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resource source identifier recombinant human flt 3 ligand flt3l protein r d systems 308 fk recombinant human igf i igf 1 protein  (R&D Systems)


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    R&D Systems resource source identifier recombinant human flt 3 ligand flt3l protein r d systems 308 fk recombinant human igf i igf 1 protein
    Resource Source Identifier Recombinant Human Flt 3 Ligand Flt3l Protein R D Systems 308 Fk Recombinant Human Igf I Igf 1 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+recombinant+proteins+ligand+1/pm41512836-315-2-10?v=R%26D+Systems
    Average 95 stars, based on 69 article reviews
    resource source identifier recombinant human flt 3 ligand flt3l protein r d systems 308 fk recombinant human igf i igf 1 protein - by Bioz Stars, 2026-07
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    R&D Systems tgfβ1 recombinant ligand
    <t>TGFβ1</t> regulates the secretion of soluble type I collagen through the activity of GLI2 . A, left, relative GLI2 mRNA expression in HPSC fibroblast treated with TGFβ1 or vehicle (control). Right, relative COL1A1 mRNA expression in HPSC fibroblasts treated with TGFβ1 or vehicle (control). HPSCs were treated with 20 ng/ml TGFβ1 over 72 h. RNA was collected, and qPCR was performed (n = 3). B, left, effect of GLI2 silencing on COL1A1 expression triggered by TGFβ1. HPSCs were incubated with siRNA targeting GLI2 (siGLI2) or nontargeting control (NT). After 48 h, cells from each group were incubated with TGFβ1 or vehicle over 72 h. RNA was collected, and qPCR was assayed (n = 3). Right, effect of GLI2 silencing on soluble type I collagen secretion triggered by TGFβ1. HPSCs were treated with siGLI2 or NT. After 48 h, cells from each group were incubated with TGFβ1 or vehicle over 72 h. Supernatants from these cell cultures were harvested, and soluble type I collagen was measured by Sircol assay (n = 3). Results are expressed as means ± SD. Statistical significance, ∗ p < 0.05; ∗∗ p < 0.01; and ∗∗∗∗ p < 0.0001. HPSC, human pancreatic stellate cell; qPCR, quantitative PCR; TGFβ1, transforming growth factor β1.
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    R&D Systems ligands nrp1
    Binding rates of VEGF‐A to VEGFR1, VEGFR2, and <t>NRP1.</t> The respective binding affinities (A; K d ), association rate constants (B; k on , M −1 s −1 ), and dissociation rate constants (C; k off , s −1 ) of VEGF‐A for VEGFR1, VEGFR2, and NRP1 are plotted. The error bar represents the weighted mean ± standard error of the rate for each receptor. A one‐tailed Welch's t test with multiple testing corrections ( p ‐value < 0.05) was used to compare a pair of groups. HUVEC, human umbilical vein endothelial cell; PAE, porcine aortic endothelial; SPR, surface plasmon resonance.
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    R&D Systems ligand nrp1
    (A) Five VEF isoforms bind to VEGFR families and <t>NRP1.</t> VEGF-A binds to VEGFR1, VEGFR2, and NRP1, while VEGF-B and PlGF binds to VEGFR1 and NRP1. VEGF-C and VEGF-D binds to VEGFR2, VEGFR3, and NRP1. (B) Five PDGF isoforms interact with three PDGFRs: PDGFRα, PDGFRαβ, and PDGFRβ. PDGFRα binds to all PDGFs except for PDGF-DD, while PDGFRαβ binds to all PDGFs except for PDGF-AA. PDGFRβ binds to only PDGF-BB and PDGF-DD.
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    R&D Systems tgfb 1 ligand
    (A) Five VEF isoforms bind to VEGFR families and <t>NRP1.</t> VEGF-A binds to VEGFR1, VEGFR2, and NRP1, while VEGF-B and PlGF binds to VEGFR1 and NRP1. VEGF-C and VEGF-D binds to VEGFR2, VEGFR3, and NRP1. (B) Five PDGF isoforms interact with three PDGFRs: PDGFRα, PDGFRαβ, and PDGFRβ. PDGFRα binds to all PDGFs except for PDGF-DD, while PDGFRαβ binds to all PDGFs except for PDGF-AA. PDGFRβ binds to only PDGF-BB and PDGF-DD.
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    Image Search Results


