot® 2 Dry Blotting System (Product # IB21001). The Blot was probed with the primary antibody (1:5000 dilution) and detected by chemiluminescence with Goat anti-Mouse IgG (H+L) Superclonal™ Recombinant Secondary Antibody, HRP (Product # A28177, 1:4000 dilution) using the iBright FL 1000 (Product # A32752). Chemiluminescent detection was performed using Novex® ECL Chemiluminescent Substrate Reagent Kit (Product # WP20005). doi:10.1038/bcj.2014.18

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Immunocytochemistry-Immunofluorescence analysis of beta-Actin in FS-11 cells using beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Immunocytochemistry-Immunofluorescence analysis of beta-Actin in FS-11 cells using beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Immunocytochemistry-Immunofluorescence analysis of beta-Actin in HS-68 cells using beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399) at 1:1000 (green) with DAPI (blue). Cells were fixed and permeabilized with methanol followed by methanol: acetone.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Immunofluorescence analysis of Actin, cytoplasmic 1 was performed using 70% confluent log phase HeLa cells. The cells were fixed with 4% paraformaldehyde for 5 minutes, permeabilized with 0.1% Triton™ X-100 for 10 minutes, and blocked with 2% BSA for 45 minutes at room temperature. The cells were labeled with beta Actin Monoclonal Antibody (AC-15) (Product # MA1-91399) at 1:100 dilution in 0.1% BSA, incubated at 4 degree celsius overnight and then labeled with Donkey anti-Mouse IgG (H+L) Highly Cross-Adsorbed Secondary Antibody, Alexa Fluor Plus 647 (Product # A32787), (1:2000 dilution), for 45 minutes at room temperature (Panel a: Green). Nuclei (Panel b:Blue) were stained with ProLong™ Diamond Antifade Mountant with DAPI (Product # P36962). F-actin (Panel c: Red) was stained with Rhodamine Phalloidin (Product # R415, 1:300). Panel d represents the merged image showing Cytoskeleton localization. Panel e represents control cells with no primary antibody to assess background. The images were captured at 60x magnification.

Supportive validation

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Supportive validation

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Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 4 Chloroquine-induced changes in Kupffer cells. ( a ) Microscopy images of chloroquine-induced vacuole formation in live cells. Cells were pretreated with 100 muM of chloroquine. Lysotracker, green. Scale bar, 50 mum (upper), 10 mum (lower). ( b ) Western blot analysis of phosphatidylinositol-binding clathrin assembly protein (PICALM), alpha-adaptin, and clathrin heavy chain expression in cells. beta-actin was used as a loading control. ( c ) Densitometric analysis of western blot results. Results represent the ratio between the protein of interest and beta-actin (mean +- s.d. of three samples), and are normalized to control cells. Statistics by Student's t -test. *** P < 0.001.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 1 shRNA-expressing viral particles reduce the level of IRP1 mRNA and increase FLC expression. Panel a: following viral infection and selection on puromycin, cells were assayed by qPCR to measure IRP1 transcript levels. Results are plotted as ratio of IRP1 transcript to beta actin transcript. Results are mean +/- SEM of three independent experiments. A paired t-test was used to test significance (* = p

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Fig 3 ITO production particles cause IkappaBalpha degradation. Representative western blot images of IkappaBalpha and actin from treated RAW ( A ) and BEAS-2B ( C ) cell lysates. Cells were treated with particle suspensions for 1 or 3 h, washed twice with PBS, and lysed. B, D . Densitometry analysis was performed and is represented as the percentage of IkappaBalpha compared to levels present in PBS control-treated lysates. Error bars represent the mean +- SD (n = 4). *, p < 0.05 compared to PBS.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: FIGURE 2 Exogenous MDVs mitigate hypoxia-induced H9C2 cardiomyocyte apoptosis. (A) Transmission electron microscopy images of the MDVs. (B) Results of particle size analysis showed that MDVs were predominantly ~50-150 nm in size. (C) H9C2 cells were treated with PKH26 (red) labeled MDVs (12 mug/mL) for 2 h. Reconstituted hypoxic MDVs were created from mitochondria isolated from ex vivo isolated Langendorff-perfused rat hearts and grouped into normoxic- (n-MDVs), mild hypoxic- (m-MDVs), and heavy hypoxic MDVs (h-MDVs). H9C2 cells were treated as indicated for 12 h: blank (without hypoxia), ctl (hypoxia alone), n-MDV (hypoxia + n-MDVs), m-MDV (hypoxia + m-MDVs), and h-MDV (hypoxia + h-MDVs). (D,E) Hypoxia significantly increased the number of apoptotic cells, which was improved by the addition of the MDVs ( n = 3); P values were estimated using one-way ANOVA with Bonferroni''s post hoc test; # P < 0.05 versus blank, * P < 0.05 versus ctl, ** P < 0.01 versus ctl. (F) Hypoxia treatment significantly increased caspase 3 activity, while all three types of MDVs reversed this trend ( n = 3); P values were estimated by one-way ANOVA with Bonferroni''s post hoc test; # P < 0.05 versus blank, * P < 0.05 versus ctl, ** P < 0.01 versus ctl. (G) H9C2 cells were treated as indicated for 12 h and immunolabeled to identify cleaved-caspase 3 (c-caspase 3, green) and nuclear material (DAPI-blue). Hypoxia significantly upregulated the expression of c-caspase 3, which could be reversed by treatme

