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affinity recombinant mouse leptin  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology affinity recombinant mouse leptin
    Fig. 1. <t>Leptin</t> receptor expression in glomerular endothelial cells (GER). (A) Ligand binding of <t>[125I]-recombinant</t> murine leptin to GER monolayers. Data are presented as Scatchard blot. Each point is the mean of four independent experiments performed in duplicate. Unspecific binding was performed in the presence of 1026 m nonradioactive murine leptin and is subtracted from the binding curve. GERs exhibit high-affinity receptors for leptin with a Kd of 4 nm and Bmax of 9700 receptors/cell. (B) Binding of 5 nm of [125I]-recombinant murine leptin in the presence of 5 mg of a goat polyclonal antimouse leptin receptor antibody (a-ObR Ab) or the same concentration of normal goat IgG. Total binding of leptin in the presence of normal goat IgG was considered as 100%. The a-ObR antibody, but not nonimmune goat IgG, significantly reduced binding of leptin to its putative receptor (P , 0.01, N 5 5 independent binding experiments). (C) Expression of the short rat isoform (r-Ob-Ra) but not the long form (r-Ob-Rb) in cultured GERs. cDNA amplification of reverse transcribed total RNA. A specific 487 bp band is detected in the r-Ob-Ra, but not the predicted 370 bp band in the r-Ob-Rb lane. This experiment was independently repeated five times with similar results. However, the r-Ob-Rb isoform could be easily amplified from rat whole brain cDNA using the same concentrations of primers and amplification conditions (data not shown).
    Affinity Recombinant Mouse Leptin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 340 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/affinity recombinant mouse leptin/product/Santa Cruz Biotechnology
    Average 95 stars, based on 340 article reviews
    affinity recombinant mouse leptin - by Bioz Stars, 2026-05
    95/100 stars

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    1) Product Images from "Leptin stimulates proliferation and TGF-beta expression in renal glomerular endothelial cells: potential role in glomerulosclerosis [seecomments]."

    Article Title: Leptin stimulates proliferation and TGF-beta expression in renal glomerular endothelial cells: potential role in glomerulosclerosis [seecomments].

    Journal: Kidney international

    doi: 10.1046/j.1523-1755.1999.00626.x

    Fig. 1. Leptin receptor expression in glomerular endothelial cells (GER). (A) Ligand binding of [125I]-recombinant murine leptin to GER monolayers. Data are presented as Scatchard blot. Each point is the mean of four independent experiments performed in duplicate. Unspecific binding was performed in the presence of 1026 m nonradioactive murine leptin and is subtracted from the binding curve. GERs exhibit high-affinity receptors for leptin with a Kd of 4 nm and Bmax of 9700 receptors/cell. (B) Binding of 5 nm of [125I]-recombinant murine leptin in the presence of 5 mg of a goat polyclonal antimouse leptin receptor antibody (a-ObR Ab) or the same concentration of normal goat IgG. Total binding of leptin in the presence of normal goat IgG was considered as 100%. The a-ObR antibody, but not nonimmune goat IgG, significantly reduced binding of leptin to its putative receptor (P , 0.01, N 5 5 independent binding experiments). (C) Expression of the short rat isoform (r-Ob-Ra) but not the long form (r-Ob-Rb) in cultured GERs. cDNA amplification of reverse transcribed total RNA. A specific 487 bp band is detected in the r-Ob-Ra, but not the predicted 370 bp band in the r-Ob-Rb lane. This experiment was independently repeated five times with similar results. However, the r-Ob-Rb isoform could be easily amplified from rat whole brain cDNA using the same concentrations of primers and amplification conditions (data not shown).
    Figure Legend Snippet: Fig. 1. Leptin receptor expression in glomerular endothelial cells (GER). (A) Ligand binding of [125I]-recombinant murine leptin to GER monolayers. Data are presented as Scatchard blot. Each point is the mean of four independent experiments performed in duplicate. Unspecific binding was performed in the presence of 1026 m nonradioactive murine leptin and is subtracted from the binding curve. GERs exhibit high-affinity receptors for leptin with a Kd of 4 nm and Bmax of 9700 receptors/cell. (B) Binding of 5 nm of [125I]-recombinant murine leptin in the presence of 5 mg of a goat polyclonal antimouse leptin receptor antibody (a-ObR Ab) or the same concentration of normal goat IgG. Total binding of leptin in the presence of normal goat IgG was considered as 100%. The a-ObR antibody, but not nonimmune goat IgG, significantly reduced binding of leptin to its putative receptor (P , 0.01, N 5 5 independent binding experiments). (C) Expression of the short rat isoform (r-Ob-Ra) but not the long form (r-Ob-Rb) in cultured GERs. cDNA amplification of reverse transcribed total RNA. A specific 487 bp band is detected in the r-Ob-Ra, but not the predicted 370 bp band in the r-Ob-Rb lane. This experiment was independently repeated five times with similar results. However, the r-Ob-Rb isoform could be easily amplified from rat whole brain cDNA using the same concentrations of primers and amplification conditions (data not shown).

