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Sequence of primers and identity of sequenced clones of rat anx cDNAs. The colored boxes represent recognition sites for restriction enzymes. Yellow, blue, green and red colors highlight the Nco I, Acc 65I, Not I and Bsa I sites, respectively. Letters in bold represent NcoI compatible sites.

Sequence of primers and identity of sequenced clones of rat anx cDNAs. The colored boxes represent recognition sites for restriction enzymes. Yellow, blue, green and red colors highlight the Nco I, Acc 65I, Not I and Bsa I sites, respectively. Letters in bold represent NcoI compatible sites.

Anxa7, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anxa7/Annexin+VII+Antibody/pmc10311354-238-49-51
Average 93 stars, based on 19 article reviews

anxa7 - by Bioz Stars, 2026-09

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1) Product Images from "RNA-binding is an ancient trait of the Annexin family"

Article Title: RNA-binding is an ancient trait of the Annexin family

Journal: Frontiers in Cell and Developmental Biology

doi: 10.3389/fcell.2023.1161588

Figure Legend Snippet: Sequence of primers and identity of sequenced clones of rat anx cDNAs. The colored boxes represent recognition sites for restriction enzymes. Yellow, blue, green and red colors highlight the Nco I, Acc 65I, Not I and Bsa I sites, respectively. Letters in bold represent NcoI compatible sites.

Techniques Used: Sequencing, Clone Assay

$AnxA1, AnxA2, AnxA4, AnxA5, AnxA6, AnxA7, AnxA10, AnxA11 and AnxA13 present in the cytoskeleton fraction (Panel A) are associated with non-polysomal mRNP complexes (Panel B) of PC12 cells. Panel (A) 30 µg of the cytoskeletal fraction (lane 1) and cytoskeleton-bound polysomes (lane 2) were separated by 10% SDS-PAGE and transferred to nitrocellulose membranes. Panel (B) samples prepared from oligo (dT)-bound mRNP complexes from the cytoskeletal fraction [supernatant after centrifugation for 2 h 100,000 g above a 1 M (35%) sucrose cushion] (lanes 3 and 4), without (lane 3) or with RNase (lane 4) treatment, as indicated above the Western blots, were subjected to similar analysis. The blots were probed with antibodies against the different Anxs and against PABP1 as a marker for poly(A)-containing mRNAs, as indicated. Antibodies against the ribosomal subunit S6 were used to inform of the distribution of ribosomes. In addition, the blots were probed with antibodies against early endosomes (EEA1), late endosomes (Rab7) and recycling endosomes (Rab11). SPC25 and LAMP1 were not detectable in any of the fractions (results not shown). Visualization of the immunoreactive protein bands was performed using the ChemiDocTM XRS+ molecular imager after incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies and enhanced chemiluminescence (ECL)-reagent. The blots shown are representative for results from three experiments.$
Figure Legend Snippet: AnxA1, AnxA2, AnxA4, AnxA5, AnxA6, AnxA7, AnxA10, AnxA11 and AnxA13 present in the cytoskeleton fraction (Panel A) are associated with non-polysomal mRNP complexes (Panel B) of PC12 cells. Panel (A) 30 µg of the cytoskeletal fraction (lane 1) and cytoskeleton-bound polysomes (lane 2) were separated by 10% SDS-PAGE and transferred to nitrocellulose membranes. Panel (B) samples prepared from oligo (dT)-bound mRNP complexes from the cytoskeletal fraction [supernatant after centrifugation for 2 h 100,000 g above a 1 M (35%) sucrose cushion] (lanes 3 and 4), without (lane 3) or with RNase (lane 4) treatment, as indicated above the Western blots, were subjected to similar analysis. The blots were probed with antibodies against the different Anxs and against PABP1 as a marker for poly(A)-containing mRNAs, as indicated. Antibodies against the ribosomal subunit S6 were used to inform of the distribution of ribosomes. In addition, the blots were probed with antibodies against early endosomes (EEA1), late endosomes (Rab7) and recycling endosomes (Rab11). SPC25 and LAMP1 were not detectable in any of the fractions (results not shown). Visualization of the immunoreactive protein bands was performed using the ChemiDocTM XRS+ molecular imager after incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies and enhanced chemiluminescence (ECL)-reagent. The blots shown are representative for results from three experiments.

