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$Figure 3. AGO2 is degraded through chaperone-mediated autophagy pathway. Stromal vascular fraction isolated from WT mice were differentiated into adipocytes and used for the following experiments. (A-B) immunoblotting analysis of AGO2 expression in the cells treated with 10 µM lactacystin for indicated time. (C-D) cells were treated with NH4Cl combined with leupeptin for indicated time, and AGO2 level was measured. (E-G) cells were transfected with control siRNA (siCtrl) or cathepsin B siRNA (siCtsb) or cathepsin D siRNA (siCtsd), and AGO2 level was analyzed. (H-I) immunoblotting analysis of AGO2 expression in the cells transfected with control siRNA (siCtrl) or Ulk1 siRNA (siUlk1). (J-K) cells were treated with 6-AN or starvation for indicated time, and AGO2 level was measured. (L-N) cells were transfected with control siRNA (siCtrl) or Hspa8 siRNA (siHspa8) or <t>Lamp2</t> siRNA (siLamp2), and AGO2 expression was analyzed. (O) interaction of AGO2 and HSPA8 in adipose tissue were detected by immunoprecipitation and immunoblotting analysis. (P) co-staining of AGO2 and lysosomal HSPA8 in abdominal adipose tissue. Red: AGO2; green: HSPA8; blue: DAPI. (Q) the interaction of AGO2 and LAMP2 in adipose tissue was detected by immunoprecipitation and immunoblotting analysis. (R) co-staining of AGO2 and LAMP2 in abdominal adipose tissue. Red: AGO2; green: LAMP2; blue: DAPI. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, and n. S. non-significant, derived from Student’s t tests.$
Lamp2 Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 35 article reviews

lamp2 sirna - by Bioz Stars, 2026-03

94/100 stars

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1) Product Images from "Pycard deficiency inhibits microRNA maturation and prevents neointima formation by promoting chaperone-mediated autophagic degradation of AGO2/argonaute 2 in adipose tissue."

Article Title: Pycard deficiency inhibits microRNA maturation and prevents neointima formation by promoting chaperone-mediated autophagic degradation of AGO2/argonaute 2 in adipose tissue.

Journal: Autophagy

doi: 10.1080/15548627.2023.2277610

$Figure 3. AGO2 is degraded through chaperone-mediated autophagy pathway. Stromal vascular fraction isolated from WT mice were differentiated into adipocytes and used for the following experiments. (A-B) immunoblotting analysis of AGO2 expression in the cells treated with 10 µM lactacystin for indicated time. (C-D) cells were treated with NH4Cl combined with leupeptin for indicated time, and AGO2 level was measured. (E-G) cells were transfected with control siRNA (siCtrl) or cathepsin B siRNA (siCtsb) or cathepsin D siRNA (siCtsd), and AGO2 level was analyzed. (H-I) immunoblotting analysis of AGO2 expression in the cells transfected with control siRNA (siCtrl) or Ulk1 siRNA (siUlk1). (J-K) cells were treated with 6-AN or starvation for indicated time, and AGO2 level was measured. (L-N) cells were transfected with control siRNA (siCtrl) or Hspa8 siRNA (siHspa8) or Lamp2 siRNA (siLamp2), and AGO2 expression was analyzed. (O) interaction of AGO2 and HSPA8 in adipose tissue were detected by immunoprecipitation and immunoblotting analysis. (P) co-staining of AGO2 and lysosomal HSPA8 in abdominal adipose tissue. Red: AGO2; green: HSPA8; blue: DAPI. (Q) the interaction of AGO2 and LAMP2 in adipose tissue was detected by immunoprecipitation and immunoblotting analysis. (R) co-staining of AGO2 and LAMP2 in abdominal adipose tissue. Red: AGO2; green: LAMP2; blue: DAPI. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, and n. S. non-significant, derived from Student’s t tests.$
Figure Legend Snippet: Figure 3. AGO2 is degraded through chaperone-mediated autophagy pathway. Stromal vascular fraction isolated from WT mice were differentiated into adipocytes and used for the following experiments. (A-B) immunoblotting analysis of AGO2 expression in the cells treated with 10 µM lactacystin for indicated time. (C-D) cells were treated with NH4Cl combined with leupeptin for indicated time, and AGO2 level was measured. (E-G) cells were transfected with control siRNA (siCtrl) or cathepsin B siRNA (siCtsb) or cathepsin D siRNA (siCtsd), and AGO2 level was analyzed. (H-I) immunoblotting analysis of AGO2 expression in the cells transfected with control siRNA (siCtrl) or Ulk1 siRNA (siUlk1). (J-K) cells were treated with 6-AN or starvation for indicated time, and AGO2 level was measured. (L-N) cells were transfected with control siRNA (siCtrl) or Hspa8 siRNA (siHspa8) or Lamp2 siRNA (siLamp2), and AGO2 expression was analyzed. (O) interaction of AGO2 and HSPA8 in adipose tissue were detected by immunoprecipitation and immunoblotting analysis. (P) co-staining of AGO2 and lysosomal HSPA8 in abdominal adipose tissue. Red: AGO2; green: HSPA8; blue: DAPI. (Q) the interaction of AGO2 and LAMP2 in adipose tissue was detected by immunoprecipitation and immunoblotting analysis. (R) co-staining of AGO2 and LAMP2 in abdominal adipose tissue. Red: AGO2; green: LAMP2; blue: DAPI. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, and n. S. non-significant, derived from Student’s t tests.

