neural agrin Search Results


rat neural agrin lg3 (residues leu 1759–pro 1948  (Becton Dickinson)
90
Becton Dickinson rat neural agrin lg3 (residues leu 1759–pro 1948
Characterization of the agrin–LRP4 interaction. (A) Schematic domain organizations of rat agrin and LRP4. The boundaries of protein fragments used in this study are indicated. (NtA) N-terminal agrin domain; (FS) follistatin-like repeat; (LB) laminin-B-like domain; (S/T) serine/threonine glycosylation sites; (EG) EGF-like domain; (LG) laminin-G-like domain; (LDLa) LDL class A repeats; (YWTD) YWTD repeat-containing β propeller; (TM) transmembrane region. (B) Agrin <t>LG3</t> (residues Leu 1759–Pro 1948) forms a stable complex with LRP4V396–A737 in solution, as demonstrated by size exclusion chromatography. (C) Analytic ultracentrifugation (AUC) studies of agrin LG3, agrin LG2/LG3 (residues Leu 1481–Pro 1948), and the agrin LG3–LRP4T353–A737 complex. Agrin LG3 and LG2/LG3 are both monomeric in solution, and the agrin–LRP4 complex dimerizes with an average Kd of ∼39 μM. (Bottom panel) Absorbance data (blue dots) fit to a single-species model (LG2/LG3 and LG3) or a monomer–dimer model (agrin LG3–LRP4 complex) (red line). (Top panel) Residuals from the fit.
Rat Neural Agrin Lg3 (Residues Leu 1759–Pro 1948, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/neural+agrin/rat+neural+agrin+lg3++residues+leu+1759+pro+1948/pmc03278892-395-0-20
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rat neural agrin lg3 (residues leu 1759–pro 1948 - by Bioz Stars, 2026-10
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recombinant rat agrin protein  (Bio-Techne corporation)
95
Bio-Techne corporation recombinant rat agrin protein
Characterization of the agrin–LRP4 interaction. (A) Schematic domain organizations of rat agrin and LRP4. The boundaries of protein fragments used in this study are indicated. (NtA) N-terminal agrin domain; (FS) follistatin-like repeat; (LB) laminin-B-like domain; (S/T) serine/threonine glycosylation sites; (EG) EGF-like domain; (LG) laminin-G-like domain; (LDLa) LDL class A repeats; (YWTD) YWTD repeat-containing β propeller; (TM) transmembrane region. (B) Agrin <t>LG3</t> (residues Leu 1759–Pro 1948) forms a stable complex with LRP4V396–A737 in solution, as demonstrated by size exclusion chromatography. (C) Analytic ultracentrifugation (AUC) studies of agrin LG3, agrin LG2/LG3 (residues Leu 1481–Pro 1948), and the agrin LG3–LRP4T353–A737 complex. Agrin LG3 and LG2/LG3 are both monomeric in solution, and the agrin–LRP4 complex dimerizes with an average Kd of ∼39 μM. (Bottom panel) Absorbance data (blue dots) fit to a single-species model (LG2/LG3 and LG3) or a monomer–dimer model (agrin LG3–LRP4 complex) (red line). (Top panel) Residuals from the fit.
Recombinant Rat Agrin Protein, supplied by Bio-Techne corporation, 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/neural+agrin/Recombinant+Rat+Agrin+Protein/custom%40550-ag%4040876077
Average 95 stars, based on 1 article reviews
recombinant rat agrin protein - by Bioz Stars, 2026-10
95/100 stars
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chick neural agrin cagrin7a4b8  (BioWhittaker Molecular Applications)
90
BioWhittaker Molecular Applications chick neural agrin cagrin7a4b8
Characterization of the agrin–LRP4 interaction. (A) Schematic domain organizations of rat agrin and LRP4. The boundaries of protein fragments used in this study are indicated. (NtA) N-terminal agrin domain; (FS) follistatin-like repeat; (LB) laminin-B-like domain; (S/T) serine/threonine glycosylation sites; (EG) EGF-like domain; (LG) laminin-G-like domain; (LDLa) LDL class A repeats; (YWTD) YWTD repeat-containing β propeller; (TM) transmembrane region. (B) Agrin <t>LG3</t> (residues Leu 1759–Pro 1948) forms a stable complex with LRP4V396–A737 in solution, as demonstrated by size exclusion chromatography. (C) Analytic ultracentrifugation (AUC) studies of agrin LG3, agrin LG2/LG3 (residues Leu 1481–Pro 1948), and the agrin LG3–LRP4T353–A737 complex. Agrin LG3 and LG2/LG3 are both monomeric in solution, and the agrin–LRP4 complex dimerizes with an average Kd of ∼39 μM. (Bottom panel) Absorbance data (blue dots) fit to a single-species model (LG2/LG3 and LG3) or a monomer–dimer model (agrin LG3–LRP4 complex) (red line). (Top panel) Residuals from the fit.
Chick Neural Agrin Cagrin7a4b8, supplied by BioWhittaker Molecular Applications, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/neural+agrin/chick+neural+agrin+cagrin7a4b8/pm22644824-70-0-33
Average 90 stars, based on 1 article reviews
chick neural agrin cagrin7a4b8 - by Bioz Stars, 2026-10
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electromyography (emg) research  (MyoLearn)
99
MyoLearn electromyography (emg) research
Characterization of the agrin–LRP4 interaction. (A) Schematic domain organizations of rat agrin and LRP4. The boundaries of protein fragments used in this study are indicated. (NtA) N-terminal agrin domain; (FS) follistatin-like repeat; (LB) laminin-B-like domain; (S/T) serine/threonine glycosylation sites; (EG) EGF-like domain; (LG) laminin-G-like domain; (LDLa) LDL class A repeats; (YWTD) YWTD repeat-containing β propeller; (TM) transmembrane region. (B) Agrin <t>LG3</t> (residues Leu 1759–Pro 1948) forms a stable complex with LRP4V396–A737 in solution, as demonstrated by size exclusion chromatography. (C) Analytic ultracentrifugation (AUC) studies of agrin LG3, agrin LG2/LG3 (residues Leu 1481–Pro 1948), and the agrin LG3–LRP4T353–A737 complex. Agrin LG3 and LG2/LG3 are both monomeric in solution, and the agrin–LRP4 complex dimerizes with an average Kd of ∼39 μM. (Bottom panel) Absorbance data (blue dots) fit to a single-species model (LG2/LG3 and LG3) or a monomer–dimer model (agrin LG3–LRP4 complex) (red line). (Top panel) Residuals from the fit.
Electromyography (Emg) Research, supplied by MyoLearn, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/neural+agrin/Electromyography+(EMG)+Research/custom%40emg%4031174064
Average 99 stars, based on 1 article reviews
electromyography (emg) research - by Bioz Stars, 2026-10
99/100 stars
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Image Search Results