Techniques Used: SDS Page, Centrifugation, Western Blot, Marker, Incubation

An overview of the binding of rat Anxs to the different RNA probes as determined by spot blot and UV crosslinking (xlinking) experiments. xxx indicates strong binding and X indicates weak RNA binding with XX indicating intermediate binding. Also the presence of Anxs in mRNP complexes derived from PC12 cells detected with specific antibodies are indicated.

Figure Legend Snippet: An overview of the binding of rat Anxs to the different RNA probes as determined by spot blot and UV crosslinking (xlinking) experiments. xxx indicates strong binding and X indicates weak RNA binding with XX indicating intermediate binding. Also the presence of Anxs in mRNP complexes derived from PC12 cells detected with specific antibodies are indicated.

Techniques Used: Binding Assay, RNA Binding Assay, Derivative Assay

UV-crosslinking competition experiments employing rat Anxs and radiolabeled [α 32 P]-rUTP c-myc or anxA2 3′UTRs. 2 μM purified rat Anxs (except 0.4 µM of AnxA7; 0.3 µM of AnxA9 and 0.5 µM of AnxA11) were UV-crosslinked in the absence of RNA (lanes 1 and 5). 100,000 cpm of radiolabeled anxA2 3′UTR (7 fmoles) or c-myc 3′UTR (6 fmoles) were UV-crosslinked to purified rat Anxs in the absence (lanes 2 and 6) or presence of 25x (lanes 3 and 7), or 50x (lanes 4 and 8) molar excess of the corresponding unlabeled transcript. 2 μM BSA and mutant AnxA2 served as negative controls. After UV-crosslinking and RNase treatment, the samples were subjected to 4%–15% SDS-PAGE and the proteins were stained with Coomassie Brilliant Blue (lanes 1–4), whereafter the gels were dried. The [α 32 P]-rUTP-labeled RNA covalently bound to the respective Anxs, as indicated, was visualized using screens and phosphor-imaging following an overnight (c-myc 3′UTR) or 6 h (anxA2 3′UTR) exposure (lanes 5–8). PageRuler prestained protein ladder (from top to bottom: 100 kDa, 70 kDa (the most prominent band), 55 kDa, 40 kDa, 35 kDa and 25 kDa) are shown to the left of the AnxA1, AnxA3, AnxA5, AnxA7, AnxA8, AnxA10, Δ188AnxA11 and BSA samples. The representative images are from two experiments performed with competition while RNA-Anx binding was performed four times without competition.

Figure Legend Snippet: UV-crosslinking competition experiments employing rat Anxs and radiolabeled [α 32 P]-rUTP c-myc or anxA2 3′UTRs. 2 μM purified rat Anxs (except 0.4 µM of AnxA7; 0.3 µM of AnxA9 and 0.5 µM of AnxA11) were UV-crosslinked in the absence of RNA (lanes 1 and 5). 100,000 cpm of radiolabeled anxA2 3′UTR (7 fmoles) or c-myc 3′UTR (6 fmoles) were UV-crosslinked to purified rat Anxs in the absence (lanes 2 and 6) or presence of 25x (lanes 3 and 7), or 50x (lanes 4 and 8) molar excess of the corresponding unlabeled transcript. 2 μM BSA and mutant AnxA2 served as negative controls. After UV-crosslinking and RNase treatment, the samples were subjected to 4%–15% SDS-PAGE and the proteins were stained with Coomassie Brilliant Blue (lanes 1–4), whereafter the gels were dried. The [α 32 P]-rUTP-labeled RNA covalently bound to the respective Anxs, as indicated, was visualized using screens and phosphor-imaging following an overnight (c-myc 3′UTR) or 6 h (anxA2 3′UTR) exposure (lanes 5–8). PageRuler prestained protein ladder (from top to bottom: 100 kDa, 70 kDa (the most prominent band), 55 kDa, 40 kDa, 35 kDa and 25 kDa) are shown to the left of the AnxA1, AnxA3, AnxA5, AnxA7, AnxA8, AnxA10, Δ188AnxA11 and BSA samples. The representative images are from two experiments performed with competition while RNA-Anx binding was performed four times without competition.

