Journal: Nature Communications

Article Title: The TEX44-CPT1B axis regulates mitochondrial sheath assembly and fatty acid oxidation in sperm

doi: 10.1038/s41467-025-63280-x

Figure Lengend Snippet: A , B Co-immunoprecipitation assays assessing interactions between FLAG-TEX44 and HA-CPT1B. TEX44-FLAG and CPT1B-HA were immunoprecipitated from HEK293T cell lysate transfected with the indicated vectors with anti-FLAG ( A ) and anti-HA ( B ) antibodies. Interactions between proteins were detected with antibodies to FLAG or HA. Uncropped blots are provided in . C Immunofluorescent staining for TEX44-EGFP (green) or CPT1B-HA (magenta) with antibodies to EGFP or HA in HeLa cell lines. TOMM20 served as a mitochondrial marker (blue). The magnified region in the right panel shows TEX44 assemblies between mitochondria (marked by white arrows). Scale bars: 10 μm (left), 2 μm (right). D Immunofluorescent staining was performed to examine the expression of TEX44 and CPT1B during various stages of spermiogenesis (steps 1–16) in the testes of adult wild-type mice. TEX44 (magenta) and CPT1B (green) antibodies were used, along with PNA (white) to highlight acrosomal structures. Nuclei were stained with Hoechst (blue). Scale bars: 20 μm. E Immunofluorescent staining for CPT1B (magenta) and TEX44 (green) in human and mice sperm samples. Nuclei were stained with Hoechst (blue). Scale bars: 5 μm. F Graph showing disordered regions (IDRs) of TEX44 identified by IUPred3. A score of ≥0.5 indicates disordered regions. A schematic representation of TEX44 protein and truncated mutants is shown, with orange boxes indicating IDRs. The numbers represent amino acid residues. G Co-immunoprecipitation assay for full-length or truncated TEX44-FLAG and CPT1B-HA with antibodies to FALG or HA. Uncropped blots are provided in . H Immunofluorescent staining for full-length or truncated TEX44-FLAG (green) and CPT1B-HA (magenta) in HeLa cells. Nuclei were stained with Hoechst (blue). Scale bars: 10 μm. A – E , G , H All experiments were independently repeated at least three times with consistent results. Representative data are shown.

Article Snippet: Cpt1b flox/flox mice were generated by Cyagen Biosciences Inc.

Techniques: Immunoprecipitation, Transfection, Staining, Marker, Expressing, Co-Immunoprecipitation Assay

Journal: Nature Communications

Article Title: The TEX44-CPT1B axis regulates mitochondrial sheath assembly and fatty acid oxidation in sperm

doi: 10.1038/s41467-025-63280-x

Figure Lengend Snippet: A Generation of Cpt1b gene knockout mice through Cre-LoxP mediated exon deletion. B Scanning electron microscopy of spermatozoa from the cauda epididymis of control and Cpt1b gKO mice. White arrows indicate regions lacking mitochondria. Scale bars: 10 μm (left), 2 μm(right). C Transmission electron microscopy of spermatozoa from the cauda epididymis of control and Cpt1b gKO mice. The black boxed areas in the upper panels of each group are shown at higher magnification in the corresponding lower panels. Scale bars: 2 μm (upper), 1 μm (lower). D Immunofluorescence analysis of TEX44 (green) in spermatozoa from control and Cpt1b gKO mice. The mitochondrial sheath was labeled with TOMM20 (magenta), and nuclei were stained with Hoechst (blue). Scale bars: 50 μm. E Immunofluorescence analysis of TEX44 (green) from control and Cpt1b gKO testis. The mitochondrial sheath, acrosome, and nuclei were stained with GPX4 (magenta), WGA (yellow), and Hoechst (white), respectively. The regions demarcated by white dashed boxes in the middle panels of each group are presented at higher magnification in the corresponding right panels. The lower panels display the fluorescence intensity profiles corresponding to the areas indicated by the light blue lines. Scale bars: 20 μm (left), 10 μm (right). F Immunofluorescence analysis of CPT1B (green) from Tex44 +/+ and Tex44 −/− testis. TOMM20 (magenta) were used to stain the mitochondrial sheath, Hoechst (white) were used to stain nucleus, wheat germ agglutinin (WGA; yellow) were used to determine the step of spermiogenesis. The regions demarcated by white dashed boxes in the middle panels of each group are presented at higher magnification in the corresponding right panels. The lower panels display the fluorescence intensity profiles corresponding to the areas indicated by the light blue lines. Scale bars: 20 μm (left), 10 μm (right). B – F All experiments were independently repeated at least three times with consistent results. Representative data are shown.