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: FIGURE 3 Exogenous MDVs protect against hypoxia-induced H9C2 cardiomyocyte apoptosis via the mitochondrial pathway. H9C2 cells were treated as follows for 12 h: blank (without hypoxia), ctl (hypoxia alone), n-MDV (hypoxia + n-MDVs), m-MDV (hypoxia + m-MDVs), and h-MDV (hypoxia + h-MDVs). (A) Hypoxia significantly increased caspase 9 activity, with all three types of MDVs reversing this trend ( n = 3); # P < 0.05 versus blank, * P < 0.05 versus ctl. (B) Hypoxia significantly upregulated the expression of cleaved-caspase 9 (c-caspase 9), and treatment with MDVs could reverse some of this increased expression ( n = 3); P values were estimated using one-way ANOVA with Bonferroni''s post hoc test; # P < 0.05 versus blank, * P < 0.05 versus ctl. (C,D) Hypoxia significantly upregulated the expression of cytoplasmic CytC and reduced the expression of mitochondrial CytC, both of which were reversed following treatment with MDVs ( n = 3); P values were estimated using one-way ANOVA with Bonferroni''s post hoc test; # P < 0.05 versus blank, * P < 0.05 versus ctl, ** P < 0.01 versus ctl.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: FIGURE 4 Exogenous MDVs exert direct protective effects on mitochondria. (A) Representative images of the colocalization of MDVs labeled with PKH26 (red) and mitochondria labeled with MitoTracker Green (green). (B) H9C2 cells were treated as indicated for 12 h. Hypoxia significantly reduced intracellular ATP levels, which could be reversed following treatment with any of the three types of MDVs ( n = 3); P values were estimated by one-way ANOVA with Bonferroni''s post hoc test; # P < 0.05 versus blank, * P < 0.05 versus ctl, ** P < 0.01 versus ctl. (C) H9C2 cells were treated as indicated for 12 h and ROS generation was evaluated using DCFH-DA dye. Hypoxia significantly increased intracellular ROS levels, which could be reversed by any of the three types of MDVs. (D) H9C2 cells were treated as indicated for 3 h and mPTP opening was assessed by co-loading calcein AM and CoCl 2 . Opening of mPTP was significantly enhanced following hypoxia and was seen to significantly decrease following the addition of MDVs. (E) H9C2 cells were treated as indicated for 12 h. Hypoxia significantly upregulated the expression of CHOP and cleaved-caspase 12 (c-caspase 12), but no significant changes were observed following the addition of any of the three types of MDVs ( n = 3); P values were estimated using one-way ANOVA with Bonferroni''s post hoc test; * P < 0.05 versus blank.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: FIGURE 5 Exogenous MDVs protect against hypoxia-induced H9C2 cardiomyocyte apoptosis by conveying Bcl-2. (A) H9C2 cells were subjected to hypoxic conditions for 1 h and then homogenized for fractionation. Light fraction containing Bcl-2 appeared at the 20/30% sucrose interface and a heavier fraction containing Bcl-2 sedimented at the 40/50% interface. (B) Proteins were collected from MDVs for Western blot (whole cell protein served as a control). (C) H9C2 cells were treated with hypoxia for 1 h and immunolabeled for TOM20 (green), Bcl-2 (red), and PDH (blue). TOM20 + vesicles could be observed (white arrow); Bcl-2 + /PDH + vesicles (white triangle) rather than Bcl-2 + /TOM20 + vesicles were observed. (D) Proteins were collected from different types of MDVs, and equal quantities of MDV proteins were used for Bcl-2 detection. (E) H9C2 cells were treated with the three types of MDVs and total proteins were collected, showing that cells treated with MDVs had more Bcl-2 than the control ( n = 3); P values were estimated using one-way ANOVA with Bonferroni''s post hoc test; * P < 0.05 versus blank, ** P < 0.01 versus blank.

Supportive validation

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Experimental details: Figure 5 Western blotting for the expression of signaling protein. (A,B) Cell lysate were collected and subjected to Western blot assay to estimate the level of expression of interleukin 1 receptor-associated kinase 1 (IRAK1), transforming growth factor beta-activated kinase 1 (TAK1), TGF-beta-activated kinase 1 (TAB1), TNF receptor-associated factor 6 (TRAF6), and cyclin D1. (C,D) Expression of pIRAK1 and pTAK1. beta-actin was used as loading control. The respective bar graphs are presented as densitometry analysis as mean +- SD of experiments ( p < 0.05 is treated as significant).