Techniques Used: Purification, Mutagenesis, SDS Page, Staining, Labeling, Imaging, Binding Assay

Blocking Assay:

Article Title: Early proteome analysis of rat pancreatic acinar AR42J cells treated with taurolithocholic acid 3-sulfate.
Article Snippet: Background: Bile acids are the initiating factors of biliary acute pancreatitis.. Bile acids can induce the activation of intracellular zymogen, thus leading injury in pancreatic acinar cells.. Pathological zymogen activation in pancreatic acinar cells is a common feature of all types of acute pancreatitis.

Saline:

Membrane:

Incubation:

Image Search Results

Figure 1. Lipid droplets exist in neurons and activation of ANXA7 promotes lipid droplets formation. a–c) The OGD/R model was constructed on primary neurons after SEC or ABO treatment for 1 h. The neutral lipid dye HCS LipidTOX was used to detect the levels of neutral lipids and lipid droplets in diﬀerent groups. Scale bar: 10 μm. d) The OGD/R model was constructed on neurons treated with SEC or ABO for 1 h, and the lipid peroxidation (LPO) kit was used to detect the lipid peroxidation level of neurons. e–g) Lipid droplets in neurons were stained by BODIPY 493/503 after OGD/R treatment with SEC or ABO. Scale bar: 10 μm. h) GO analysis was performed between SEC+OGD/R group and OGD/R treatment group after 4D proteomic sequencing. i) The results of up/down regulated activities in biological process (BP) analysis. The data were presented as mean ± SD, and ANOVA was used for analysis. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Lipid Droplets Metabolism Mediated by ANXA7-PPARγ Signaling Axis Regulates Spinal Cord Injury Repair in Mice.

doi: 10.1002/advs.202417326

Figure Lengend Snippet: Figure 1. Lipid droplets exist in neurons and activation of ANXA7 promotes lipid droplets formation. a–c) The OGD/R model was constructed on primary neurons after SEC or ABO treatment for 1 h. The neutral lipid dye HCS LipidTOX was used to detect the levels of neutral lipids and lipid droplets in diﬀerent groups. Scale bar: 10 μm. d) The OGD/R model was constructed on neurons treated with SEC or ABO for 1 h, and the lipid peroxidation (LPO) kit was used to detect the lipid peroxidation level of neurons. e–g) Lipid droplets in neurons were stained by BODIPY 493/503 after OGD/R treatment with SEC or ABO. Scale bar: 10 μm. h) GO analysis was performed between SEC+OGD/R group and OGD/R treatment group after 4D proteomic sequencing. i) The results of up/down regulated activities in biological process (BP) analysis. The data were presented as mean ± SD, and ANOVA was used for analysis. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Article Snippet: After blocking with 5% BSA, the samples were incubated with primary antibodies at 4 °C overnight: NRF2 (Cell signaling technology, Cat# 12721S), HO-1 (Abcam, Cat# ab189491), PPARγ (Abcam, Cat# ab178860), ANXA7 (Proteintech, Cat# 10154-2-AP), PLIN5 (Proteintech, Cat# 26951-1-AP), PLIN2 (Santa Cruz, Cat# sc-377429), PLIN1(Abcam, Cat# ab172907), VDAC1 (Proteintech, Cat# 66345-1-Ig).