    TGFβ1 regulates the secretion of soluble type I collagen through the activity of GLI2 . A, left, relative GLI2 mRNA expression in HPSC fibroblast treated with TGFβ1 or vehicle (control). Right, relative COL1A1 mRNA expression in HPSC fibroblasts treated with TGFβ1 or vehicle (control). HPSCs were treated with 20 ng/ml TGFβ1 over 72 h. RNA was collected, and qPCR was performed (n = 3). B, left, effect of GLI2 silencing on COL1A1 expression triggered by TGFβ1. HPSCs were incubated with siRNA targeting GLI2 (siGLI2) or nontargeting control (NT). After 48 h, cells from each group were incubated with TGFβ1 or vehicle over 72 h. RNA was collected, and qPCR was assayed (n = 3). Right, effect of GLI2 silencing on soluble type I collagen secretion triggered by TGFβ1. HPSCs were treated with siGLI2 or NT. After 48 h, cells from each group were incubated with TGFβ1 or vehicle over 72 h. Supernatants from these cell cultures were harvested, and soluble type I collagen was measured by Sircol assay (n = 3). Results are expressed as means ± SD. Statistical significance, ∗ p < 0.05; ∗∗ p < 0.01; and ∗∗∗∗ p < 0.0001. HPSC, human pancreatic stellate cell; qPCR, quantitative PCR; TGFβ1, transforming growth factor β1.

    Journal: The Journal of Biological Chemistry

    Article Title: Paracrine regulation of pancreatic cancer cell response to chemotherapy by GLI2–collagen I signaling

    doi: 10.1016/j.jbc.2025.110311

    Figure Lengend Snippet: TGFβ1 regulates the secretion of soluble type I collagen through the activity of GLI2 . A, left, relative GLI2 mRNA expression in HPSC fibroblast treated with TGFβ1 or vehicle (control). Right, relative COL1A1 mRNA expression in HPSC fibroblasts treated with TGFβ1 or vehicle (control). HPSCs were treated with 20 ng/ml TGFβ1 over 72 h. RNA was collected, and qPCR was performed (n = 3). B, left, effect of GLI2 silencing on COL1A1 expression triggered by TGFβ1. HPSCs were incubated with siRNA targeting GLI2 (siGLI2) or nontargeting control (NT). After 48 h, cells from each group were incubated with TGFβ1 or vehicle over 72 h. RNA was collected, and qPCR was assayed (n = 3). Right, effect of GLI2 silencing on soluble type I collagen secretion triggered by TGFβ1. HPSCs were treated with siGLI2 or NT. After 48 h, cells from each group were incubated with TGFβ1 or vehicle over 72 h. Supernatants from these cell cultures were harvested, and soluble type I collagen was measured by Sircol assay (n = 3). Results are expressed as means ± SD. Statistical significance, ∗ p < 0.05; ∗∗ p < 0.01; and ∗∗∗∗ p < 0.0001. HPSC, human pancreatic stellate cell; qPCR, quantitative PCR; TGFβ1, transforming growth factor β1.

    Article Snippet: For TGFβ1 treatment, 20 ng/ml (HPSC) or 4 ng/ml (MRC-5) TGFβ1 recombinant ligand (240-B-002/CF; R&D Systems) was added to cells in complete media.

    Techniques: Activity Assay, Expressing, Control, Incubation, Real-time Polymerase Chain Reaction

    Binding rates of VEGF‐A to VEGFR1, VEGFR2, and NRP1. The respective binding affinities (A; K d ), association rate constants (B; k on , M −1 s −1 ), and dissociation rate constants (C; k off , s −1 ) of VEGF‐A for VEGFR1, VEGFR2, and NRP1 are plotted. The error bar represents the weighted mean ± standard error of the rate for each receptor. A one‐tailed Welch's t test with multiple testing corrections ( p ‐value < 0.05) was used to compare a pair of groups. HUVEC, human umbilical vein endothelial cell; PAE, porcine aortic endothelial; SPR, surface plasmon resonance.