Article Snippet: Cpt1b flox/flox mice were generated by Cyagen Biosciences Inc.

Techniques: Gene Knockout, Electron Microscopy, Control, Transmission Assay, Immunofluorescence, Labeling, Staining, Fluorescence

Journal: Nature Communications

Article Title: The TEX44-CPT1B axis regulates mitochondrial sheath assembly and fatty acid oxidation in sperm

doi: 10.1038/s41467-025-63280-x

Figure Lengend Snippet: A Schematic diagram of fatty acid transport. CPT1B, located on the mitochondrial outer membrane, converts long-chain acyl-CoA into long-chain acyl-carnitine. Short-chain fatty acids freely diffuse across mitochondrial membrane. B Quantification of carnitine, carnitine-conjugated long-chain fatty acids (LCFAs), and carnitine-conjugated short-chain fatty acids (SCFAs) in spermatozoa from control ( n = 16), Cpt1b gKO ( n = 9), and Tex44 −/− ( n = 9) mice. For L-palmitoylcarnitine, significant differences were observed between Cpt1b gKO and control ( P = 3.64 × 10 −5 ) and between Tex44 −/− and control ( P = 0.0019). For myristoyl-L-carnitine, significant differences were also observed between Cpt1b gKO and control ( P = 0.0002) and between Tex44 −/− and control ( P = 0.0002). Asterisks indicate statistical significance: P < 0.01 (**), P < 0.001 (***), P < 0.0001 (****); ns not significant, P ≥ 0.05. C Immunofluorescence analysis of CPT1B (green) in spermatozoa from Tex44 +/+ and Tex44 −/− mice. TOMM20 (magenta) marks mitochondria, Hoechst (blue) stains nuclei. Scale bars: 50 μm. D Western blot analysis showing comparable CPT1B protein levels in sperm from Tex44 +/+ and Tex44 −/− mice, with β-tubulin as a loading control. Uncropped blots are provided in . E Quantitative analysis of CPT1B protein level was performed and normalized with β-tubulin protein level ( n = 3). No statistically significant difference was observed (ns, P ≥ 0.05). F Schematic workflow for protein expression, purification, and subsequent CPT1B enzyme activity assay. CPT1B enzyme activity was tested alone and in combination with TEX44-FL or TEX44-C. G Coomassie brilliant blue staining to assess protein purity (CPT1B, TEX44-FL, TEX44-C), with BSA used as a reference for protein quantification. H CPT1B enzyme activity at incremental concentrations showing a linear relationship ( R 2 = 0.9884). Relative enzyme activity of CPT1B in the presence of TEX44-FL ( I ) or TEX44-C ( J ) at various TEX44-to-CPT1B ratios. TEX44-FL inhibits CPT1B activity in a dose-dependent manner, whereas TEX44-C enhances activity. For ( B , E ), data are presented as mean ± s.e.m. P values were determined using two-tailed unpaired Student’s t -tests. n values represent the number of biologically independent animals. C – E Experiments were performed using samples from three biologically independent mice, with consistent results observed. Representative images and blots are shown.

Article Snippet: Cpt1b flox/flox mice were generated by Cyagen Biosciences Inc.

Techniques: Membrane, Control, Immunofluorescence, Western Blot, Expressing, Purification, Enzyme Activity Assay, Activity Assay, Staining, Two Tailed Test

Journal: Nature Communications

Article Title: The TEX44-CPT1B axis regulates mitochondrial sheath assembly and fatty acid oxidation in sperm

doi: 10.1038/s41467-025-63280-x

Figure Lengend Snippet: A Predicted structure of full-length CPT1B and TEX44 colored by chain (left) or pLDDT scores (right). The top hit was presented. B , C Predicted structure of full-length CPT1B and TEX44 (385–530). Two representative results were presented. The N-terminal of TEX44 insert through CPT1B in ( B ) but not in ( C ). D All five predicted results of the complex structure between CPT1B and TEX44 (385–530) show an invariant segment of TEX44 (424–450) highlighted in red. E Electrostatic surface of CPT1B (left) and TEX44 (424–450) (right). Positively and negatively charges are indicated by blue and red colors, respectively.

Article Snippet: Cpt1b flox/flox mice were generated by Cyagen Biosciences Inc.