Characterization of the agrin–LRP4 interaction. (A) Schematic domain organizations of rat agrin and LRP4. The boundaries of protein fragments used in this study are indicated. (NtA) N-terminal agrin domain; (FS) follistatin-like repeat; (LB) laminin-B-like domain; (S/T) serine/threonine glycosylation sites; (EG) EGF-like domain; (LG) laminin-G-like domain; (LDLa) LDL class A repeats; (YWTD) YWTD repeat-containing β propeller; (TM) transmembrane region. (B) Agrin LG3 (residues Leu 1759–Pro 1948) forms a stable complex with LRP4V396–A737 in solution, as demonstrated by size exclusion chromatography. (C) Analytic ultracentrifugation (AUC) studies of agrin LG3, agrin LG2/LG3 (residues Leu 1481–Pro 1948), and the agrin LG3–LRP4T353–A737 complex. Agrin LG3 and LG2/LG3 are both monomeric in solution, and the agrin–LRP4 complex dimerizes with an average Kd of ∼39 μM. (Bottom panel) Absorbance data (blue dots) fit to a single-species model (LG2/LG3 and LG3) or a monomer–dimer model (agrin LG3–LRP4 complex) (red line). (Top panel) Residuals from the fit.

Journal: Genes & Development

Article Title: Structural basis of agrin-LRP4-MuSK signaling

doi: 10.1101/gad.180885.111

Figure Lengend Snippet: Characterization of the agrin–LRP4 interaction. (A) Schematic domain organizations of rat agrin and LRP4. The boundaries of protein fragments used in this study are indicated. (NtA) N-terminal agrin domain; (FS) follistatin-like repeat; (LB) laminin-B-like domain; (S/T) serine/threonine glycosylation sites; (EG) EGF-like domain; (LG) laminin-G-like domain; (LDLa) LDL class A repeats; (YWTD) YWTD repeat-containing β propeller; (TM) transmembrane region. (B) Agrin LG3 (residues Leu 1759–Pro 1948) forms a stable complex with LRP4V396–A737 in solution, as demonstrated by size exclusion chromatography. (C) Analytic ultracentrifugation (AUC) studies of agrin LG3, agrin LG2/LG3 (residues Leu 1481–Pro 1948), and the agrin LG3–LRP4T353–A737 complex. Agrin LG3 and LG2/LG3 are both monomeric in solution, and the agrin–LRP4 complex dimerizes with an average Kd of ∼39 μM. (Bottom panel) Absorbance data (blue dots) fit to a single-species model (LG2/LG3 and LG3) or a monomer–dimer model (agrin LG3–LRP4 complex) (red line). (Top panel) Residuals from the fit.