    Techniques Used: Expressing, Ligand Binding Assay, Recombinant, Binding Assay, Concentration Assay, Cell Culture, Reverse Transcription

    Fig. 4. Leptin stimulates expression of transforming growth factor-b1 (TGF-b1) in glomerular endothelial cells (GERs). (A) TGF-b1 protein secretion in the cell culture supernatant was also significantly stimulated by a single dose of leptin (6.25 to 625 nm) for 48 hours (N 5 3 to 4 independent stimulation experiments, *P , 0.05 vs. unstimulated controls). (B) Northern blot. A single dose of 0.62 to 625 nm leptin for 48 hours increased TGF-b1 mRNA expression. This blot is representative of three independent experiments with qualitatively similar results.
    Figure Legend Snippet: Fig. 4. Leptin stimulates expression of transforming growth factor-b1 (TGF-b1) in glomerular endothelial cells (GERs). (A) TGF-b1 protein secretion in the cell culture supernatant was also significantly stimulated by a single dose of leptin (6.25 to 625 nm) for 48 hours (N 5 3 to 4 independent stimulation experiments, *P , 0.05 vs. unstimulated controls). (B) Northern blot. A single dose of 0.62 to 625 nm leptin for 48 hours increased TGF-b1 mRNA expression. This blot is representative of three independent experiments with qualitatively similar results.

    Techniques Used: Expressing, Cell Culture, Northern Blot

    Fig. 6. Glomerular mRNA expression in leptin-infused rats. (A) Intraperitoneal infusion of murine leptin with osmotic minipumps for 72 hours stimulated glomerular mRNA expression for PCNA and TGF-b1, but not for a1(IV) collagen. (B) Continuous infusion for three weeks increased glomerular transcripts for TGF-b1 and a1(IV) collagen, whereas PCNA mRNA returned to baseline. This blot is representative of three independent experiments with qualitatively similar results.
    Figure Legend Snippet: Fig. 6. Glomerular mRNA expression in leptin-infused rats. (A) Intraperitoneal infusion of murine leptin with osmotic minipumps for 72 hours stimulated glomerular mRNA expression for PCNA and TGF-b1, but not for a1(IV) collagen. (B) Continuous infusion for three weeks increased glomerular transcripts for TGF-b1 and a1(IV) collagen, whereas PCNA mRNA returned to baseline. This blot is representative of three independent experiments with qualitatively similar results.

    Techniques Used: Expressing

    Fig. 7. Immunohistological staining of renal sections from in vivo infusion experiments. (A and B) Staining of kidney sections of control or leptin- infused rats (72 hr) with a specific anti-PCNA antibody to assess in vivo proliferation of renal cells. Kidney section of rats infused with solvent for 72 hours revealed no glomerular PCNA staining, suggesting very low basal proliferation in normal glomeruli (A). In contrast, in leptin-infused animals PCNA-expressing cells are found in glomeruli (arrow; B). (C–F) Staining for collagen type IV in rats infused for three weeks with solvent or leptin. There was a light collagen type IV staining in mesangial matrix and tubular basal membranes of control-infused rats (C). However, an increase in glomerular collagen type IV staining was detected in rats infused with leptin for three weeks (D). A higher magnification reveals glomerular collagen type IV staining restricted to the mesangial area of control-infused animals (E), whereas leptin-infused animals exhibit a segmental increase in collagen type IV deposition (F). Magnifications 3150 for A–D, 3 300 for E and F.
    Figure Legend Snippet: Fig. 7. Immunohistological staining of renal sections from in vivo infusion experiments. (A and B) Staining of kidney sections of control or leptin- infused rats (72 hr) with a specific anti-PCNA antibody to assess in vivo proliferation of renal cells. Kidney section of rats infused with solvent for 72 hours revealed no glomerular PCNA staining, suggesting very low basal proliferation in normal glomeruli (A). In contrast, in leptin-infused animals PCNA-expressing cells are found in glomeruli (arrow; B). (C–F) Staining for collagen type IV in rats infused for three weeks with solvent or leptin. There was a light collagen type IV staining in mesangial matrix and tubular basal membranes of control-infused rats (C). However, an increase in glomerular collagen type IV staining was detected in rats infused with leptin for three weeks (D). A higher magnification reveals glomerular collagen type IV staining restricted to the mesangial area of control-infused animals (E), whereas leptin-infused animals exhibit a segmental increase in collagen type IV deposition (F). Magnifications 3150 for A–D, 3 300 for E and F.