Techniques:

Journal: Nature Communications

Article Title: The TEX44-CPT1B axis regulates mitochondrial sheath assembly and fatty acid oxidation in sperm

doi: 10.1038/s41467-025-63280-x

Figure Lengend Snippet: A Schematic workflow for detecting ROS levels, morphological defects, and apoptosis in control, Tex44 −/− , and Cpt1b gKO spermatozoa after treatment with palmitoyl-CoA and carnitine. B Mean fluorescence intensity of ROS levels in sperm treated with increasing concentrations of palmitoyl coenzyme A (0, 10 nM, 100 nM, and 1 µM) in control, Tex44 −/− , and Cpt1b gKO mice ( n = 9 per group). Compared to controls, Tex44 −/− sperm showed significantly higher ROS levels at 0 nM ( P = 9.15 × 10 −15 ), 10 nM ( P = 2.38 × 10 −17 ), 100 nM ( P = 2.88 × 10 −20 ), and 1 µM ( P = 2.81 × 10 −19 ); Cpt1b gKO sperm showed significantly lower ROS levels at 0 nM ( P = 4.88 × 10 −18 ), 10 nM ( P = 4.32 × 10 −14 ), 100 nM ( P = 6.94 × 10 −20 ), and 1 µM ( P = 1.86 × 10 −19 ). The concentration of L-carnitine in each group was 1 mM. C , D HE staining of spermatozoa from control, Tex44 −/− and Cpt1b gKO mice ( C ) before and after treatment with 1 µM palmitoyl-CoA and 1 mM carnitine (n = 3, each). Quantification of bent tail rates in spermatozoa after treatment with 1 µM palmitoyl-CoA and 1 mM carnitine. Tex44 −/− spermatozoa show a significant increase after treatment ( P = 2.73 × 10 −5 ), while a moderate increase is seen in controls ( P = 0.0341). No significant change is observed in Cpt1b gKO spermatozoa ( P = 0.1304). Scale bars: 50 μm. E , F TUNEL staining (red) of control, Tex44 −/− and Cpt1b gKO spermatozoa, before and after treatment with 1 µM palmitoyl-CoA and 1 mM carnitine (n = 3, each). The quantification of TUNEL-positive spermatozoa is comparable between the control ( P = 0.2236) and Cpt1b gKO ( P = 0.5059) mice after treatment with 1 µM palmitoyl-CoA and 1 mM carnitine, but a significant increase in the Tex44 −/− mice ( P = 1.24 × 10 −7 ). The nuclei were stained with Hoechst (blue). Scale bars: 100 μm. For ( B , D , F ), data are presented as mean ± s.e.m. P values were determined using two-tailed unpaired Student’s t -tests. n values represent the number of biologically independent animals. * indicates statistical significance at P < 0.05. **** indicates statistical significance at P < 0.0001. ns not significant.

Article Snippet: Cpt1b flox/flox mice were generated by Cyagen Biosciences Inc.

Techniques: Control, Fluorescence, Concentration Assay, Staining, TUNEL Assay, Two Tailed Test

Journal: Nutrition & Diabetes

Article Title: Effect of puerarin in promoting fatty acid oxidation by increasing mitochondrial oxidative capacity and biogenesis in skeletal muscle in diabetic rats

doi: 10.1038/s41387-017-0009-6

Figure Lengend Snippet: Representative blot and quantification of ( a ) total CD36 protein in muscle lysates, and ( b ) membrane CD36 in muscle sarcolemma. β subunit of insulin receptor (IR) was performed to confirm PM localization and normalization. c Western blot analyses and quantification of CPT-1b, p-AMPK (Thr172)/AMPK and p-ACC (Ser79)/ACC in muscle lysates. d Relative mRNA expressions of LCAD, ACOX1, PPAR-δ were analyzed by real-time RT-PCR and normalized to β-actin. e Representative TEM micrographs showed significant IMCLs accumulation (arrows) in diabetic rats and with much reduced IMCLs in puerarin-treated animals. Scale bar: 1 μm. Data were normalized to NC and presented as mean ± s.d., n = 5. ** P < 0.01, vs. NC group; # P < 0.05, ## P < 0.01 vs. DM group

Article Snippet: Antibodies against CPT-1b (orb308786) were obtained from Biorbyt Ltd. (Cambridge, UK).

