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recombinant soluble human cr1 scr1 (R&D Systems)

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R&D Systems recombinant soluble human cr1 scr1
Kinetic and equilibrium dissociation constants for the binding of C1q to immobilized soluble CR1 (sCR1) and CR1 CCP22-30.

Kinetic and equilibrium dissociation constants for the binding of C1q to immobilized soluble CR1 (sCR1) and CR1 CCP22-30.

Recombinant Soluble Human Cr1 Scr1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews

recombinant soluble human cr1 scr1 - by Bioz Stars, 2026-03

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1) Product Images from "C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules"

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

Journal: Frontiers in Immunology

doi: 10.3389/fimmu.2018.00453

Figure Legend Snippet: Kinetic and equilibrium dissociation constants for the binding of C1q to immobilized soluble CR1 (sCR1) and CR1 CCP22-30.

Techniques Used: Binding Assay

Localization of the C1q binding sites in CR1 CCP22-30 using deletion fragments. (A) Schematic view of the different fragments of CR1 CCP22-30. Potential N-glycosylations are represented by open circles ○. (B) Interaction of C1q with immobilized CR1 CCP22-30 fragments analyzed by ELISA. C1q (10 µg/ml in PBS) was added to microtiter plate coated with 3.4 pmol of each CCP22-30 fragment as described in Section “ .” After 1.5 h incubation at room temperature, bound C1q was detected with rabbit antibodies recognizing C1q and HRP secondary antibodies. Data are presented as the mean ± SE of four individual experiments. (**), Student’s t -test values p < 0.01 of C1q binding to each fragment compared to CCP22-30.

Figure Legend Snippet: Localization of the C1q binding sites in CR1 CCP22-30 using deletion fragments. (A) Schematic view of the different fragments of CR1 CCP22-30. Potential N-glycosylations are represented by open circles ○. (B) Interaction of C1q with immobilized CR1 CCP22-30 fragments analyzed by ELISA. C1q (10 µg/ml in PBS) was added to microtiter plate coated with 3.4 pmol of each CCP22-30 fragment as described in Section “ .” After 1.5 h incubation at room temperature, bound C1q was detected with rabbit antibodies recognizing C1q and HRP secondary antibodies. Data are presented as the mean ± SE of four individual experiments. (**), Student’s t -test values p < 0.01 of C1q binding to each fragment compared to CCP22-30.

Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Incubation

Complement receptor type 1 (CR1) variants produced to study the CCP24-25 module pair interaction properties. (A) Schematic view of CCP24-25 variants produced in eukaryotic cells. Potential N-glycosylations are represented by open circles ○. (B) SDS-PAGE analysis of 4 µg of the CR1variants under reducing conditions. The positions of the molecular weight markers (expressed in kilodaltons) are indicated. A full scan of the original gel is provided in Figure S1 in Supplementary Material .

Figure Legend Snippet: Complement receptor type 1 (CR1) variants produced to study the CCP24-25 module pair interaction properties. (A) Schematic view of CCP24-25 variants produced in eukaryotic cells. Potential N-glycosylations are represented by open circles ○. (B) SDS-PAGE analysis of 4 µg of the CR1variants under reducing conditions. The positions of the molecular weight markers (expressed in kilodaltons) are indicated. A full scan of the original gel is provided in Figure S1 in Supplementary Material .

Techniques Used: Produced, SDS Page, Molecular Weight

Kinetic analysis of the interaction of C1q and mannose-binding lectin (MBL) with CR1 CCP24-25. C1q (A) and MBL (B) , at indicated concentrations, were injected in 50 mM triethanolamine-HCl (TEA), 145 mM NaCl, 0.05% surfactant P20, pH 7.4, on immobilized CR1 CCP24-25 (1,000 RU). The buffer was supplemented with 3 mM EDTA for MBL binding. Fits are shown as dotted lines and were obtained by global fitting of the data using a 1:1 Langmuir-binding model. The kinetic constants obtained are framed on the top of each sensorgramm.