Supportive validation

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Experimental details: Figure 5. Mutation of the automethylated lysines decreases PRC2 HMTase activity in vitro and in vivo. ( A ) Mutation of the three lysines (K510A K514A K515A, ""methylmutant"") decreases PRC2 activity on reconstituted trinucleosomes relative to activity of WT PRC2 preincubated with SAM. Another mutant (K514A K515A) showed less perturbation of catalytic activity. Radioactive 14 C-SAM was titrated from 1.3 to 12 uM. ( Right ) Quantification of the automethylation and H3K27 methylation signal of WT and methylmutant (mean +- SD, n = 3). ( B ) Mutation of the three lysines (K > A) decreases PRC2 activity on native polynucleosome substrate, whereas the triple K > R mutant has substantially normal activity. ( C ) EZH2 automethylation is essential for de novo H3K27me3 deposition. ( Left ) WT or methylmutant EZH2 plasmid was transfected into the EZH2-depleted HEK293T strain to test for restoration of the H3K27me3 level. ( Middle ) Western blot results of the strains transfected with WT, methylmutant, or blank control, with beta-actin used as a loading control. Nine microliters or 4.5 uL of lysate was loaded on the gel for Western blot analysis. ( Right ) Quantification of the EZH2, H3K27me3, and H3K27me2 Western blot results (9 uL of lysate), normalized to beta-actin. ( D ) EZH2 automethylation is dispensable for H3K27me3 maintenance. ( Left ) CRISPR-Cas9 gene-editing scheme. cDNA encoding the remaining amino acids of full-length EZH2 is inserted into exon 2 of the EZH2 locus. The cDNA

Supportive validation

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Experimental details: Figure 9 B-actin immunostained sections in the spleen showing A: Control group shows strong positive reaction in red and white pulps. B: TTA-treated group showing weak reaction in red and white pulp. C: Rapamycin-treated group showing weak reaction in the red and white pulp. D: Filgrastim-treated group showing strong positive reaction. E: Combined rapamycin and filgrastim group showing strong positive reaction (Immunoperoxidase technique for B-actin x40, scale bar 30 um) TTA: thioacetamide

Supportive validation

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Experimental details: Figure 1. NPC1 disease fibroblasts have altered cholesterol homeostasis and Ca 2+ signaling. (A) Left: Representative Western blot of NPC1 in healthy and NPC1 I1061T disease fibroblasts. Right: Quantification of NPC1 protein expression, normalized to beta-actin. (B) Representative superresolution images of healthy and NPC1 I1061T fibroblasts fixed and stained with filipin to show cholesterol distribution. Scale bar of inset represents 2.5 um. (C) Representative time series from Fluo-4-loaded healthy and NPC1 I1061T fibroblasts. (D-F) Quantification of Fluo-4 signals from healthy and NPC1 I1061T fibroblasts. (G) Comparison of resting fura-2 ratios. Error bars represent the standard error of the mean.

Supportive validation

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Experimental details: Figure 2. Resting SOCE, coupled with STIM1/ORAI1 expression and distribution, is increased in NPC1 I1061T fibroblasts. (A) Diagram of SOCE in healthy cells (i), schematic of GCAMP-CAAX Ca 2+ probe in healthy cells (ii), and representative live confocal images of a healthy cell expressing GCAMP-CAAX (iii). (B) Same as A, only for NPC1 I1061T fibroblasts. (C) Quantification of resting GCAMP-CAAX fluorescence. Gray portion indicates the AnCoA4-sensitive reduction in resting fluorescence. (D) Left: Representative ORAI1 Western blot from healthy and NPC1 I1061T fibroblasts. Right: Quantification of ORAI1 protein expression in fibroblasts, normalized to beta-actin. (E) Same as D, only for STIM1. (F) Top: Representative TIRF images from healthy and NPC1 I1061T fibroblasts stained for anti-ORAI1. Bottom: Superresolution localization map from dashed boxes within the TIRF images; dashed lines delineate edges of cells. Inset: Representative ORAI1 puncta. Scale bar represents 0.25 um. (G) Quantification of anti-ORAI1 localization map. (H and I) Same as F and G, only for STIM1. Error bars represent the standard error of the mean.