Techniques: Membrane, Western Blot, Quantitative RT-PCR

Journal: Nutrition & Diabetes

Article Title: Effect of puerarin in promoting fatty acid oxidation by increasing mitochondrial oxidative capacity and biogenesis in skeletal muscle in diabetic rats

doi: 10.1038/s41387-017-0009-6

Figure Lengend Snippet: a Insulin-stimulated phosphorylation of Akt (Ser473) determined by western blot. Cells were incubated with 100 nM insulin during the last 20 min of treatment. b Western blot analyses and quantification of total and membrane CD36 in myotubes. IR-β was performed to confirm PM localization and normalization. c Relative mRNA expressions of ACSL1, LCAD, and ACOX1 analyzed by real-time RT-PCR and normalized to β-actin. d Western blot analyses and quantification of CPT-1b and p-ACC (Ser79)/ACC. e FFA content in cells normalized by respective protein content. f Representative electron micrographs showed the deposition of lipid droplets (arrowheads) in palmitate-treated myotubes but few lipids accumulation in cells pretreated with puerarin. Scale bar: 0.5 μm. All data were from three independent experiments and presented as mean ± s.d. * P < 0.05, ** P < 0.01, vs. BSA group; # P < 0.05, ## P < 0.01 vs. PA group. PA palmitate

Article Snippet: Antibodies against CPT-1b (orb308786) were obtained from Biorbyt Ltd. (Cambridge, UK).

Techniques: Phospho-proteomics, Western Blot, Incubation, Membrane, Quantitative RT-PCR

Journal: Dose-response : a publication of International Hormesis Society

Article Title: Enhancement of Acylcarnitine Levels in Small Intestine of Abdominal Irradiation Rats Might Relate to Fatty Acid β-Oxidation Pathway Disequilibration.

doi: 10.1177/15593258221075118

Figure Lengend Snippet: Figure 4. Changes of carnitine palmitoyltransferase 1 (CPT1) expression level and enzyme activity in the small intestine samples of SD rats after abdominal irradiated with 0 Gy, 10 Gy, or 15 Gy of 60Co gamma rays (n = 3 rats per group). (A) The mRNA levels of CPT1 A and CPT1 B in the small intestine samples of SD rats were detected with real-time PCR at 72 h after abdominal irradiated with 0 Gy, 10 Gy, or 15 Gy of 60Co gamma rays. (B, C) The protein levels of CPT1A and CPT1B in the small intestine samples of SD rats were detected with western blot and quantified by densitometry at 72 h after abdominal irradiated with 0 Gy, 10 Gy, or 15 Gy of 60Co gamma rays. β-actin was used as a loading control. (D) The CPT1 enzymatic activities in the small intestinal homogenates of SD rats at 72 h after abdominal irradiated with 0 Gy, 10 Gy, or 15 Gy of 60Co gamma rays. Results were presented as fold change in enzymatic activity in the 10 Gy or 15 Gy group relative to that in the 0 Gy group. Data represent mean ± SEM (*P < .05, **P < .01, ***P < .001, compared with 0 Gy group, LSD t-test).

Article Snippet: Antibodies against CPT1A and β-actin were purchased from Proteintech (USA), antibody against CPT1B was purchased from Novus (USA), and anti-normal rabbit IgG and anti-normal mouse IgG were purchased from ZSGB (China).

Techniques: Expressing, Activity Assay, Irradiation, Real-time Polymerase Chain Reaction, Western Blot, Control

Journal: Cell reports

Article Title: PHDs/CPT1B/VDAC1 axis regulates long-chain fatty acid oxidation in cardiomyocytes

