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primary antibodies against: lrp-1, rage, ir- β  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc primary antibodies against: lrp-1, rage, ir- β
    Primary Antibodies Against: Lrp 1, Rage, Ir β, supplied by Cell Signaling Technology Inc, 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: lrp-1, rage, ir- β/product/Cell Signaling Technology Inc
    Average 90 stars, based on 1 article reviews
    primary antibodies against: lrp-1, rage, ir- β - by Bioz Stars, 2026-03
    90/100 stars

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    Santa Cruz Biotechnology primary antibodies against ir β-subunit
    Abolished IR expression and insulin-stimulated signaling in NIRKO neurons. (A) Immunoblot analysis of IR expression on protein extracts from microdissected individual brain regions of control and NIRKO mice. (B) IR and IGF-1-IR expression in cultured neurons from control and NIRKO mice analyzed by Western blot. The blots were probed with a polyclonal antiserum specific for the <t>β-subunit</t> of the IGF-IR and the β-subunit IR. (C) Immunoblot analysis of insulin-stimulated tyrosine phosphorylation of the IR β-subunit (top blot) and of cellular proteins (second blot) on protein extracts from control and NIRKO mice. Insulin-stimulated activation of Akt and Erk by Western blot analysis using phospho-specific antibodies against Akt (Ser-473) and Erk (Tyr-204) from control and NIRKO hypothalami (third and fourth blots) also are shown. Insulin-stimulated IRS-1- and IRS-2-associated phosphatidylinositol 3-kinase activity from control and NIRKO hypothalami (fifth and sixth blots) was determined 15 min after i.v. injection of 5 milliunits of insulin. (D) Immunohistochemistry with anti-PIP3 (Upper) and anti-pSTAT3 (Lower) antibodies. Sections through the hypothalamus were prepared from control (Wild) or NIRKO mice that had been injected with vehicle alone, 5 milliunits of insulin, or 10 μg of leptin per g of body weight through the tail vein at 30 min before harvesting.
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    Key materials and software.

    Journal: Cell Discovery

    Article Title: A decrease in Flavonifractor plautii and its product, phytosphingosine, predisposes individuals with phlegm-dampness constitution to metabolic disorders

    doi: 10.1038/s41421-025-00789-x

    Figure Lengend Snippet: Key materials and software.

    Article Snippet: Primary antibody against p-IR-β , Cell Signaling Technology, Inc., Shanghai, China , #2381.

    Techniques: Software, Recombinant, Luciferase, Reporter Gene Assay, Plasmid Preparation, Control, Transfection, Enzyme-linked Immunosorbent Assay, Staining

    Primer sequences used in real-time PCR quantification of mRNA

    Journal: Journal of Ginseng Research

    Article Title: The non-saponin fraction of Korean Red Ginseng (KGC05P0) decreases glucose uptake and transport in vitro and modulates glucose production via down-regulation of the PI3K/AKT pathway in vivo

    doi: 10.1016/j.jgr.2019.12.004

    Figure Lengend Snippet: Primer sequences used in real-time PCR quantification of mRNA

    Article Snippet: After washing, the membranes were probed overnight at 4°C with primary antibodies against β-actin, IRS-1, P-IRS-1, AKT, phospho-AKT, PI3K, and phospho-PI3K (Cell Signaling Technology, 1:1000).

    Techniques: Real-time Polymerase Chain Reaction

    Effects of KGC05P0 on basal and insulin action on gluconeogenesis pathway-related mRNA levels in HepG2 cells

    Journal: Journal of Ginseng Research

    Article Title: The non-saponin fraction of Korean Red Ginseng (KGC05P0) decreases glucose uptake and transport in vitro and modulates glucose production via down-regulation of the PI3K/AKT pathway in vivo

    doi: 10.1016/j.jgr.2019.12.004

    Figure Lengend Snippet: Effects of KGC05P0 on basal and insulin action on gluconeogenesis pathway-related mRNA levels in HepG2 cells

    Article Snippet: After washing, the membranes were probed overnight at 4°C with primary antibodies against β-actin, IRS-1, P-IRS-1, AKT, phospho-AKT, PI3K, and phospho-PI3K (Cell Signaling Technology, 1:1000).

    Techniques:

    Effects of KGC05P0 on protein and mRNA expression in liver from C57BL/6J and C57BLKS/J db/db mice. (A) Protein expressions, (B) mRNA expression of IRS-1, (C) the ratio of phosphorylated/total PI3K protein expression, (D) the ratio of phosphorylated/total AKT protein expression, (E) FoxO1 mRNA expression, (F) G6Pase mRNA expression, (G) PEPCK mRNA expression, (H) GLUT2 mRNA expression, (I) glucokinase mRNA expression, (J) phosphofructokinase mRNA expression, and (K) acetyl-CoA carboxylase mRNA expressions. Values are presented as mean ± SD, and different alphabets indicate significance at P < 0.05. NC, normal control; C, control; PC, positive control (inulin, 400 mg/kg b.w.); L, low (KGC05P0 100 mg/kg b.w.); M, medium (KGC05P0 200 mg/kg b.w.); H, high (KGC05P0 400 mg/kg b.w.).

    Journal: Journal of Ginseng Research

    Article Title: The non-saponin fraction of Korean Red Ginseng (KGC05P0) decreases glucose uptake and transport in vitro and modulates glucose production via down-regulation of the PI3K/AKT pathway in vivo

    doi: 10.1016/j.jgr.2019.12.004

    Figure Lengend Snippet: Effects of KGC05P0 on protein and mRNA expression in liver from C57BL/6J and C57BLKS/J db/db mice. (A) Protein expressions, (B) mRNA expression of IRS-1, (C) the ratio of phosphorylated/total PI3K protein expression, (D) the ratio of phosphorylated/total AKT protein expression, (E) FoxO1 mRNA expression, (F) G6Pase mRNA expression, (G) PEPCK mRNA expression, (H) GLUT2 mRNA expression, (I) glucokinase mRNA expression, (J) phosphofructokinase mRNA expression, and (K) acetyl-CoA carboxylase mRNA expressions. Values are presented as mean ± SD, and different alphabets indicate significance at P < 0.05. NC, normal control; C, control; PC, positive control (inulin, 400 mg/kg b.w.); L, low (KGC05P0 100 mg/kg b.w.); M, medium (KGC05P0 200 mg/kg b.w.); H, high (KGC05P0 400 mg/kg b.w.).

    Article Snippet: After washing, the membranes were probed overnight at 4°C with primary antibodies against β-actin, IRS-1, P-IRS-1, AKT, phospho-AKT, PI3K, and phospho-PI3K (Cell Signaling Technology, 1:1000).

    Techniques: Expressing, Control, Positive Control

    Abolished IR expression and insulin-stimulated signaling in NIRKO neurons. (A) Immunoblot analysis of IR expression on protein extracts from microdissected individual brain regions of control and NIRKO mice. (B) IR and IGF-1-IR expression in cultured neurons from control and NIRKO mice analyzed by Western blot. The blots were probed with a polyclonal antiserum specific for the β-subunit of the IGF-IR and the β-subunit IR. (C) Immunoblot analysis of insulin-stimulated tyrosine phosphorylation of the IR β-subunit (top blot) and of cellular proteins (second blot) on protein extracts from control and NIRKO mice. Insulin-stimulated activation of Akt and Erk by Western blot analysis using phospho-specific antibodies against Akt (Ser-473) and Erk (Tyr-204) from control and NIRKO hypothalami (third and fourth blots) also are shown. Insulin-stimulated IRS-1- and IRS-2-associated phosphatidylinositol 3-kinase activity from control and NIRKO hypothalami (fifth and sixth blots) was determined 15 min after i.v. injection of 5 milliunits of insulin. (D) Immunohistochemistry with anti-PIP3 (Upper) and anti-pSTAT3 (Lower) antibodies. Sections through the hypothalamus were prepared from control (Wild) or NIRKO mice that had been injected with vehicle alone, 5 milliunits of insulin, or 10 μg of leptin per g of body weight through the tail vein at 30 min before harvesting.

    Journal:

    Article Title: Role for neuronal insulin resistance in neurodegenerative diseases

    doi: 10.1073/pnas.0308724101

    Figure Lengend Snippet: Abolished IR expression and insulin-stimulated signaling in NIRKO neurons. (A) Immunoblot analysis of IR expression on protein extracts from microdissected individual brain regions of control and NIRKO mice. (B) IR and IGF-1-IR expression in cultured neurons from control and NIRKO mice analyzed by Western blot. The blots were probed with a polyclonal antiserum specific for the β-subunit of the IGF-IR and the β-subunit IR. (C) Immunoblot analysis of insulin-stimulated tyrosine phosphorylation of the IR β-subunit (top blot) and of cellular proteins (second blot) on protein extracts from control and NIRKO mice. Insulin-stimulated activation of Akt and Erk by Western blot analysis using phospho-specific antibodies against Akt (Ser-473) and Erk (Tyr-204) from control and NIRKO hypothalami (third and fourth blots) also are shown. Insulin-stimulated IRS-1- and IRS-2-associated phosphatidylinositol 3-kinase activity from control and NIRKO hypothalami (fifth and sixth blots) was determined 15 min after i.v. injection of 5 milliunits of insulin. (D) Immunohistochemistry with anti-PIP3 (Upper) and anti-pSTAT3 (Lower) antibodies. Sections through the hypothalamus were prepared from control (Wild) or NIRKO mice that had been injected with vehicle alone, 5 milliunits of insulin, or 10 μg of leptin per g of body weight through the tail vein at 30 min before harvesting.

    Article Snippet: Primary antibodies against the IR β-subunit, insulin-like growth factor (IGF)-IR β-subunit, and Tau (Santa Cruz Biotechnology); Akt, pAkt, glycogen synthase kinase (GSK)3β, and pGSK3β (Upstate Biotechnology, Lake Placid, NY); and AT8 and AT180 (Innogenetic, Ghent, Belgium) were used.

    Techniques: Expressing, Western Blot, Cell Culture, Activation Assay, Activity Assay, Injection, Immunohistochemistry