    Journal: FASEB BioAdvances

    Article Title: Obesity Alters the Vascular Morphology and VEGF‐A Signaling in Adipose Tissue

    doi: 10.1096/fba.2025-00027

    Figure Lengend Snippet: Binding rates of VEGF‐A to VEGFR1, VEGFR2, and NRP1. The respective binding affinities (A; K d ), association rate constants (B; k on , M −1 s −1 ), and dissociation rate constants (C; k off , s −1 ) of VEGF‐A for VEGFR1, VEGFR2, and NRP1 are plotted. The error bar represents the weighted mean ± standard error of the rate for each receptor. A one‐tailed Welch's t test with multiple testing corrections ( p ‐value < 0.05) was used to compare a pair of groups. HUVEC, human umbilical vein endothelial cell; PAE, porcine aortic endothelial; SPR, surface plasmon resonance.

    Article Snippet: The ligands NRP1 (Cat. #3870‐N1‐025/CF, R&D Systems) and VEGFR2 (Cat. #357‐KD‐050/CF, R&D Systems) were immobilized using an amine coupling method.

    Techniques: Binding Assay, One-tailed Test, SPR Assay

    (A) Five VEF isoforms bind to VEGFR families and NRP1. VEGF-A binds to VEGFR1, VEGFR2, and NRP1, while VEGF-B and PlGF binds to VEGFR1 and NRP1. VEGF-C and VEGF-D binds to VEGFR2, VEGFR3, and NRP1. (B) Five PDGF isoforms interact with three PDGFRs: PDGFRα, PDGFRαβ, and PDGFRβ. PDGFRα binds to all PDGFs except for PDGF-DD, while PDGFRαβ binds to all PDGFs except for PDGF-AA. PDGFRβ binds to only PDGF-BB and PDGF-DD.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: (A) Five VEF isoforms bind to VEGFR families and NRP1. VEGF-A binds to VEGFR1, VEGFR2, and NRP1, while VEGF-B and PlGF binds to VEGFR1 and NRP1. VEGF-C and VEGF-D binds to VEGFR2, VEGFR3, and NRP1. (B) Five PDGF isoforms interact with three PDGFRs: PDGFRα, PDGFRαβ, and PDGFRβ. PDGFRα binds to all PDGFs except for PDGF-DD, while PDGFRαβ binds to all PDGFs except for PDGF-AA. PDGFRβ binds to only PDGF-BB and PDGF-DD.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    (A) VEGF-A binds to all types of receptors: VEGFR1, VEGFR2, NRP1, PDGFR⍺, and PDGFRβ. VEGF-B and PlGF bind to VEGFR1 and NRP1. PDGF-AA, PDGF-AB, and PDGF-BB bind to VEGFR2 and PDGFR⍺ while PDGF-AB and –BB bind to PDGFRβ unlike PDGF-AA. (B) Receptors also form complex with or without ligand binding. VEGFR1 can form a complex with NRP1. VEGF-A:VEGFR2 complex can bind to NRP1, leading to a VEGF-A:VEGFR2:NRP1 complex. VEGF-A:NRP1 complex can bind to VEGFR2, forming a VEGF-A:VEGFR2:NRP1 complex, again.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: (A) VEGF-A binds to all types of receptors: VEGFR1, VEGFR2, NRP1, PDGFR⍺, and PDGFRβ. VEGF-B and PlGF bind to VEGFR1 and NRP1. PDGF-AA, PDGF-AB, and PDGF-BB bind to VEGFR2 and PDGFR⍺ while PDGF-AB and –BB bind to PDGFRβ unlike PDGF-AA. (B) Receptors also form complex with or without ligand binding. VEGFR1 can form a complex with NRP1. VEGF-A:VEGFR2 complex can bind to NRP1, leading to a VEGF-A:VEGFR2:NRP1 complex. VEGF-A:NRP1 complex can bind to VEGFR2, forming a VEGF-A:VEGFR2:NRP1 complex, again.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques: Ligand Binding Assay

