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primary antibodies against hscd1  (Alpha Diagnostics)

 
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    Alpha Diagnostics primary antibodies against hscd1
    Preconfluent myoblasts were transiently transfected with <t>pcDNA3.0-hSCD1</t> or the empty parent vector. After 7 days in DFM, cells were harvested to obtain total RNA. Overexpression of SCD1 was confirmed in differentiated myotubes by (A) semiquantitative PCR of mRNA and (B) Western blot analysis of protein. β-actin mRNA and GAPDH protein were used as loading controls. Metabolic assays were performed following a 3 hr incubation with 100 μM [14C]oleate and 0.25% BSA. (C) Fatty acid oxidation was determined by measuring 14C-label incorporation into CO2. (D) Glycerolipid synthesis was determined by measuring 14C-label incorporation into triacylglycerol (TAG) and phospholipid (PL). All assays were performed in triplicate and values represent the mean ± SEM from four separate experiments. Differences between groups were analyzed by Student’s t test, *p < 0.05, **p < 0.01. (E) ACCβ mRNA levels were quantified by RTQ-PCR and are expressed as relative units in cells transfected with SCD1 versus empty vector controls. Cyclophilin B was measured as an endogenous control. Data are representative of five experiments and differences between groups were analyzed by Student’s t test, *p < 0.05. (F) Total and phosphorylated AMPK and ACCβ were analyzed by immunoblotting with antibodies against the AMPKα 1 and 2 catalytic subunits, ACCβ, AMPK-thr172, and ACCβ-ser79. GAPDH protein expression was not different between groups.
    Primary Antibodies Against Hscd1, supplied by Alpha Diagnostics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary antibodies against hscd1/product/Alpha Diagnostics
    Average 90 stars, based on 1 article reviews
    primary antibodies against hscd1 - by Bioz Stars, 2026-03
    90/100 stars

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    1) Product Images from "Elevated stearoyl-CoA desaturase-1 expression in skeletal muscle contributes to abnormal fatty acid partitioning in obese humans"

    Article Title: Elevated stearoyl-CoA desaturase-1 expression in skeletal muscle contributes to abnormal fatty acid partitioning in obese humans

    Journal: Cell metabolism

    doi: 10.1016/j.cmet.2005.09.002

    Preconfluent myoblasts were transiently transfected with pcDNA3.0-hSCD1 or the empty parent vector. After 7 days in DFM, cells were harvested to obtain total RNA. Overexpression of SCD1 was confirmed in differentiated myotubes by (A) semiquantitative PCR of mRNA and (B) Western blot analysis of protein. β-actin mRNA and GAPDH protein were used as loading controls. Metabolic assays were performed following a 3 hr incubation with 100 μM [14C]oleate and 0.25% BSA. (C) Fatty acid oxidation was determined by measuring 14C-label incorporation into CO2. (D) Glycerolipid synthesis was determined by measuring 14C-label incorporation into triacylglycerol (TAG) and phospholipid (PL). All assays were performed in triplicate and values represent the mean ± SEM from four separate experiments. Differences between groups were analyzed by Student’s t test, *p < 0.05, **p < 0.01. (E) ACCβ mRNA levels were quantified by RTQ-PCR and are expressed as relative units in cells transfected with SCD1 versus empty vector controls. Cyclophilin B was measured as an endogenous control. Data are representative of five experiments and differences between groups were analyzed by Student’s t test, *p < 0.05. (F) Total and phosphorylated AMPK and ACCβ were analyzed by immunoblotting with antibodies against the AMPKα 1 and 2 catalytic subunits, ACCβ, AMPK-thr172, and ACCβ-ser79. GAPDH protein expression was not different between groups.
    Figure Legend Snippet: Preconfluent myoblasts were transiently transfected with pcDNA3.0-hSCD1 or the empty parent vector. After 7 days in DFM, cells were harvested to obtain total RNA. Overexpression of SCD1 was confirmed in differentiated myotubes by (A) semiquantitative PCR of mRNA and (B) Western blot analysis of protein. β-actin mRNA and GAPDH protein were used as loading controls. Metabolic assays were performed following a 3 hr incubation with 100 μM [14C]oleate and 0.25% BSA. (C) Fatty acid oxidation was determined by measuring 14C-label incorporation into CO2. (D) Glycerolipid synthesis was determined by measuring 14C-label incorporation into triacylglycerol (TAG) and phospholipid (PL). All assays were performed in triplicate and values represent the mean ± SEM from four separate experiments. Differences between groups were analyzed by Student’s t test, *p < 0.05, **p < 0.01. (E) ACCβ mRNA levels were quantified by RTQ-PCR and are expressed as relative units in cells transfected with SCD1 versus empty vector controls. Cyclophilin B was measured as an endogenous control. Data are representative of five experiments and differences between groups were analyzed by Student’s t test, *p < 0.05. (F) Total and phosphorylated AMPK and ACCβ were analyzed by immunoblotting with antibodies against the AMPKα 1 and 2 catalytic subunits, ACCβ, AMPK-thr172, and ACCβ-ser79. GAPDH protein expression was not different between groups.

    Techniques Used: Transfection, Plasmid Preparation, Over Expression, Western Blot, Incubation, Control, Expressing



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    primary antibodies against hscd1  (Alpha Diagnostics)
    90
    Alpha Diagnostics primary antibodies against hscd1
    Preconfluent myoblasts were transiently transfected with <t>pcDNA3.0-hSCD1</t> or the empty parent vector. After 7 days in DFM, cells were harvested to obtain total RNA. Overexpression of SCD1 was confirmed in differentiated myotubes by (A) semiquantitative PCR of mRNA and (B) Western blot analysis of protein. β-actin mRNA and GAPDH protein were used as loading controls. Metabolic assays were performed following a 3 hr incubation with 100 μM [14C]oleate and 0.25% BSA. (C) Fatty acid oxidation was determined by measuring 14C-label incorporation into CO2. (D) Glycerolipid synthesis was determined by measuring 14C-label incorporation into triacylglycerol (TAG) and phospholipid (PL). All assays were performed in triplicate and values represent the mean ± SEM from four separate experiments. Differences between groups were analyzed by Student’s t test, *p < 0.05, **p < 0.01. (E) ACCβ mRNA levels were quantified by RTQ-PCR and are expressed as relative units in cells transfected with SCD1 versus empty vector controls. Cyclophilin B was measured as an endogenous control. Data are representative of five experiments and differences between groups were analyzed by Student’s t test, *p < 0.05. (F) Total and phosphorylated AMPK and ACCβ were analyzed by immunoblotting with antibodies against the AMPKα 1 and 2 catalytic subunits, ACCβ, AMPK-thr172, and ACCβ-ser79. GAPDH protein expression was not different between groups.
    Primary Antibodies Against Hscd1, supplied by Alpha Diagnostics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary antibodies against hscd1/product/Alpha Diagnostics
    Average 90 stars, based on 1 article reviews
    primary antibodies against hscd1 - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

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    Preconfluent myoblasts were transiently transfected with pcDNA3.0-hSCD1 or the empty parent vector. After 7 days in DFM, cells were harvested to obtain total RNA. Overexpression of SCD1 was confirmed in differentiated myotubes by (A) semiquantitative PCR of mRNA and (B) Western blot analysis of protein. β-actin mRNA and GAPDH protein were used as loading controls. Metabolic assays were performed following a 3 hr incubation with 100 μM [14C]oleate and 0.25% BSA. (C) Fatty acid oxidation was determined by measuring 14C-label incorporation into CO2. (D) Glycerolipid synthesis was determined by measuring 14C-label incorporation into triacylglycerol (TAG) and phospholipid (PL). All assays were performed in triplicate and values represent the mean ± SEM from four separate experiments. Differences between groups were analyzed by Student’s t test, *p < 0.05, **p < 0.01. (E) ACCβ mRNA levels were quantified by RTQ-PCR and are expressed as relative units in cells transfected with SCD1 versus empty vector controls. Cyclophilin B was measured as an endogenous control. Data are representative of five experiments and differences between groups were analyzed by Student’s t test, *p < 0.05. (F) Total and phosphorylated AMPK and ACCβ were analyzed by immunoblotting with antibodies against the AMPKα 1 and 2 catalytic subunits, ACCβ, AMPK-thr172, and ACCβ-ser79. GAPDH protein expression was not different between groups.

    Journal: Cell metabolism

    Article Title: Elevated stearoyl-CoA desaturase-1 expression in skeletal muscle contributes to abnormal fatty acid partitioning in obese humans

    doi: 10.1016/j.cmet.2005.09.002

    Figure Lengend Snippet: Preconfluent myoblasts were transiently transfected with pcDNA3.0-hSCD1 or the empty parent vector. After 7 days in DFM, cells were harvested to obtain total RNA. Overexpression of SCD1 was confirmed in differentiated myotubes by (A) semiquantitative PCR of mRNA and (B) Western blot analysis of protein. β-actin mRNA and GAPDH protein were used as loading controls. Metabolic assays were performed following a 3 hr incubation with 100 μM [14C]oleate and 0.25% BSA. (C) Fatty acid oxidation was determined by measuring 14C-label incorporation into CO2. (D) Glycerolipid synthesis was determined by measuring 14C-label incorporation into triacylglycerol (TAG) and phospholipid (PL). All assays were performed in triplicate and values represent the mean ± SEM from four separate experiments. Differences between groups were analyzed by Student’s t test, *p < 0.05, **p < 0.01. (E) ACCβ mRNA levels were quantified by RTQ-PCR and are expressed as relative units in cells transfected with SCD1 versus empty vector controls. Cyclophilin B was measured as an endogenous control. Data are representative of five experiments and differences between groups were analyzed by Student’s t test, *p < 0.05. (F) Total and phosphorylated AMPK and ACCβ were analyzed by immunoblotting with antibodies against the AMPKα 1 and 2 catalytic subunits, ACCβ, AMPK-thr172, and ACCβ-ser79. GAPDH protein expression was not different between groups.

    Article Snippet: Blots were probed with primary antibodies against hSCD1 (4 μg/mL, Alpha Diagnostics International, San Anto-nio, TX) and GAPDH (1:100 dilution, Santa Cruz Biotechnology, Santa Cruz, CA) followed by anti-rabbit and anti-goat secondary antibodies respectively (1:8000 and 1:10000 dilutions, respectively; Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques: Transfection, Plasmid Preparation, Over Expression, Western Blot, Incubation, Control, Expressing