SPR-507 Search Results


bmp6  (R&D Systems)
95
R&D Systems bmp6
Figure 1. Structure-function study of the N and C terminus of ERFE. A, diagram of the human ERFE protein showing the signal sequence, N-terminal, and C-terminal domains, and their respective amino acid boundaries. B, AlphaFold2 model of human ERFE structure (left; colors correspond to segments in the diagram A and right; colored by confidence parameter pLDDT, blue = highest degree of confidence). C, amino acid conservation alignments of ERFE N- terminal and C-terminal domains across vertebrate species. D, top: diagrams of full-length, N terminus, and C terminus ERFE constructs that were used in bioassay and SPR. Bottom: qPCR expression of hepcidin in Hep3B cells treated with a range of concentrations of ERFE variants for 16 h. Data are normalized to untreated controls. N = 3 biological replicates. E, surface plasmon resonance sensorgrams of full-length, N-terminal, and C-terminal ERFE binding to immobilized BMP2, <t>BMP6,</t> and BMP2/6. BMP, bone morphogenetic protein; ERFE, erythroferrone; pLDDT, predicted local distance difference test; SPR, surface plasmon resonance.
Bmp6, supplied by R&D Systems, 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/product/SPR-507/Recombinant+Human+BMP-6+Protein/pm37866631-250-30-36
Average 95 stars, based on 1 article reviews
bmp6 - by Bioz Stars, 2026-10
95/100 stars
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human vps25 activation kit by crispra  (OriGene)
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VPS25 CRISPRa kit CRISPR gene activation of human vacuolar protein sorting 25 homolog
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mouse tyrobp activation kit by crispra  (OriGene)
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Tyrobp CRISPRa kit CRISPR gene activation of mouse TYRO protein tyrosine kinase binding protein
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apobec3d crispr/cas9 ko plasmid  (Santa Cruz Biotechnology)
N/A
Target species: human. CRISPR/Cas9 KO Plasmids consists of APOBEC3D-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double
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trip6 crispr/cas9 ko plasmid  (Santa Cruz Biotechnology)
N/A
CRISPR/Cas9 KO Plasmids consists of TRIP6-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double strand break (DSB)
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c11orf45 crispr activation plasmid  (Santa Cruz Biotechnology)
N/A
Target species: human. CRISPR/Cas9 KO Plasmids consists of C11orf45-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double
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aof1 crispr/cas9 ko plasmid  (Santa Cruz Biotechnology)
N/A
CRISPR/Cas9 KO Plasmids consists of AOF1-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double strand break (DSB)
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mzt2b crispr/cas9 ko plasmid  (Santa Cruz Biotechnology)
N/A
Target species: human. CRISPR/Cas9 KO Plasmids consists of MZT2B-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double
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olfr447 crispr/cas9 ko plasmid  (Santa Cruz Biotechnology)
N/A
Target species: mouse. CRISPR/Cas9 KO Plasmids consists of Olfr447-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double
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or10g9 crispr activation plasmid  (Santa Cruz Biotechnology)
N/A
Target species: human. CRISPR/Cas9 KO Plasmids consists of OR10G9-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double
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olfr201 crispr/cas9 ko plasmid  (Santa Cruz Biotechnology)
N/A
Target species: mouse. CRISPR/Cas9 KO Plasmids consists of Olfr201-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double
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olfr202 crispr/cas9 ko plasmid  (Santa Cruz Biotechnology)
N/A
Target species: mouse. CRISPR/Cas9 KO Plasmids consists of Olfr202-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double
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Image Search Results


Figure 1. Structure-function study of the N and C terminus of ERFE. A, diagram of the human ERFE protein showing the signal sequence, N-terminal, and C-terminal domains, and their respective amino acid boundaries. B, AlphaFold2 model of human ERFE structure (left; colors correspond to segments in the diagram A and right; colored by confidence parameter pLDDT, blue = highest degree of confidence). C, amino acid conservation alignments of ERFE N- terminal and C-terminal domains across vertebrate species. D, top: diagrams of full-length, N terminus, and C terminus ERFE constructs that were used in bioassay and SPR. Bottom: qPCR expression of hepcidin in Hep3B cells treated with a range of concentrations of ERFE variants for 16 h. Data are normalized to untreated controls. N = 3 biological replicates. E, surface plasmon resonance sensorgrams of full-length, N-terminal, and C-terminal ERFE binding to immobilized BMP2, BMP6, and BMP2/6. BMP, bone morphogenetic protein; ERFE, erythroferrone; pLDDT, predicted local distance difference test; SPR, surface plasmon resonance.

Journal: The Journal of biological chemistry

Article Title: Characterization of erythroferrone structural domains relevant to its iron-regulatory function.

doi: 10.1016/j.jbc.2023.105374

Figure Lengend Snippet: Figure 1. Structure-function study of the N and C terminus of ERFE. A, diagram of the human ERFE protein showing the signal sequence, N-terminal, and C-terminal domains, and their respective amino acid boundaries. B, AlphaFold2 model of human ERFE structure (left; colors correspond to segments in the diagram A and right; colored by confidence parameter pLDDT, blue = highest degree of confidence). C, amino acid conservation alignments of ERFE N- terminal and C-terminal domains across vertebrate species. D, top: diagrams of full-length, N terminus, and C terminus ERFE constructs that were used in bioassay and SPR. Bottom: qPCR expression of hepcidin in Hep3B cells treated with a range of concentrations of ERFE variants for 16 h. Data are normalized to untreated controls. N = 3 biological replicates. E, surface plasmon resonance sensorgrams of full-length, N-terminal, and C-terminal ERFE binding to immobilized BMP2, BMP6, and BMP2/6. BMP, bone morphogenetic protein; ERFE, erythroferrone; pLDDT, predicted local distance difference test; SPR, surface plasmon resonance.

Article Snippet: For the SPR competition assay, Activin RIIA-Fc (#340-RC2100), BMPRIA/ALK3-Fc (#2406-BR-100), BMPRII-Fc (#811-BR-100), Activin RIA/ALK2-Fc (#637-AR-100), Activin RIIB-Fc (#339-RB-100/CF), human IgG1-Fc for control (#110- HG-100), BMP2/6 (#7145-BP-010/CF), BMP2 (#355-BM-010/ CF), and BMP6 (507-BP-020/CF) were all obtained from RND Systems.

Techniques: Sequencing, Construct, Bioassay, Expressing, SPR Assay, Binding Assay

Figure 6. ERFE and BMP receptors bind BMPs in a similar manner. A, crystallography-resolved structure of BMP2 homodimer bound to ALK3 (PDB: 2QJ9). Callout box enlarges the interaction and identifies the contacting residues. B, AlphaFold2 model of a BMP2 homodimer (tan color) bound to ERFE colored by segment (left) and confidence pLDDT (right). Callout box shows the analogous interaction that BMPs have with their receptors. C, surface plasmon reso- nance sensorgrams of competition between WT ERFE, W82A ERFE, and activin RIIA for BMP2 (left) and BMP6 (right) binding. Extracellular portions of activin RIIA were immobilized, and BMP analyte flowed over alone or mixed with WT or W82A ERFE N-terminal segments. D, surface plasmon resonance of the ERFE N terminus binding to extracellular portions of five BMP receptors. BMP, bone morphogenetic protein; ERFE, erythroferrone; pLDDT, predicted local distance difference test.

Journal: The Journal of biological chemistry

Article Title: Characterization of erythroferrone structural domains relevant to its iron-regulatory function.

doi: 10.1016/j.jbc.2023.105374

Figure Lengend Snippet: Figure 6. ERFE and BMP receptors bind BMPs in a similar manner. A, crystallography-resolved structure of BMP2 homodimer bound to ALK3 (PDB: 2QJ9). Callout box enlarges the interaction and identifies the contacting residues. B, AlphaFold2 model of a BMP2 homodimer (tan color) bound to ERFE colored by segment (left) and confidence pLDDT (right). Callout box shows the analogous interaction that BMPs have with their receptors. C, surface plasmon reso- nance sensorgrams of competition between WT ERFE, W82A ERFE, and activin RIIA for BMP2 (left) and BMP6 (right) binding. Extracellular portions of activin RIIA were immobilized, and BMP analyte flowed over alone or mixed with WT or W82A ERFE N-terminal segments. D, surface plasmon resonance of the ERFE N terminus binding to extracellular portions of five BMP receptors. BMP, bone morphogenetic protein; ERFE, erythroferrone; pLDDT, predicted local distance difference test.

Article Snippet: For the SPR competition assay, Activin RIIA-Fc (#340-RC2100), BMPRIA/ALK3-Fc (#2406-BR-100), BMPRII-Fc (#811-BR-100), Activin RIA/ALK2-Fc (#637-AR-100), Activin RIIB-Fc (#339-RB-100/CF), human IgG1-Fc for control (#110- HG-100), BMP2/6 (#7145-BP-010/CF), BMP2 (#355-BM-010/ CF), and BMP6 (507-BP-020/CF) were all obtained from RND Systems.

Techniques: Binding Assay, SPR Assay