    The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the VEGFR1 density is 1,600 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the VEGFR1 density is 1,600 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the VEGFR1 density is 1,600 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the VEGFR1 density is 1,600 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of VEGFR1 density is 1,600 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of VEGFR1 density is 1,600 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the VEGFR2 density is 4,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the VEGFR2 density is 4,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the VEGFR2 density is 4,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the VEGFR2 density is 4,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of VEGFR2 density is 4,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of VEGFR2 density is 4,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of the concentrations of free and bound VEGF-A (A), VEGF-B, (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) at each NRP1 density are plotted. The light blue area represents the percentage of free ligands, while the dark blue area represents the percentage of bound ligands for each receptor density. The baseline of NRP1 density is 44,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of the concentrations of free and bound VEGF-A (A), VEGF-B, (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) at each NRP1 density are plotted. The light blue area represents the percentage of free ligands, while the dark blue area represents the percentage of bound ligands for each receptor density. The baseline of NRP1 density is 44,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The colored area represents the concentration of free VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) for each density of the receptor. The baseline of NRP1 density is 44,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The colored area represents the concentration of free VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) for each density of the receptor. The baseline of NRP1 density is 44,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques: Concentration Assay

    The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the NRP1 density is 44,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the NRP1 density is 44,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the NRP1 density is 44,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the NRP1 density is 44,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of NRP1 density is 44,100 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of NRP1 density is 44,100 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of the concentrations of free and bound VEGF-A (A), VEGF-B, (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) at each NRP1 density are plotted. The light blue area represents the percentage of free ligands, while the dark blue area represents the percentage of bound ligands for each receptor density. The baseline of PDGFRα density is 5,000 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of the concentrations of free and bound VEGF-A (A), VEGF-B, (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) at each NRP1 density are plotted. The light blue area represents the percentage of free ligands, while the dark blue area represents the percentage of bound ligands for each receptor density. The baseline of PDGFRα density is 5,000 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of PDGFRα density is 5,000 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of PDGFRα density is 5,000 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the PDGFRα density is 5,000 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the PDGFRα density is 5,000 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the PDGFRα density is 5,000 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the PDGFRα density is 5,000 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the PDGFRβ density is 5,300 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The concentrations of VEGFR1, VEGFR2, NRP1, PDGFRα, and PDGFRβ that are bound to VEGF-A (A), VEGF-B (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) are represented. The baseline value of the PDGFRβ density is 5,300 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of the concentrations of free and bound VEGF-A (A), VEGF-B, (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) at each NRP1 density are plotted. The light blue area represents the percentage of free ligands, while the dark blue area represents the percentage of bound ligands for each receptor density. The baseline of PDGFRβ density is 5,300 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of the concentrations of free and bound VEGF-A (A), VEGF-B, (B), PlGF (C), PDGF-AA (D), PDGF-AB (E), and PDGF-BB (F) at each NRP1 density are plotted. The light blue area represents the percentage of free ligands, while the dark blue area represents the percentage of bound ligands for each receptor density. The baseline of PDGFRβ density is 5,300 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of PDGFRβ density is 5,300 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of free and bound VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The light blue area represents the percentage of free receptors, while the dark blue area represents the percentage of bound receptors for each receptor density. The baseline of PDGFRβ density is 5,300 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques:

    The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the PDGFRβ density is 5,300 rec/cell.

    Journal: bioRxiv

    Article Title: Cross-family interactions of vascular endothelial growth factors and platelet-derived growth factors on the endothelial cell surface: A computational model

    doi: 10.1101/2025.02.27.640640

    Figure Lengend Snippet: The percentages of VEGF-A, VEGF-B, PlGF, PDGF-AA, PDGF-AB, and PDGF-BB bound to VEGFR1 (A), VEGFR2 (B), NRP1 (C), PDGFRα (D), and PDGFRβ (E) are represented. The baseline value of the PDGFRβ density is 5,300 rec/cell.

    Article Snippet: The ligand NRP1 (Cat. #3870-N1-025/CF, R&D Systems), VEGFR1 (Cat. #321-FL-050/CF, R&D Systems) and VEGFR2 (Cat. #357-KD-050/CF, R&D Systems), were immobilized using an amine coupling method.

    Techniques: