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human rh leptin r fc chimera  (R&D Systems)


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    R&D Systems human rh leptin r fc chimera
    Fig. 2. Determination of the expression of human <t>leptin</t> receptor (OB-R) in human skeletal muscle. Protein extracts were prepared from muscle, SAT, and hypothalamus (HIP), and OB-R, perilipin A, and -tubulin protein expression was analyzed by Western blot. A: representative immunoblot assay after incubation with a polyclonal rabbit anti-OB-R antibody specifically raised against the long isoform. B: representative Western blot after incubation with a polyclonal rabbit anti-perilipin A antibody in the same samples used in A. C: representative immunoblot analysis after incubation with the monoclonal mouse anti--tubulin antibody in the same samples used in A. D: densitometric immunosignal values (arbitrary units of band densities) of OB-R bands relative to those obtained for -tubulin.
    Human Rh Leptin R Fc Chimera, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+rh+leptin+r+fc+chimera/pm17234799-41-2-31?v=R%26D+Systems
    Average 93 stars, based on 4 article reviews
    human rh leptin r fc chimera - by Bioz Stars, 2026-07
    93/100 stars

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    1) Product Images from "Leptin receptors in human skeletal muscle."

    Article Title: Leptin receptors in human skeletal muscle.

    Journal: Journal of applied physiology (Bethesda, Md. : 1985)

    doi: 10.1152/japplphysiol.01313.2006

    Fig. 2. Determination of the expression of human leptin receptor (OB-R) in human skeletal muscle. Protein extracts were prepared from muscle, SAT, and hypothalamus (HIP), and OB-R, perilipin A, and -tubulin protein expression was analyzed by Western blot. A: representative immunoblot assay after incubation with a polyclonal rabbit anti-OB-R antibody specifically raised against the long isoform. B: representative Western blot after incubation with a polyclonal rabbit anti-perilipin A antibody in the same samples used in A. C: representative immunoblot analysis after incubation with the monoclonal mouse anti--tubulin antibody in the same samples used in A. D: densitometric immunosignal values (arbitrary units of band densities) of OB-R bands relative to those obtained for -tubulin.
    Figure Legend Snippet: Fig. 2. Determination of the expression of human leptin receptor (OB-R) in human skeletal muscle. Protein extracts were prepared from muscle, SAT, and hypothalamus (HIP), and OB-R, perilipin A, and -tubulin protein expression was analyzed by Western blot. A: representative immunoblot assay after incubation with a polyclonal rabbit anti-OB-R antibody specifically raised against the long isoform. B: representative Western blot after incubation with a polyclonal rabbit anti-perilipin A antibody in the same samples used in A. C: representative immunoblot analysis after incubation with the monoclonal mouse anti--tubulin antibody in the same samples used in A. D: densitometric immunosignal values (arbitrary units of band densities) of OB-R bands relative to those obtained for -tubulin.

    Techniques Used: Expressing, Western Blot, Incubation

    Fig. 3. The anti-OB-R antibody recognized specifically the three OB-R bands detected in the muscle protein extracts. Increasing amounts of recombinant human (RH) leptin R/Fc (RH OB-R) chimera (0, 10, 100, 500 ng) were preincubated with anti-OB-R antibody (1:2,000). OB-R protein expression from muscle extracts was analyzed by immunoblotting using the preincubation solution. A: representative Western blot analysis with different preincubation solutions in the same muscle protein extract (50 g). B: representative immunoblot with the -tubulin antibody as a loading control. C: densitometric percentage of OB-R immnunostaining values (band quenching) in presence of increasing amounts (10, 100, 500 ng) of RH OB-R relative to those observed for a control (0 ng of RH OB-R). *P 0.01 vs. 0 ng of RH OB-R.
    Figure Legend Snippet: Fig. 3. The anti-OB-R antibody recognized specifically the three OB-R bands detected in the muscle protein extracts. Increasing amounts of recombinant human (RH) leptin R/Fc (RH OB-R) chimera (0, 10, 100, 500 ng) were preincubated with anti-OB-R antibody (1:2,000). OB-R protein expression from muscle extracts was analyzed by immunoblotting using the preincubation solution. A: representative Western blot analysis with different preincubation solutions in the same muscle protein extract (50 g). B: representative immunoblot with the -tubulin antibody as a loading control. C: densitometric percentage of OB-R immnunostaining values (band quenching) in presence of increasing amounts (10, 100, 500 ng) of RH OB-R relative to those observed for a control (0 ng of RH OB-R). *P 0.01 vs. 0 ng of RH OB-R.

    Techniques Used: Recombinant, Expressing, Western Blot, Control



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    human rh leptin r fc chimera  (R&D Systems)
    93
    R&D Systems human rh leptin r fc chimera
    Fig. 2. Determination of the expression of human <t>leptin</t> receptor (OB-R) in human skeletal muscle. Protein extracts were prepared from muscle, SAT, and hypothalamus (HIP), and OB-R, perilipin A, and -tubulin protein expression was analyzed by Western blot. A: representative immunoblot assay after incubation with a polyclonal rabbit anti-OB-R antibody specifically raised against the long isoform. B: representative Western blot after incubation with a polyclonal rabbit anti-perilipin A antibody in the same samples used in A. C: representative immunoblot analysis after incubation with the monoclonal mouse anti--tubulin antibody in the same samples used in A. D: densitometric immunosignal values (arbitrary units of band densities) of OB-R bands relative to those obtained for -tubulin.
    Human Rh Leptin R Fc Chimera, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+rh+leptin+r+fc+chimera/pm17234799-41-2-31?v=R%26D+Systems
    Average 93 stars, based on 1 article reviews
    human rh leptin r fc chimera - by Bioz Stars, 2026-07
    93/100 stars
    		  Buy from Supplier

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    Fig. 2. Determination of the expression of human leptin receptor (OB-R) in human skeletal muscle. Protein extracts were prepared from muscle, SAT, and hypothalamus (HIP), and OB-R, perilipin A, and -tubulin protein expression was analyzed by Western blot. A: representative immunoblot assay after incubation with a polyclonal rabbit anti-OB-R antibody specifically raised against the long isoform. B: representative Western blot after incubation with a polyclonal rabbit anti-perilipin A antibody in the same samples used in A. C: representative immunoblot analysis after incubation with the monoclonal mouse anti--tubulin antibody in the same samples used in A. D: densitometric immunosignal values (arbitrary units of band densities) of OB-R bands relative to those obtained for -tubulin.

    Journal: Journal of applied physiology (Bethesda, Md. : 1985)

    Article Title: Leptin receptors in human skeletal muscle.

    doi: 10.1152/japplphysiol.01313.2006

    Figure Lengend Snippet: Fig. 2. Determination of the expression of human leptin receptor (OB-R) in human skeletal muscle. Protein extracts were prepared from muscle, SAT, and hypothalamus (HIP), and OB-R, perilipin A, and -tubulin protein expression was analyzed by Western blot. A: representative immunoblot assay after incubation with a polyclonal rabbit anti-OB-R antibody specifically raised against the long isoform. B: representative Western blot after incubation with a polyclonal rabbit anti-perilipin A antibody in the same samples used in A. C: representative immunoblot analysis after incubation with the monoclonal mouse anti--tubulin antibody in the same samples used in A. D: densitometric immunosignal values (arbitrary units of band densities) of OB-R bands relative to those obtained for -tubulin.

    Article Snippet: The recombinant human (RH) leptin R/Fc chimera, generated from DNA containing the extracellular domain of OB-R (amino acid residues 1-839) fused to the Fc region of human IgG1, was obtained from R&D Systems (McKinley Place).

    Techniques: Expressing, Western Blot, Incubation

    Fig. 3. The anti-OB-R antibody recognized specifically the three OB-R bands detected in the muscle protein extracts. Increasing amounts of recombinant human (RH) leptin R/Fc (RH OB-R) chimera (0, 10, 100, 500 ng) were preincubated with anti-OB-R antibody (1:2,000). OB-R protein expression from muscle extracts was analyzed by immunoblotting using the preincubation solution. A: representative Western blot analysis with different preincubation solutions in the same muscle protein extract (50 g). B: representative immunoblot with the -tubulin antibody as a loading control. C: densitometric percentage of OB-R immnunostaining values (band quenching) in presence of increasing amounts (10, 100, 500 ng) of RH OB-R relative to those observed for a control (0 ng of RH OB-R). *P 0.01 vs. 0 ng of RH OB-R.

    Journal: Journal of applied physiology (Bethesda, Md. : 1985)

    Article Title: Leptin receptors in human skeletal muscle.

    doi: 10.1152/japplphysiol.01313.2006

    Figure Lengend Snippet: Fig. 3. The anti-OB-R antibody recognized specifically the three OB-R bands detected in the muscle protein extracts. Increasing amounts of recombinant human (RH) leptin R/Fc (RH OB-R) chimera (0, 10, 100, 500 ng) were preincubated with anti-OB-R antibody (1:2,000). OB-R protein expression from muscle extracts was analyzed by immunoblotting using the preincubation solution. A: representative Western blot analysis with different preincubation solutions in the same muscle protein extract (50 g). B: representative immunoblot with the -tubulin antibody as a loading control. C: densitometric percentage of OB-R immnunostaining values (band quenching) in presence of increasing amounts (10, 100, 500 ng) of RH OB-R relative to those observed for a control (0 ng of RH OB-R). *P 0.01 vs. 0 ng of RH OB-R.

    Article Snippet: The recombinant human (RH) leptin R/Fc chimera, generated from DNA containing the extracellular domain of OB-R (amino acid residues 1-839) fused to the Fc region of human IgG1, was obtained from R&D Systems (McKinley Place).

    Techniques: Recombinant, Expressing, Western Blot, Control