Techniques: Activation Assay, Construct, Staining, Sequencing

Figure 2. ANXA7 activation could suppress oxidative stress induced by OGD/R treatment. a) GSEA analysis after 4D proteome sequencing between SEC+OGD/R and OGD/R treatment group. b,c) OGD/R model was constructed on neurons after SEC or ABO treatment for 1 h, and NRF2 protein level was detected by immunoﬂuorescence. Scale bar: 20 μm. d,e) The OGD/R model was constructed on neurons after SEC treatment for 1 h, and the GPX4 protein level was detected by WB. f–h) OGD/R model was constructed on neurons after SEC treatment for 1 h, and mRNA levels of Nrf2, Ho-1, and Gpx4 in diﬀerent treatment groups were detected by qPCR. i,j) HO-1 ﬂuorescent staining on neurons after OGD/R with/without SEC or ABO treatment. Scale bar: 10 μm. k,l) LPO and malondialdehyde (MDA) levels were detected in neurons treated with SEC or combination of SEC and Beauveriolide III for 1 h after OGD/R. The data were presented as mean ± SD, and Student’s T-test was used for analysis between two groups, while ANOVA was used among more than two groups. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Lipid Droplets Metabolism Mediated by ANXA7-PPARγ Signaling Axis Regulates Spinal Cord Injury Repair in Mice.

doi: 10.1002/advs.202417326

Figure Lengend Snippet: Figure 2. ANXA7 activation could suppress oxidative stress induced by OGD/R treatment. a) GSEA analysis after 4D proteome sequencing between SEC+OGD/R and OGD/R treatment group. b,c) OGD/R model was constructed on neurons after SEC or ABO treatment for 1 h, and NRF2 protein level was detected by immunoﬂuorescence. Scale bar: 20 μm. d,e) The OGD/R model was constructed on neurons after SEC treatment for 1 h, and the GPX4 protein level was detected by WB. f–h) OGD/R model was constructed on neurons after SEC treatment for 1 h, and mRNA levels of Nrf2, Ho-1, and Gpx4 in diﬀerent treatment groups were detected by qPCR. i,j) HO-1 ﬂuorescent staining on neurons after OGD/R with/without SEC or ABO treatment. Scale bar: 10 μm. k,l) LPO and malondialdehyde (MDA) levels were detected in neurons treated with SEC or combination of SEC and Beauveriolide III for 1 h after OGD/R. The data were presented as mean ± SD, and Student’s T-test was used for analysis between two groups, while ANOVA was used among more than two groups. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Techniques: Activation Assay, Sequencing, Construct, Staining

Figure 3. ANXA7 could interact with PPAR𝛾. a) SWISS-MODEL/Vasker Lab/PDBePISA websites were used to predict structure of ANXA7, PPAR𝛾, and 3D structure diagram of their interaction. b) Co-immunoprecipitation was used to detect the interaction between ANXA7 and PPAR𝛾. c) Immunoﬂuo- rescence was used to detect the colocalization of ANXA7 and PPAR𝛾, and the colocalization analysis was conducted. Scale bar: 10 μm. d,e) The protein level of PPAR𝛾was detected by WB after treatment SEC or ABO for 1 h. f,g) Neurons were treated with SEC or ABO for 1 h before OGD/R, and im- munoﬂuorescence was used to detect the nuclear level of PPAR𝛾. Scale bar: 10 μm. h,i) Nuclear expression of PPAR𝛾was detected by WB. The data were presented as mean ± SD, and ANOVA was used for analysis. **p < 0.01, ***p < 0.001, n = 3.

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Lipid Droplets Metabolism Mediated by ANXA7-PPARγ Signaling Axis Regulates Spinal Cord Injury Repair in Mice.

doi: 10.1002/advs.202417326

Figure Lengend Snippet: Figure 3. ANXA7 could interact with PPAR𝛾. a) SWISS-MODEL/Vasker Lab/PDBePISA websites were used to predict structure of ANXA7, PPAR𝛾, and 3D structure diagram of their interaction. b) Co-immunoprecipitation was used to detect the interaction between ANXA7 and PPAR𝛾. c) Immunoﬂuo- rescence was used to detect the colocalization of ANXA7 and PPAR𝛾, and the colocalization analysis was conducted. Scale bar: 10 μm. d,e) The protein level of PPAR𝛾was detected by WB after treatment SEC or ABO for 1 h. f,g) Neurons were treated with SEC or ABO for 1 h before OGD/R, and im- munoﬂuorescence was used to detect the nuclear level of PPAR𝛾. Scale bar: 10 μm. h,i) Nuclear expression of PPAR𝛾was detected by WB. The data were presented as mean ± SD, and ANOVA was used for analysis. **p < 0.01, ***p < 0.001, n = 3.

Techniques: Immunoprecipitation, Expressing

Figure 4. Expression changes of PPAR𝛾after spinal cord injury and its regulatory eﬀect on NRF2. a,b) The mouse model of spinal cord injury was constructed. The spinal cord tissue was extracted and the protein level of PPAR𝛾was detected by WB on diﬀerent time point after spinal cord injury. c) The mouse model of spinal cord injury was constructed, and qPCR was used to detect the mRNA level changes of Ppar𝛾on diﬀerent time point after spinal cord injury. d) Neurons were treated with rosiglitazone and ABO separately or in combination for 1 h, and LPO levels of the neurons were detected after OGD/R treatment. e) Neurons were treated with rosiglitazone and ABO separately or in combination for 1 h, and the survival ratio of neurons was detected by CCK8 after OGD/R. f,g) Rosiglitazone and ABO were used to treat neurons separately or in combination for 1 h, and immunoﬂuorescence was conducted to detect nuclear translocation level of NRF2 after OGD/R. Scale bar: 10 μm. h–j) Neurons were treated with diﬀerent concentrations of rosiglitazone and GW9662 for 1 h, respectively. After the OGD/R model was constructed, the protein levels of ANXA7 and NRF2 were detected by WB. The data were presented as mean ± SD, and ANOVA was used for analysis. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Lipid Droplets Metabolism Mediated by ANXA7-PPARγ Signaling Axis Regulates Spinal Cord Injury Repair in Mice.

doi: 10.1002/advs.202417326

Figure Lengend Snippet: Figure 4. Expression changes of PPAR𝛾after spinal cord injury and its regulatory eﬀect on NRF2. a,b) The mouse model of spinal cord injury was constructed. The spinal cord tissue was extracted and the protein level of PPAR𝛾was detected by WB on diﬀerent time point after spinal cord injury. c) The mouse model of spinal cord injury was constructed, and qPCR was used to detect the mRNA level changes of Ppar𝛾on diﬀerent time point after spinal cord injury. d) Neurons were treated with rosiglitazone and ABO separately or in combination for 1 h, and LPO levels of the neurons were detected after OGD/R treatment. e) Neurons were treated with rosiglitazone and ABO separately or in combination for 1 h, and the survival ratio of neurons was detected by CCK8 after OGD/R. f,g) Rosiglitazone and ABO were used to treat neurons separately or in combination for 1 h, and immunoﬂuorescence was conducted to detect nuclear translocation level of NRF2 after OGD/R. Scale bar: 10 μm. h–j) Neurons were treated with diﬀerent concentrations of rosiglitazone and GW9662 for 1 h, respectively. After the OGD/R model was constructed, the protein levels of ANXA7 and NRF2 were detected by WB. The data were presented as mean ± SD, and ANOVA was used for analysis. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Techniques: Expressing, Construct, Translocation Assay

Figure 5. Regulation of ANXA7 to PPAR𝛾and the eﬀect of PPAR𝛾on spinal cord injury repair. a,b) OGD/R model of neurons was constructed after transfected with GV657-negative control or GV657-OE-ANXA7 plasmids. Then the protein expression of PPAR𝛾and LPO content were detected by immunoﬂuorescence and LPO assay kit. Scale bar: 10 μm. c–e) The spinal cord injury mouse model was established. After 4 days, the spinal cord tissue was extracted and PPAR𝛾was detected by WB and qPCR in diﬀerent treatment groups. f,g) After transfected with ANXA7 overexpression lentivirus, neurons were treated with/without SEC or ABO for 1 h before OGD/R treatment, and protein level of PPAR𝛾was detected by WB. h,i) After transfected with ANXA7 overexpression lentivirus, neurons were treated with/without GW9662 for 1 h before OGD/R treatment, and lipid droplet levels were

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Lipid Droplets Metabolism Mediated by ANXA7-PPARγ Signaling Axis Regulates Spinal Cord Injury Repair in Mice.