Techniques Used: Isolation, Western Blot, Expressing, Transfection, Control, Immunoprecipitation, Staining, Derivative Assay

$Figure 4. Pycard deficiency promotes CMA-mediated AGO2 degradation in adipocytes. Stromal vascular fraction isolated from WT and pycard−/− mice were differentiated into adipocytes and used for the following experiments. (A-B) cells were treated with NH4Cl (N) combined with leupeptin (L) for 24 h. AGO2 level was detected by immunoblotting analysis. The ratio of N/L to veh treatment after normalization by endogenous control. (C-D) cells were transfected with control siRNA (siCtrl) or Hspa8 siRNA (siHspa8), AGO2 protein level was measured by immunoblotting analysis. (E-F) cells were transfected with control siRNA (siCtrl) or Lamp2 siRNA (siLamp2), and western blot was performed to measure AGO2 protein expression. (G-H) cells were transfected with control siRNA (siCtrl) or Ulk1 siRNA (siUlk1), andAGO2 protein expression was analyzed by immunoblotting analysis. (I) the interaction of AGO2 and HSPA8 in differentiated adipocytes was determined by immunoprecipitation and immunoblotting analysis. (J) the interaction of AGO2 and LAMP2 was analyzed in differentiated adipocytes. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, and n.S. non-significant, derived from Student’s t tests.$
Figure Legend Snippet: Figure 4. Pycard deficiency promotes CMA-mediated AGO2 degradation in adipocytes. Stromal vascular fraction isolated from WT and pycard−/− mice were differentiated into adipocytes and used for the following experiments. (A-B) cells were treated with NH4Cl (N) combined with leupeptin (L) for 24 h. AGO2 level was detected by immunoblotting analysis. The ratio of N/L to veh treatment after normalization by endogenous control. (C-D) cells were transfected with control siRNA (siCtrl) or Hspa8 siRNA (siHspa8), AGO2 protein level was measured by immunoblotting analysis. (E-F) cells were transfected with control siRNA (siCtrl) or Lamp2 siRNA (siLamp2), and western blot was performed to measure AGO2 protein expression. (G-H) cells were transfected with control siRNA (siCtrl) or Ulk1 siRNA (siUlk1), andAGO2 protein expression was analyzed by immunoblotting analysis. (I) the interaction of AGO2 and HSPA8 in differentiated adipocytes was determined by immunoprecipitation and immunoblotting analysis. (J) the interaction of AGO2 and LAMP2 was analyzed in differentiated adipocytes. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, and n.S. non-significant, derived from Student’s t tests.

Techniques Used: Isolation, Western Blot, Control, Transfection, Expressing, Immunoprecipitation, Derivative Assay

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Journal: Autophagy

Article Title: Pycard deficiency inhibits microRNA maturation and prevents neointima formation by promoting chaperone-mediated autophagic degradation of AGO2/argonaute 2 in adipose tissue.

doi: 10.1080/15548627.2023.2277610

Figure Lengend Snippet: Figure 3. AGO2 is degraded through chaperone-mediated autophagy pathway. Stromal vascular fraction isolated from WT mice were differentiated into adipocytes and used for the following experiments. (A-B) immunoblotting analysis of AGO2 expression in the cells treated with 10 µM lactacystin for indicated time. (C-D) cells were treated with NH4Cl combined with leupeptin for indicated time, and AGO2 level was measured. (E-G) cells were transfected with control siRNA (siCtrl) or cathepsin B siRNA (siCtsb) or cathepsin D siRNA (siCtsd), and AGO2 level was analyzed. (H-I) immunoblotting analysis of AGO2 expression in the cells transfected with control siRNA (siCtrl) or Ulk1 siRNA (siUlk1). (J-K) cells were treated with 6-AN or starvation for indicated time, and AGO2 level was measured. (L-N) cells were transfected with control siRNA (siCtrl) or Hspa8 siRNA (siHspa8) or Lamp2 siRNA (siLamp2), and AGO2 expression was analyzed. (O) interaction of AGO2 and HSPA8 in adipose tissue were detected by immunoprecipitation and immunoblotting analysis. (P) co-staining of AGO2 and lysosomal HSPA8 in abdominal adipose tissue. Red: AGO2; green: HSPA8; blue: DAPI. (Q) the interaction of AGO2 and LAMP2 in adipose tissue was detected by immunoprecipitation and immunoblotting analysis. (R) co-staining of AGO2 and LAMP2 in abdominal adipose tissue. Red: AGO2; green: LAMP2; blue: DAPI. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, and n. S. non-significant, derived from Student’s t tests.

Article Snippet: For transfections of Cathepsin B siRNA (Santa Cruz Biotechnology, sc -29,933), Cathepsin D siRNA (Santa Cruz Biotechnology, sc -29,934), Hspa8 siRNA (Santa Cruz Biotechnology, sc -35,593), Lamp2 siRNA (Santa Cruz Biotechnology, sc -35,791), Ulk1 siRNA (Santa Cruz Biotechnology, sc -44,849), Prmt8 siRNA (Santa Cruz Biotechnology, sc -152,473), and Mir106b mimic in adipocytes, the cells that had been differentiated for 6 days were electroporated using SE Primary Cell 4D-Nucleofector X Kit (Lonza, V4XC– 1012) according to the manufacturer’s instructions.

Techniques: Isolation, Western Blot, Expressing, Transfection, Control, Immunoprecipitation, Staining, Derivative Assay

Journal: Autophagy

Article Title: Pycard deficiency inhibits microRNA maturation and prevents neointima formation by promoting chaperone-mediated autophagic degradation of AGO2/argonaute 2 in adipose tissue.

doi: 10.1080/15548627.2023.2277610

Figure Lengend Snippet: Figure 4. Pycard deficiency promotes CMA-mediated AGO2 degradation in adipocytes. Stromal vascular fraction isolated from WT and pycard−/− mice were differentiated into adipocytes and used for the following experiments. (A-B) cells were treated with NH4Cl (N) combined with leupeptin (L) for 24 h. AGO2 level was detected by immunoblotting analysis. The ratio of N/L to veh treatment after normalization by endogenous control. (C-D) cells were transfected with control siRNA (siCtrl) or Hspa8 siRNA (siHspa8), AGO2 protein level was measured by immunoblotting analysis. (E-F) cells were transfected with control siRNA (siCtrl) or Lamp2 siRNA (siLamp2), and western blot was performed to measure AGO2 protein expression. (G-H) cells were transfected with control siRNA (siCtrl) or Ulk1 siRNA (siUlk1), andAGO2 protein expression was analyzed by immunoblotting analysis. (I) the interaction of AGO2 and HSPA8 in differentiated adipocytes was determined by immunoprecipitation and immunoblotting analysis. (J) the interaction of AGO2 and LAMP2 was analyzed in differentiated adipocytes. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, and n.S. non-significant, derived from Student’s t tests.

Techniques: Isolation, Western Blot, Control, Transfection, Expressing, Immunoprecipitation, Derivative Assay