Figure Legend Snippet: Kinetic analysis of the interaction of C1q and mannose-binding lectin (MBL) with CR1 CCP24-25. C1q (A) and MBL (B) , at indicated concentrations, were injected in 50 mM triethanolamine-HCl (TEA), 145 mM NaCl, 0.05% surfactant P20, pH 7.4, on immobilized CR1 CCP24-25 (1,000 RU). The buffer was supplemented with 3 mM EDTA for MBL binding. Fits are shown as dotted lines and were obtained by global fitting of the data using a 1:1 Langmuir-binding model. The kinetic constants obtained are framed on the top of each sensorgramm.

Techniques Used: Binding Assay, Injection

$Interaction of C1q and mannose-binding lectin (MBL) with immobilized CR1 CCP22-30 and CR1 ΔCCP24-25. The binding curves were obtained in single cycle mode by injecting increasing concentrations of C1q (A) or MBL (B) on immobilized CR1 CCP22-30 (3,000 RU) or CR1 ΔCCP24-25 (2,200 RU). C1q (0.25, 0.5, 1, 2, and 4 nM) was injected at 20 µl/min for 180 s in 50 mM triethanolamine-HCl (TEA), 150 mM NaCl, 1 mM CaCl 2 , 0.05% surfractant P20, pH 7.4. MBL (1, 2, 4, 8, and 16 nM) was injected in the same conditions except that the buffer contained 3 mM EDTA instead of CaCl 2 .$
Figure Legend Snippet: Interaction of C1q and mannose-binding lectin (MBL) with immobilized CR1 CCP22-30 and CR1 ΔCCP24-25. The binding curves were obtained in single cycle mode by injecting increasing concentrations of C1q (A) or MBL (B) on immobilized CR1 CCP22-30 (3,000 RU) or CR1 ΔCCP24-25 (2,200 RU). C1q (0.25, 0.5, 1, 2, and 4 nM) was injected at 20 µl/min for 180 s in 50 mM triethanolamine-HCl (TEA), 150 mM NaCl, 1 mM CaCl 2 , 0.05% surfractant P20, pH 7.4. MBL (1, 2, 4, 8, and 16 nM) was injected in the same conditions except that the buffer contained 3 mM EDTA instead of CaCl 2 .

Techniques Used: Binding Assay, Injection

Elongated shape of CCP24-25, associated to a possible interpretative model. (A) Small-angle X-ray scattering (SAXS) pair distance distribution, (B) SAXS dimensionless Kratky plot, which shows elongation and remaining flexibility. (C) Fit of the model [shown in panels (D,E) ] to the experimental data. (D) Top and (E) side views of an ab initio envelope computed with GASBOR. A Coral-derived model of CCP24-25 is shown inside to illustrate how the shape corresponds to two CCP modules. This interpretative model is used to illustrate the positions on each module of glycosylation sites (green), rs 4844609 SNP (magenta), Knops groups variants (cyan), acidic clusters (red) initially suggested as potential MBL binding sites, and the other acidic residues (gray and black). D1529 is the homologous counterpart of D1076 in CR1 CCP17 (black). The two flexible carbohydrates included in the model are only illustrated in the side view.

Figure Legend Snippet: Elongated shape of CCP24-25, associated to a possible interpretative model. (A) Small-angle X-ray scattering (SAXS) pair distance distribution, (B) SAXS dimensionless Kratky plot, which shows elongation and remaining flexibility. (C) Fit of the model [shown in panels (D,E) ] to the experimental data. (D) Top and (E) side views of an ab initio envelope computed with GASBOR. A Coral-derived model of CCP24-25 is shown inside to illustrate how the shape corresponds to two CCP modules. This interpretative model is used to illustrate the positions on each module of glycosylation sites (green), rs 4844609 SNP (magenta), Knops groups variants (cyan), acidic clusters (red) initially suggested as potential MBL binding sites, and the other acidic residues (gray and black). D1529 is the homologous counterpart of D1076 in CR1 CCP17 (black). The two flexible carbohydrates included in the model are only illustrated in the side view.

Techniques Used: Derivative Assay, Glycoproteomics, Binding Assay

Localization of the binding site of soluble CR1 on C1q. (A) Comparative binding of C1q and its CLF and GR on complement receptor type 1 (CR1) CCP22-30 analyzed by surface plasmon resonance (SPR). The CR1 CCP22-30 fragment was immobilized on CM5 sensor chips (4,500 RU) and 2 nM of C1q or CLF and 12 nM of GR were injected over the surfaces as described in Section “ .” (B) MBL-associated serine protease (MASP)-3 competition of the binding of C1q to CR1 CCP22-30 analyzed by SPR. C1q (2 nM) was incubated at room temperature for 20 min in the absence or presence of recombinant MASP-3 at indicated molar ratios and injected over immobilized CR1 CCP22-30 (4,500 RU). No binding was observed when MASP-3 alone (20 nM) was injected.

Figure Legend Snippet: Localization of the binding site of soluble CR1 on C1q. (A) Comparative binding of C1q and its CLF and GR on complement receptor type 1 (CR1) CCP22-30 analyzed by surface plasmon resonance (SPR). The CR1 CCP22-30 fragment was immobilized on CM5 sensor chips (4,500 RU) and 2 nM of C1q or CLF and 12 nM of GR were injected over the surfaces as described in Section “ .” (B) MBL-associated serine protease (MASP)-3 competition of the binding of C1q to CR1 CCP22-30 analyzed by SPR. C1q (2 nM) was incubated at room temperature for 20 min in the absence or presence of recombinant MASP-3 at indicated molar ratios and injected over immobilized CR1 CCP22-30 (4,500 RU). No binding was observed when MASP-3 alone (20 nM) was injected.

Techniques Used: Binding Assay, SPR Assay, Injection, Incubation, Recombinant

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Journal: Frontiers in Immunology

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

doi: 10.3389/fimmu.2018.00453

Figure Lengend Snippet: Kinetic and equilibrium dissociation constants for the binding of C1q to immobilized soluble CR1 (sCR1) and CR1 CCP22-30.

Article Snippet: Recombinant soluble human CR1 (sCR1) was purchased from R&D Systems Europe.

Techniques: Binding Assay

Journal: Frontiers in Immunology

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

doi: 10.3389/fimmu.2018.00453

Figure Lengend Snippet: Localization of the C1q binding sites in CR1 CCP22-30 using deletion fragments. (A) Schematic view of the different fragments of CR1 CCP22-30. Potential N-glycosylations are represented by open circles ○. (B) Interaction of C1q with immobilized CR1 CCP22-30 fragments analyzed by ELISA. C1q (10 µg/ml in PBS) was added to microtiter plate coated with 3.4 pmol of each CCP22-30 fragment as described in Section “ .” After 1.5 h incubation at room temperature, bound C1q was detected with rabbit antibodies recognizing C1q and HRP secondary antibodies. Data are presented as the mean ± SE of four individual experiments. (**), Student’s t -test values p < 0.01 of C1q binding to each fragment compared to CCP22-30.

Article Snippet: Recombinant soluble human CR1 (sCR1) was purchased from R&D Systems Europe.

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Incubation

Journal: Frontiers in Immunology

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

doi: 10.3389/fimmu.2018.00453

Figure Lengend Snippet: Complement receptor type 1 (CR1) variants produced to study the CCP24-25 module pair interaction properties. (A) Schematic view of CCP24-25 variants produced in eukaryotic cells. Potential N-glycosylations are represented by open circles ○. (B) SDS-PAGE analysis of 4 µg of the CR1variants under reducing conditions. The positions of the molecular weight markers (expressed in kilodaltons) are indicated. A full scan of the original gel is provided in Figure S1 in Supplementary Material .

Article Snippet: Recombinant soluble human CR1 (sCR1) was purchased from R&D Systems Europe.

Techniques: Produced, SDS Page, Molecular Weight

Journal: Frontiers in Immunology

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

doi: 10.3389/fimmu.2018.00453

Figure Lengend Snippet: Kinetic analysis of the interaction of C1q and mannose-binding lectin (MBL) with CR1 CCP24-25. C1q (A) and MBL (B) , at indicated concentrations, were injected in 50 mM triethanolamine-HCl (TEA), 145 mM NaCl, 0.05% surfactant P20, pH 7.4, on immobilized CR1 CCP24-25 (1,000 RU). The buffer was supplemented with 3 mM EDTA for MBL binding. Fits are shown as dotted lines and were obtained by global fitting of the data using a 1:1 Langmuir-binding model. The kinetic constants obtained are framed on the top of each sensorgramm.

Article Snippet: Recombinant soluble human CR1 (sCR1) was purchased from R&D Systems Europe.

Techniques: Binding Assay, Injection

Journal: Frontiers in Immunology

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

doi: 10.3389/fimmu.2018.00453

Figure Lengend Snippet: Interaction of C1q and mannose-binding lectin (MBL) with immobilized CR1 CCP22-30 and CR1 ΔCCP24-25. The binding curves were obtained in single cycle mode by injecting increasing concentrations of C1q (A) or MBL (B) on immobilized CR1 CCP22-30 (3,000 RU) or CR1 ΔCCP24-25 (2,200 RU). C1q (0.25, 0.5, 1, 2, and 4 nM) was injected at 20 µl/min for 180 s in 50 mM triethanolamine-HCl (TEA), 150 mM NaCl, 1 mM CaCl 2 , 0.05% surfractant P20, pH 7.4. MBL (1, 2, 4, 8, and 16 nM) was injected in the same conditions except that the buffer contained 3 mM EDTA instead of CaCl 2 .

Article Snippet: Recombinant soluble human CR1 (sCR1) was purchased from R&D Systems Europe.

Techniques: Binding Assay, Injection

Journal: Frontiers in Immunology

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

doi: 10.3389/fimmu.2018.00453

Figure Lengend Snippet: Elongated shape of CCP24-25, associated to a possible interpretative model. (A) Small-angle X-ray scattering (SAXS) pair distance distribution, (B) SAXS dimensionless Kratky plot, which shows elongation and remaining flexibility. (C) Fit of the model [shown in panels (D,E) ] to the experimental data. (D) Top and (E) side views of an ab initio envelope computed with GASBOR. A Coral-derived model of CCP24-25 is shown inside to illustrate how the shape corresponds to two CCP modules. This interpretative model is used to illustrate the positions on each module of glycosylation sites (green), rs 4844609 SNP (magenta), Knops groups variants (cyan), acidic clusters (red) initially suggested as potential MBL binding sites, and the other acidic residues (gray and black). D1529 is the homologous counterpart of D1076 in CR1 CCP17 (black). The two flexible carbohydrates included in the model are only illustrated in the side view.

Article Snippet: Recombinant soluble human CR1 (sCR1) was purchased from R&D Systems Europe.

Techniques: Derivative Assay, Glycoproteomics, Binding Assay

Journal: Frontiers in Immunology

Article Title: C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules

doi: 10.3389/fimmu.2018.00453

Figure Lengend Snippet: Localization of the binding site of soluble CR1 on C1q. (A) Comparative binding of C1q and its CLF and GR on complement receptor type 1 (CR1) CCP22-30 analyzed by surface plasmon resonance (SPR). The CR1 CCP22-30 fragment was immobilized on CM5 sensor chips (4,500 RU) and 2 nM of C1q or CLF and 12 nM of GR were injected over the surfaces as described in Section “ .” (B) MBL-associated serine protease (MASP)-3 competition of the binding of C1q to CR1 CCP22-30 analyzed by SPR. C1q (2 nM) was incubated at room temperature for 20 min in the absence or presence of recombinant MASP-3 at indicated molar ratios and injected over immobilized CR1 CCP22-30 (4,500 RU). No binding was observed when MASP-3 alone (20 nM) was injected.

Article Snippet: Recombinant soluble human CR1 (sCR1) was purchased from R&D Systems Europe.

Techniques: Binding Assay, SPR Assay, Injection, Incubation, Recombinant

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