doi: 10.1002/advs.202417326

Figure Lengend Snippet: Figure 5. Regulation of ANXA7 to PPAR𝛾and the eﬀect of PPAR𝛾on spinal cord injury repair. a,b) OGD/R model of neurons was constructed after transfected with GV657-negative control or GV657-OE-ANXA7 plasmids. Then the protein expression of PPAR𝛾and LPO content were detected by immunoﬂuorescence and LPO assay kit. Scale bar: 10 μm. c–e) The spinal cord injury mouse model was established. After 4 days, the spinal cord tissue was extracted and PPAR𝛾was detected by WB and qPCR in diﬀerent treatment groups. f,g) After transfected with ANXA7 overexpression lentivirus, neurons were treated with/without SEC or ABO for 1 h before OGD/R treatment, and protein level of PPAR𝛾was detected by WB. h,i) After transfected with ANXA7 overexpression lentivirus, neurons were treated with/without GW9662 for 1 h before OGD/R treatment, and lipid droplet levels were

Techniques: Construct, Transfection, Negative Control, Expressing, Over Expression

Figure 6. Eﬀect of PPAR𝛾on LDs formation and oxidative stress. a–c) Neutral lipid staining in primary neurons treated with negative control and sh- ANXA7 lentivirus, and statistical analysis of neutral lipid level and LDs number was performed. Scale bar: 10 μm. d) Primary neurons were treated with negative control or shANXA7 lentivirus, with/without rosiglitazone for 1 h, and lipid peroxidation levels were detected. e–g) The OGD/R model was constructed after primary neurons transfected with negative control or shANXA7 lentivirus were treated with/without GW9662 for 1 h, and nuclear level of PPAR𝛾and NRF2 were detected. h,i) Lipid peroxidation and mitochondrial ATP production were detected by LPO and ATP kits after 1 h of treatment with rosiglitazone and/or Beauveriolide III, respectively. j,k) Western Blot detection of GPX4 protein levels in neurons treated with Rosiglitazone and/or Beauveriolide III for 1 h before OGD/R treatment. l,m) Neurons were treated with rosiglitazone or Beauveriolide III and in combination with rosiglitazone and Beauveriolide III for 1 h, and then OGD/R model was constructed. ROS probe DCFH-DA was used to detect ROS level. Scale bar: 20 μm. The data were presented as mean ± SD, and Student’s T-test was used for analysis between two groups, while ANOVA was used among more than two groups. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Lipid Droplets Metabolism Mediated by ANXA7-PPARγ Signaling Axis Regulates Spinal Cord Injury Repair in Mice.

doi: 10.1002/advs.202417326

Figure Lengend Snippet: Figure 6. Eﬀect of PPAR𝛾on LDs formation and oxidative stress. a–c) Neutral lipid staining in primary neurons treated with negative control and sh- ANXA7 lentivirus, and statistical analysis of neutral lipid level and LDs number was performed. Scale bar: 10 μm. d) Primary neurons were treated with negative control or shANXA7 lentivirus, with/without rosiglitazone for 1 h, and lipid peroxidation levels were detected. e–g) The OGD/R model was constructed after primary neurons transfected with negative control or shANXA7 lentivirus were treated with/without GW9662 for 1 h, and nuclear level of PPAR𝛾and NRF2 were detected. h,i) Lipid peroxidation and mitochondrial ATP production were detected by LPO and ATP kits after 1 h of treatment with rosiglitazone and/or Beauveriolide III, respectively. j,k) Western Blot detection of GPX4 protein levels in neurons treated with Rosiglitazone and/or Beauveriolide III for 1 h before OGD/R treatment. l,m) Neurons were treated with rosiglitazone or Beauveriolide III and in combination with rosiglitazone and Beauveriolide III for 1 h, and then OGD/R model was constructed. ROS probe DCFH-DA was used to detect ROS level. Scale bar: 20 μm. The data were presented as mean ± SD, and Student’s T-test was used for analysis between two groups, while ANOVA was used among more than two groups. *p < 0.05, **p < 0.01, ***p < 0.001, n = 3.

Techniques: Staining, Negative Control, Construct, Transfection, Western Blot

Figure 7. ANXA7-PPAR𝛾regulates LDs formation by aﬀecting PLIN5 expression. a,b) OGD/R model was constructed after SEC treated neurons for 1 h, and the SEC pretreatment group was treated with Beauveriolide III during reoxygenation processing. Mitochondrial ATP probe pCMV-Mito-AT1.03 and ATP test kit were used to detect the level of ATP in neurons. Scale bar:10 μm. c–f) After treatment by SEC with/without GW9662 for 1 h, OGD/R model was constructed, and the levels of PLIN1, PLIN2, and PLIN5 were detected by WB. g) Neurons were treated with rosiglitazone, GW9662, or combination with SEC and GW9662, and OGD/R treatment was conducted. The immunoﬂuorescence was used to detect the expression of PLIN2 and PLIN5. Scale

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Lipid Droplets Metabolism Mediated by ANXA7-PPARγ Signaling Axis Regulates Spinal Cord Injury Repair in Mice.

doi: 10.1002/advs.202417326

Figure Lengend Snippet: Figure 7. ANXA7-PPAR𝛾regulates LDs formation by aﬀecting PLIN5 expression. a,b) OGD/R model was constructed after SEC treated neurons for 1 h, and the SEC pretreatment group was treated with Beauveriolide III during reoxygenation processing. Mitochondrial ATP probe pCMV-Mito-AT1.03 and ATP test kit were used to detect the level of ATP in neurons. Scale bar:10 μm. c–f) After treatment by SEC with/without GW9662 for 1 h, OGD/R model was constructed, and the levels of PLIN1, PLIN2, and PLIN5 were detected by WB. g) Neurons were treated with rosiglitazone, GW9662, or combination with SEC and GW9662, and OGD/R treatment was conducted. The immunoﬂuorescence was used to detect the expression of PLIN2 and PLIN5. Scale

Techniques: Expressing, Construct

Journal: Frontiers in Cell and Developmental Biology

Article Title: RNA-binding is an ancient trait of the Annexin family

doi: 10.3389/fcell.2023.1161588

Figure Lengend Snippet: Sequence of primers and identity of sequenced clones of rat anx cDNAs. The colored boxes represent recognition sites for restriction enzymes. Yellow, blue, green and red colors highlight the Nco I, Acc 65I, Not I and Bsa I sites, respectively. Letters in bold represent NcoI compatible sites.

Article Snippet: The membranes were probed against AnxA1 (HPA011272, Sigma-Aldrich, Saint-Louis, United States; 1:1,000), AnxA2 (610069; BD Biosciences, Franklin Lakes, United States; 1:1,000), AnxA4 (PA5-82296, Invitrogen, Thermo Fisher Scientific, Waltham, United States; 1:1,000), AnxA5 (MA5-35789, Invitrogen, Thermo Fisher Scientific, Waltham, United States; 1:1,000), AnxA6 (NBP1-90149, Novus Biologicals LTD., Bristol, UK; 1:1,000), AnxA7 (sc-17815, Santa Cruz Biotechnology, Dallas, United States; 1:1,000), AnxA10 (ab213656, Abcam, Cambridge, UK; 1:1,000), AnxA11 (sc-9322, Santa Cruz Biotechnology, Dallas, United States; 1:1,000), AnxA13 (PA5-109395, Invitrogen, Thermo Fisher Scientific, Waltham, United States; 1:1,000)), Rab7 (R4779, Sigma/Merck,; 1:1,000), Rab11 (610657, BD Transduction Lab/Thermo Fisher Scientific, Waltham, United States; 1:1,000), EEA1 (610457, BD Transduction Lab/Thermo Fisher Scientific, Waltham, United States; 1:1,000), S6 (710405; Thermo Fisher Scientific; Waltham, United States; 1:1,000), and PABP1 (4992S; Cell Signaling Technology, Danvers, United States; 1:1,000) primary antibodies.

Techniques: Sequencing, Clone Assay

Journal: Frontiers in Cell and Developmental Biology

Article Title: RNA-binding is an ancient trait of the Annexin family

doi: 10.3389/fcell.2023.1161588

Figure Lengend Snippet: AnxA1, AnxA2, AnxA4, AnxA5, AnxA6, AnxA7, AnxA10, AnxA11 and AnxA13 present in the cytoskeleton fraction (Panel A) are associated with non-polysomal mRNP complexes (Panel B) of PC12 cells. Panel (A) 30 µg of the cytoskeletal fraction (lane 1) and cytoskeleton-bound polysomes (lane 2) were separated by 10% SDS-PAGE and transferred to nitrocellulose membranes. Panel (B) samples prepared from oligo (dT)-bound mRNP complexes from the cytoskeletal fraction [supernatant after centrifugation for 2 h 100,000 g above a 1 M (35%) sucrose cushion] (lanes 3 and 4), without (lane 3) or with RNase (lane 4) treatment, as indicated above the Western blots, were subjected to similar analysis. The blots were probed with antibodies against the different Anxs and against PABP1 as a marker for poly(A)-containing mRNAs, as indicated. Antibodies against the ribosomal subunit S6 were used to inform of the distribution of ribosomes. In addition, the blots were probed with antibodies against early endosomes (EEA1), late endosomes (Rab7) and recycling endosomes (Rab11). SPC25 and LAMP1 were not detectable in any of the fractions (results not shown). Visualization of the immunoreactive protein bands was performed using the ChemiDocTM XRS+ molecular imager after incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies and enhanced chemiluminescence (ECL)-reagent. The blots shown are representative for results from three experiments.

Techniques: SDS Page, Centrifugation, Western Blot, Marker, Incubation

Journal: Frontiers in Cell and Developmental Biology

Article Title: RNA-binding is an ancient trait of the Annexin family

doi: 10.3389/fcell.2023.1161588

Figure Lengend Snippet: An overview of the binding of rat Anxs to the different RNA probes as determined by spot blot and UV crosslinking (xlinking) experiments. xxx indicates strong binding and X indicates weak RNA binding with XX indicating intermediate binding. Also the presence of Anxs in mRNP complexes derived from PC12 cells detected with specific antibodies are indicated.

Techniques: Binding Assay, RNA Binding Assay, Derivative Assay

Journal: Frontiers in Cell and Developmental Biology

Article Title: RNA-binding is an ancient trait of the Annexin family

doi: 10.3389/fcell.2023.1161588

Figure Lengend Snippet: UV-crosslinking competition experiments employing rat Anxs and radiolabeled [α 32 P]-rUTP c-myc or anxA2 3′UTRs. 2 μM purified rat Anxs (except 0.4 µM of AnxA7; 0.3 µM of AnxA9 and 0.5 µM of AnxA11) were UV-crosslinked in the absence of RNA (lanes 1 and 5). 100,000 cpm of radiolabeled anxA2 3′UTR (7 fmoles) or c-myc 3′UTR (6 fmoles) were UV-crosslinked to purified rat Anxs in the absence (lanes 2 and 6) or presence of 25x (lanes 3 and 7), or 50x (lanes 4 and 8) molar excess of the corresponding unlabeled transcript. 2 μM BSA and mutant AnxA2 served as negative controls. After UV-crosslinking and RNase treatment, the samples were subjected to 4%–15% SDS-PAGE and the proteins were stained with Coomassie Brilliant Blue (lanes 1–4), whereafter the gels were dried. The [α 32 P]-rUTP-labeled RNA covalently bound to the respective Anxs, as indicated, was visualized using screens and phosphor-imaging following an overnight (c-myc 3′UTR) or 6 h (anxA2 3′UTR) exposure (lanes 5–8). PageRuler prestained protein ladder (from top to bottom: 100 kDa, 70 kDa (the most prominent band), 55 kDa, 40 kDa, 35 kDa and 25 kDa) are shown to the left of the AnxA1, AnxA3, AnxA5, AnxA7, AnxA8, AnxA10, Δ188AnxA11 and BSA samples. The representative images are from two experiments performed with competition while RNA-Anx binding was performed four times without competition.

Techniques: Purification, Mutagenesis, SDS Page, Staining, Labeling, Imaging, Binding Assay

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anxa7 (Santa Cruz Biotechnology)

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