doi: 10.1016/j.celrep.2021.109767

Figure Lengend Snippet: (A) Coomassie-stained SDS-PAGE of FLAG-PHD3 co-immunoprecipitated proteins in NRVMs. PHD3 or LacZ was overexpressed in NRVMs, and co-immunoprecipitation was performed with anti-FLAG agarose beads. Pulled-down proteins were separated with SDS-PAGE and visualized with G-250 Coomassie blue. Protein identities were determined by tandem mass spectrometry analysis (1. Dync1h1; 2. Na + /K + ATPase α−1; 3. ATP synthase B; 4. GAPDH; 5. ANT; 6. MLP). The respective positions of PHD3 and CPT1B are labeled in the figure. (B) Co-immunoprecipitation and western blot revealed PHD2 and 3 binding to CPT1B. FLAG-PHD2 and FLAG-PHD3 were immunoprecipitated by anti-FLAG beads, and the precipitated proteins were analyzed by western blot with anti-FLAG and anti-CPT1B antibodies. (C) Co-immunoprecipitation and western blot revealed endogenous CPT1B binds to endogenous PHD2 and 3. The precipitated proteins were analyzed by western blot with anti-PHD2, PHD3, or CPT1B antibodies. (D) Oxygen consumption rate (OCR) in primary cardiomyocytes after DMOG or Etomoxir (CPT1 inhibitor, Eto) treatment. OCR was real-time analyzed in living NRVMs by using a SeaHorse XFp Flux Analyzer. DMOG treatment leads to a drastic decrease in LC-FAO. (E) Maximal respiration rate was estimated for each experimental group of cells. (F and G) Similar experiment was conducted by using PHD2/3_HKO NMCMs. After 4 consecutive days of 4-hydroxyl-tamoxifen (4OHT) treatment to induce PHD2/3 disruption (or DMSO for untreated control cells), OCR was measured following the same protocol that described for NRVMs (F) and maximal respiration rate estimated afterward (G). A dramatic decrease in LC-FAO was found in PHD2/3-deficient cardiomyocytes, and maximal respiration rate was significantly decreased only in 4OHT treated PHD2/3_HKO NMCMs therefore in response to the loss of PHD2/3. (H) Mitochondrial LCFA uptake in primary cardiomyocytes after DMOG treatment. Five days after seeding, NRVMs were cultured in serum free medium with 1 μM BODIPY 500/510 C12 in the presence of DMOG (1mM) or DMSO for 16 h (H, left panel). Mitochondria were labeled 5 with Mitotracker Red (H, middle panel). (I) The same overlay of each experiment at a higher magnification. Scale bars, 50 μm. For (D)–(G), results are shown ±SEM for an average of at least 4 different experiments: ****p < 0.0001.

Article Snippet: Mouse Cpt1b , Origene , Cat#MR210564.

Techniques: Staining, SDS Page, Immunoprecipitation, Mass Spectrometry, Labeling, Western Blot, Binding Assay, Disruption, Control, Cell Culture

Journal: Cell reports

Article Title: PHDs/CPT1B/VDAC1 axis regulates long-chain fatty acid oxidation in cardiomyocytes

doi: 10.1016/j.celrep.2021.109767

Figure Lengend Snippet: (A) Representative western blot for D2/3_HKO cardiac lysates collected at 0, 1, 2, and 4 weeks after tamoxifen infusion. The CPT1B protein level was transiently increased at 1 week after tamoxifen treatment, whereas the Hexokinase-2 (HK-2) protein level started to gradually increase. (B) Relative level of CPT1B level of transcript over the time after PHD2/3 disruption (n = 4 per group). (C) Western blot for PHD2/3_HWT and PHD2/3_HKO cardiac lysates collected after 4 weeks of tamoxifen infusion. (D) Quantitative analysis of CPT1B protein level was performed and normalized with actin protein level (n = 4 per group). (E) CPT1B catalytic activity in D2/3_HWT and D2/3_HKO mouse hearts by DTNB colorimetric assay (n = 10 per group), showing no difference regardless the genotype. (F) Liquid chromatography-mass spectrometry analysis of relative abundance of carnitine-conjugated LCFA in the heart of D2/3_HKO mouse (n = 4 per group), suggesting an accumulation of carnitine-conjugated LCFA and acetyl-carnitine in the heart of PHD2/3_HKO mice. Data are presented as means ± SEM. Statistically significant difference is shown by asterisks: *p < 0.05, **p < 0.01.

Article Snippet: Mouse Cpt1b , Origene , Cat#MR210564.

Techniques: Western Blot, Disruption, Activity Assay, Colorimetric Assay, Liquid Chromatography, Mass Spectrometry