Supportive validation

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Experimental details: Figure 4. Resting luminal ER Ca 2+ is reduced in NPC1 I1061T fibroblasts. (A) Graphical depiction of differential ER Ca 2+ , mediated by enhanced ER Ca 2+ leak in NPC1 I1061T fibroblasts. (B) Schematic of D1-ER Ca 2+ probe. (C) Representative live confocal images of healthy and NPC1 I1061T fibroblasts expressing D1-ER. (D) Quantification of D1-ER FRET ratios. (E) Normalized individual Fluo-4 intensities (gray) and averaged intensity (black, n = 31) from healthy fibroblasts following addition of a Ca 2+ -free ionomycin-containing external solution. (F) Same as E, only NPC1 I1061T fibroblasts (red, n = 14). (G) Quantification of the normalized area under the ionomycin curve. (H) Left: Representative Western blot for SERCA 2A/2B from healthy and NPC1 I1061T lysates. Right: Quantification of protein expression, normalized to beta-actin. (I) Same as H, only for calreticulin (CALR). (J) Normalized D1-ER FRET ratios from healthy (black circles) and NPC1 I1061T fibroblasts (red squares) following application of TG. Fitted lines (healthy: black; NPC1 I1061T : red) represent one-phase decay curves. (K and L) Quantitative comparison of the slope decay and time constant from the healthy and NPC1 I1061T nonlinear regression curves. Error bars represent the standard error of the mean.

Supportive validation

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Experimental details: Figure 5. Differential expression of PSEN1 alters ER Ca 2+ and SOCE in NPC1 I1061T fibroblasts. (A) Representative PSEN1-NTF and PSEN1-CTF Western blots from healthy and NPC1 I1061T cells with or without siRNA targeting PSEN1. (B) Quantification of differential protein expression, normalized to beta-actin. (C) Top: Representative PSEN1 Western blot from tsA-201 cells transfected with PSEN1 and treated with NPC1 inhibitor, UA, or vehicle control. Bottom: Quantification of differential PSEN1 protein expression, normalized to beta-actin. (D) Averaged intracellular Fluo-4 responses following ionomycin treatment in NPC1 I1061T fibroblasts transfected for 48 h with either negative control siRNA (red) or siRNA targeting PSEN1 (orange). (E) Quantification of AUC, from NPC1 I1061T fibroblasts transfected with PSEN1 (orange) or control (red) siRNA. (F) Averaged time-course of NPC1 I1061T fibroblasts transfected with control siRNA (red) or siRNA targeting PSEN1 (orange). (G) Quantification of the AUC during TG. (H) Quantification of the AUC during SOCE. (I) Representative Western blot of NPC1 in healthy and NPC1 I1061T fibroblasts with or without siRNA (24 h) targeting PSEN1. (J) Quantification of differential protein expression, normalized to beta-actin. (K) Representative superresolution images of filipin staining from NPC1 I1061T fibroblasts treated with control or PSEN1 siRNA for 72 h. (L-N) Quantification of superresolution filipin images. Error bars represent the standard error of

Supportive validation

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Experimental details: Figure 1. CPT1C is necessary for proper axon growth. ( A ) Primary cortical neurons derived from WT and Cpt1c KO E16 mouse embryos were cultured and fixed at 4DIV. Then, axons were labeled with a specific marker (SMI-312; in green) and nuclei were detected with Hoechst staining (blue). CPT1C absence in KO cultures was corroborated by western blot. Axonal length was analyzed from three independent experiments performed in biological triplicates. Right graph shows the percentage of cells with axons of a certain length (intervals of 50 um), while in left graph the mean +- SEM of all axons is shown (n = 100 cells per genotype; Student's t test; ***p

Supportive validation

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Experimental details: Figure 3. CPT1C-protrudin interaction. ( A ) CPT1C-protrudin binding was analyzed in HeLa cells by co-immunoprecipitation (co-IP). HeLa cells were co-transfected with mCitrine-protrudin or mCitrine-ER-5 (Citrine-KDEL) and MYC-CPT1C. 36 hr later, citrine-containing proteins were immunoprecipitated with the GFP-Trap assay, and the indicated proteins were detected by immunoblot in whole lysate (input) and immunoprecipitated samples (IP). The co-IP was performed in biological triplicates. A representative image of the experiment is shown. ( B-C ) Binding evaluation by FRET assay in HEK293 cells. Percentage of FRET was measured by the increase of donor intensity after photobleaching. mTurquoise-ER (KDEL), mTurquoise-calnexin and Tubulin-mTurquoise2 (TUB) with CPT1C-SYFP2 were used as negative interactions, while Atlastin1-mTurquoise2 (ATL1) with protrudin-SYFP2 and atlastin-1-mTurquoise2 with CPT1C-SYFP2, as positive controls. Representative images of transfected cells with proteins fused to mTurquoise2 (donor; red) or SYFP2 (acceptor; green) are shown in B. Scale bar, 20 um. Values are shown in C as mean +- SD of 2 independent experiments performed in biological duplicates (n = 5-11 cells per condition were analyzed; One-way ANOVA followed by Bonferroni's multiple comparison test; **p