    Techniques Used: Staining, In Vivo, Control, Solvent, Expressing



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    affinity recombinant mouse leptin  (Santa Cruz Biotechnology)
    95
    Santa Cruz Biotechnology affinity recombinant mouse leptin
    Fig. 1. <t>Leptin</t> receptor expression in glomerular endothelial cells (GER). (A) Ligand binding of <t>[125I]-recombinant</t> murine leptin to GER monolayers. Data are presented as Scatchard blot. Each point is the mean of four independent experiments performed in duplicate. Unspecific binding was performed in the presence of 1026 m nonradioactive murine leptin and is subtracted from the binding curve. GERs exhibit high-affinity receptors for leptin with a Kd of 4 nm and Bmax of 9700 receptors/cell. (B) Binding of 5 nm of [125I]-recombinant murine leptin in the presence of 5 mg of a goat polyclonal antimouse leptin receptor antibody (a-ObR Ab) or the same concentration of normal goat IgG. Total binding of leptin in the presence of normal goat IgG was considered as 100%. The a-ObR antibody, but not nonimmune goat IgG, significantly reduced binding of leptin to its putative receptor (P , 0.01, N 5 5 independent binding experiments). (C) Expression of the short rat isoform (r-Ob-Ra) but not the long form (r-Ob-Rb) in cultured GERs. cDNA amplification of reverse transcribed total RNA. A specific 487 bp band is detected in the r-Ob-Ra, but not the predicted 370 bp band in the r-Ob-Rb lane. This experiment was independently repeated five times with similar results. However, the r-Ob-Rb isoform could be easily amplified from rat whole brain cDNA using the same concentrations of primers and amplification conditions (data not shown).
    Affinity Recombinant Mouse Leptin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/affinity recombinant mouse leptin/product/Santa Cruz Biotechnology
    Average 95 stars, based on 1 article reviews
    affinity recombinant mouse leptin - by Bioz Stars, 2026-05
    95/100 stars
    		  Buy from Supplier

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    Fig. 1. Leptin receptor expression in glomerular endothelial cells (GER). (A) Ligand binding of [125I]-recombinant murine leptin to GER monolayers. Data are presented as Scatchard blot. Each point is the mean of four independent experiments performed in duplicate. Unspecific binding was performed in the presence of 1026 m nonradioactive murine leptin and is subtracted from the binding curve. GERs exhibit high-affinity receptors for leptin with a Kd of 4 nm and Bmax of 9700 receptors/cell. (B) Binding of 5 nm of [125I]-recombinant murine leptin in the presence of 5 mg of a goat polyclonal antimouse leptin receptor antibody (a-ObR Ab) or the same concentration of normal goat IgG. Total binding of leptin in the presence of normal goat IgG was considered as 100%. The a-ObR antibody, but not nonimmune goat IgG, significantly reduced binding of leptin to its putative receptor (P , 0.01, N 5 5 independent binding experiments). (C) Expression of the short rat isoform (r-Ob-Ra) but not the long form (r-Ob-Rb) in cultured GERs. cDNA amplification of reverse transcribed total RNA. A specific 487 bp band is detected in the r-Ob-Ra, but not the predicted 370 bp band in the r-Ob-Rb lane. This experiment was independently repeated five times with similar results. However, the r-Ob-Rb isoform could be easily amplified from rat whole brain cDNA using the same concentrations of primers and amplification conditions (data not shown).

    Journal: Kidney international

    Article Title: Leptin stimulates proliferation and TGF-beta expression in renal glomerular endothelial cells: potential role in glomerulosclerosis [seecomments].

    doi: 10.1046/j.1523-1755.1999.00626.x

    Figure Lengend Snippet: Fig. 1. Leptin receptor expression in glomerular endothelial cells (GER). (A) Ligand binding of [125I]-recombinant murine leptin to GER monolayers. Data are presented as Scatchard blot. Each point is the mean of four independent experiments performed in duplicate. Unspecific binding was performed in the presence of 1026 m nonradioactive murine leptin and is subtracted from the binding curve. GERs exhibit high-affinity receptors for leptin with a Kd of 4 nm and Bmax of 9700 receptors/cell. (B) Binding of 5 nm of [125I]-recombinant murine leptin in the presence of 5 mg of a goat polyclonal antimouse leptin receptor antibody (a-ObR Ab) or the same concentration of normal goat IgG. Total binding of leptin in the presence of normal goat IgG was considered as 100%. The a-ObR antibody, but not nonimmune goat IgG, significantly reduced binding of leptin to its putative receptor (P , 0.01, N 5 5 independent binding experiments). (C) Expression of the short rat isoform (r-Ob-Ra) but not the long form (r-Ob-Rb) in cultured GERs. cDNA amplification of reverse transcribed total RNA. A specific 487 bp band is detected in the r-Ob-Ra, but not the predicted 370 bp band in the r-Ob-Rb lane. This experiment was independently repeated five times with similar results. However, the r-Ob-Rb isoform could be easily amplified from rat whole brain cDNA using the same concentrations of primers and amplification conditions (data not shown).

    Article Snippet: Additional cells were treated with binant murine leptin in the presence of 5 mg of an affinity- recombinant mouse leptin from two additional suppliers purified goat polyclonal antibody (Santa Cruz Biotech- (Biomol, Hamburg, Germany; and Pepro Tech, Rocky nology, Santa Cruz, CA, USA) raised against a peptide Hill, CT, USA), to insure that the results were not depencorresponding to amino acids 32 to 51 mapping at the dent on the source of the leptin.

    Techniques: Expressing, Ligand Binding Assay, Recombinant, Binding Assay, Concentration Assay, Cell Culture, Reverse Transcription

    Fig. 4. Leptin stimulates expression of transforming growth factor-b1 (TGF-b1) in glomerular endothelial cells (GERs). (A) TGF-b1 protein secretion in the cell culture supernatant was also significantly stimulated by a single dose of leptin (6.25 to 625 nm) for 48 hours (N 5 3 to 4 independent stimulation experiments, *P , 0.05 vs. unstimulated controls). (B) Northern blot. A single dose of 0.62 to 625 nm leptin for 48 hours increased TGF-b1 mRNA expression. This blot is representative of three independent experiments with qualitatively similar results.

    Journal: Kidney international

    Article Title: Leptin stimulates proliferation and TGF-beta expression in renal glomerular endothelial cells: potential role in glomerulosclerosis [seecomments].

    doi: 10.1046/j.1523-1755.1999.00626.x

    Figure Lengend Snippet: Fig. 4. Leptin stimulates expression of transforming growth factor-b1 (TGF-b1) in glomerular endothelial cells (GERs). (A) TGF-b1 protein secretion in the cell culture supernatant was also significantly stimulated by a single dose of leptin (6.25 to 625 nm) for 48 hours (N 5 3 to 4 independent stimulation experiments, *P , 0.05 vs. unstimulated controls). (B) Northern blot. A single dose of 0.62 to 625 nm leptin for 48 hours increased TGF-b1 mRNA expression. This blot is representative of three independent experiments with qualitatively similar results.

    Article Snippet: Additional cells were treated with binant murine leptin in the presence of 5 mg of an affinity- recombinant mouse leptin from two additional suppliers purified goat polyclonal antibody (Santa Cruz Biotech- (Biomol, Hamburg, Germany; and Pepro Tech, Rocky nology, Santa Cruz, CA, USA) raised against a peptide Hill, CT, USA), to insure that the results were not depencorresponding to amino acids 32 to 51 mapping at the dent on the source of the leptin.

    Techniques: Expressing, Cell Culture, Northern Blot

    Fig. 6. Glomerular mRNA expression in leptin-infused rats. (A) Intraperitoneal infusion of murine leptin with osmotic minipumps for 72 hours stimulated glomerular mRNA expression for PCNA and TGF-b1, but not for a1(IV) collagen. (B) Continuous infusion for three weeks increased glomerular transcripts for TGF-b1 and a1(IV) collagen, whereas PCNA mRNA returned to baseline. This blot is representative of three independent experiments with qualitatively similar results.

    Journal: Kidney international

    Article Title: Leptin stimulates proliferation and TGF-beta expression in renal glomerular endothelial cells: potential role in glomerulosclerosis [seecomments].

    doi: 10.1046/j.1523-1755.1999.00626.x

    Figure Lengend Snippet: Fig. 6. Glomerular mRNA expression in leptin-infused rats. (A) Intraperitoneal infusion of murine leptin with osmotic minipumps for 72 hours stimulated glomerular mRNA expression for PCNA and TGF-b1, but not for a1(IV) collagen. (B) Continuous infusion for three weeks increased glomerular transcripts for TGF-b1 and a1(IV) collagen, whereas PCNA mRNA returned to baseline. This blot is representative of three independent experiments with qualitatively similar results.

    Article Snippet: Additional cells were treated with binant murine leptin in the presence of 5 mg of an affinity- recombinant mouse leptin from two additional suppliers purified goat polyclonal antibody (Santa Cruz Biotech- (Biomol, Hamburg, Germany; and Pepro Tech, Rocky nology, Santa Cruz, CA, USA) raised against a peptide Hill, CT, USA), to insure that the results were not depencorresponding to amino acids 32 to 51 mapping at the dent on the source of the leptin.

    Techniques: Expressing

    Fig. 7. Immunohistological staining of renal sections from in vivo infusion experiments. (A and B) Staining of kidney sections of control or leptin- infused rats (72 hr) with a specific anti-PCNA antibody to assess in vivo proliferation of renal cells. Kidney section of rats infused with solvent for 72 hours revealed no glomerular PCNA staining, suggesting very low basal proliferation in normal glomeruli (A). In contrast, in leptin-infused animals PCNA-expressing cells are found in glomeruli (arrow; B). (C–F) Staining for collagen type IV in rats infused for three weeks with solvent or leptin. There was a light collagen type IV staining in mesangial matrix and tubular basal membranes of control-infused rats (C). However, an increase in glomerular collagen type IV staining was detected in rats infused with leptin for three weeks (D). A higher magnification reveals glomerular collagen type IV staining restricted to the mesangial area of control-infused animals (E), whereas leptin-infused animals exhibit a segmental increase in collagen type IV deposition (F). Magnifications 3150 for A–D, 3 300 for E and F.

    Journal: Kidney international

    Article Title: Leptin stimulates proliferation and TGF-beta expression in renal glomerular endothelial cells: potential role in glomerulosclerosis [seecomments].

    doi: 10.1046/j.1523-1755.1999.00626.x

    Figure Lengend Snippet: Fig. 7. Immunohistological staining of renal sections from in vivo infusion experiments. (A and B) Staining of kidney sections of control or leptin- infused rats (72 hr) with a specific anti-PCNA antibody to assess in vivo proliferation of renal cells. Kidney section of rats infused with solvent for 72 hours revealed no glomerular PCNA staining, suggesting very low basal proliferation in normal glomeruli (A). In contrast, in leptin-infused animals PCNA-expressing cells are found in glomeruli (arrow; B). (C–F) Staining for collagen type IV in rats infused for three weeks with solvent or leptin. There was a light collagen type IV staining in mesangial matrix and tubular basal membranes of control-infused rats (C). However, an increase in glomerular collagen type IV staining was detected in rats infused with leptin for three weeks (D). A higher magnification reveals glomerular collagen type IV staining restricted to the mesangial area of control-infused animals (E), whereas leptin-infused animals exhibit a segmental increase in collagen type IV deposition (F). Magnifications 3150 for A–D, 3 300 for E and F.

    Article Snippet: Additional cells were treated with binant murine leptin in the presence of 5 mg of an affinity- recombinant mouse leptin from two additional suppliers purified goat polyclonal antibody (Santa Cruz Biotech- (Biomol, Hamburg, Germany; and Pepro Tech, Rocky nology, Santa Cruz, CA, USA) raised against a peptide Hill, CT, USA), to insure that the results were not depencorresponding to amino acids 32 to 51 mapping at the dent on the source of the leptin.

    Techniques: Staining, In Vivo, Control, Solvent, Expressing