Journal: Cell reports

Article Title: PHDs/CPT1B/VDAC1 axis regulates long-chain fatty acid oxidation in cardiomyocytes

doi: 10.1016/j.celrep.2021.109767

Figure Lengend Snippet: (A) CPT1B/VDAC1 binding domain identification. Full-length and C-terminal-truncated CPT1B were overexpressed with VDAC1 in 293T cells. Immunoblot for VDAC1 after anti-FLAG co-immunoprecipitation demonstrates that both CPT1B 1–616 and CPT1B 1–451 bind to VDAC1, whereas CPT1B 1–219 lost its binding capacity to VDAC1. (B) Recombinant PHD2 interacts with GST-CPT1B 220–451 in vitro . (C) Both VDAC1 and C-terminal-truncated VDAC1 bind to CPT1B. Immunoblot for CPT1B following co-immunoprecipitation with full-length or C-terminal-truncated (1–240) VDAC1 in 293T cells, which validates CPT1B/VDAC1 complex formation. (D) Competitive co-immunoprecipitation between CPT1B and C-truncated CPT1B. FLAG-tagged CPT1B was co-overexpressed in NRVMs, aside with a gradient expression level of GFP-tagged CPT1B 1–616 , which significantly decreases the amount of pull-down VDAC1. (E and F) VDAC1 knockout induced by Sh-RNA interference leads to a decrease in respiratory capacity (E), leading to a significant decrease in Maximal oxygen consumption rate (F). (G) Oxidative respiration was challenged in isolated NRVMs overexpressing CPT1B, CPT1B 1–616 , or GFP (control), showing a significant decrease of OCR in CPT1B 1–616 -overexpressing NRVMs. (H) Maximal OCR rate was significantly decreased in response to CPT1B 1–616 overexpression, whereas full-length CPT1B overexpression did not lead to any significant change. Representative pictures from 4 different experiments were shown per each result, as an average ± SEM. Statistically significant difference is represented by asterisks: **p < 0.01, ***p < 0.001.

Article Snippet: Mouse Cpt1b , Origene , Cat#MR210564.

Techniques: Binding Assay, Western Blot, Immunoprecipitation, Recombinant, In Vitro, Expressing, Knock-Out, Isolation, Control, Over Expression

Journal: Cell reports

Article Title: PHDs/CPT1B/VDAC1 axis regulates long-chain fatty acid oxidation in cardiomyocytes

doi: 10.1016/j.celrep.2021.109767

Figure Lengend Snippet: (A and B) Representative co-immunoprecipitation of CPT1B and overexpressed VDAC1-GFP in 293T cells (A) or endogenous VDAC1 in NRVMs (B), and resulted quantification (bottom panel, n = 4). (C) LC-MS/MS spectrum for prolyl-hydroxylation of GST-CPT1B 220–451 catalyzed by recombinant PHD2 in vitro . P295 residue was identified as the hydroxylation site in CPT1B. (D) Co-immunoprecipitation of VDAC1-GFP with FLAG-CPT1B-WT or CPT1B-P295A from PBS- or DMOG-pre-treated 293T cells, showing a better preservation of CPT1B-295A binding capacity to VDAC1 in DMOG pre-treated 293T cells. (E) OCR measurement by Sea Horse flux analyzer in D2/3_HKO NMCMs following PHD2/3 depletion and CPT1B-WT or CPT1B-P295 overexpression. (F) Estimated maximal oxygen consumption rate. Diagrams are shown as an average of 4 experiments ± SEM. Statistically significant difference is indicated by asterisks: *p < 0.05, ***p < 0.001, ****p < 0.0001.

Article Snippet: Mouse Cpt1b , Origene , Cat#MR210564.

Techniques: Immunoprecipitation, Liquid Chromatography with Mass Spectroscopy, Recombinant, In Vitro, Residue, Preserving, Binding Assay, Over Expression

Journal: Cell reports

Article Title: PHDs/CPT1B/VDAC1 axis regulates long-chain fatty acid oxidation in cardiomyocytes

doi: 10.1016/j.celrep.2021.109767

Figure Lengend Snippet: PHD2/3 catalyze prolyl-4-hydroxylation on CPT1B P295 residue, which promotes CPT1B/VDAC1 complex formation and facilitates LFCA mitochondrial uptake. Hypoxia inhibits PHD2/3 enzymatic activity, resulting in the disruption of CPT1B/VDAC1 complex and inhibition of LCFA mitochondrial uptake and metabolism.

Article Snippet: Mouse Cpt1b , Origene , Cat#MR210564.

Techniques: Residue, Activity Assay, Disruption, Inhibition

Journal: Cell reports

Article Title: PHDs/CPT1B/VDAC1 axis regulates long-chain fatty acid oxidation in cardiomyocytes

doi: 10.1016/j.celrep.2021.109767

Figure Lengend Snippet:

Article Snippet: Mouse Cpt1b , Origene , Cat#MR210564.

Techniques: Recombinant, Isolation, Purification, cDNA Synthesis, SYBR Green Assay, Control, Plasmid Preparation, Software