Article Snippet: Rat neural agrin LG3 (residues Leu 1759–Pro 1948), containing the z8 (ELTNEIPA) sequence, was subcloned into a modified pAcGP67 vector (BD Biosciences) that harbors an N-terminal six-histidine (6His) tag and a HRV 3C protease cleavage site.

Techniques: Size-exclusion Chromatography

Binary complex of agrin LG3 (agrin) and LRP4V396–A737 (LRP4). (A) The association of agrin (green) and LRP4 (orange) is mostly mediated by the neuron-specific z8 alternative splicing sequence in agrin. This loop is unambiguously defined by excellent electron densities (2Fo − Fc map contoured at 1σ) (in cyan). (B) The structure of rat agrin (green) in the context of an agrin–LRP4 complex is superimposed on the structure of an apo form of chicken agrin that also has an eight-amino-acid insert at the B/z site (magenta; PDB code 1PZ8). The arrows indicate the boundaries of the disordered z8 loop of the apo chicken agrin. (C) Stereoview of the detailed interactions between agrin (green/cyan) and LRP4 (yellow). Key residues that are directly involved in complex interactions are shown as the ball-and-stick model. Hydrogen bonds are indicated by dotted lines. (D) Open-book view of the electrostatic potential of the z8-interacting surfaces (highlighted with squares). The negatively charged z8 loop is complementary to the positively charged surface in LRP4.

Journal: Genes & Development

Article Title: Structural basis of agrin-LRP4-MuSK signaling

doi: 10.1101/gad.180885.111

Figure Lengend Snippet: Binary complex of agrin LG3 (agrin) and LRP4V396–A737 (LRP4). (A) The association of agrin (green) and LRP4 (orange) is mostly mediated by the neuron-specific z8 alternative splicing sequence in agrin. This loop is unambiguously defined by excellent electron densities (2Fo − Fc map contoured at 1σ) (in cyan). (B) The structure of rat agrin (green) in the context of an agrin–LRP4 complex is superimposed on the structure of an apo form of chicken agrin that also has an eight-amino-acid insert at the B/z site (magenta; PDB code 1PZ8). The arrows indicate the boundaries of the disordered z8 loop of the apo chicken agrin. (C) Stereoview of the detailed interactions between agrin (green/cyan) and LRP4 (yellow). Key residues that are directly involved in complex interactions are shown as the ball-and-stick model. Hydrogen bonds are indicated by dotted lines. (D) Open-book view of the electrostatic potential of the z8-interacting surfaces (highlighted with squares). The negatively charged z8 loop is complementary to the positively charged surface in LRP4.

Article Snippet: Rat neural agrin LG3 (residues Leu 1759–Pro 1948), containing the z8 (ELTNEIPA) sequence, was subcloned into a modified pAcGP67 vector (BD Biosciences) that harbors an N-terminal six-histidine (6His) tag and a HRV 3C protease cleavage site.

Techniques: Sequencing

Agrin-induced tetramerization of agrin–LRP4 is critical for AChR clustering and MuSK phosphorylation. (A) The z8 interface plays a predominant role in assembly of the agrin–LRP4 complex. GST pull-down assays were performed between GST-agrin variants (containing a HA tag) and LRP4L23–A737 (containing a His tag). Agrin and LRP4 were detected by an anti-HA antibody and an anti-His antibody, respectively. (B) MuSK phosphorylation induced by agrin variants. Fully differentiated myotubes were treated with wild-type or mutant agrin at 100 nM. MuSK was immunoprecipitated with anti-MuSK polyclonal antibody, and phosphorylation was detected by immunoblotting with anti-phosphotyrosine antibody 4G10. The bar graph shows mean ± SD, n = 3; (*) P < 0.05 in comparison with the wild-type agrin. (C) Representative images of AChR clustering (red dots) on C2C12 myotubes induced by wild-type LG3, LG3-N1783A, or LG3-H1795L. (D) Quantitative analyses of AChR clustering assay for agrin variants. Data are mean ± SD based on three independent experiments.

Journal: Genes & Development

Article Title: Structural basis of agrin-LRP4-MuSK signaling

doi: 10.1101/gad.180885.111

Figure Lengend Snippet: Agrin-induced tetramerization of agrin–LRP4 is critical for AChR clustering and MuSK phosphorylation. (A) The z8 interface plays a predominant role in assembly of the agrin–LRP4 complex. GST pull-down assays were performed between GST-agrin variants (containing a HA tag) and LRP4L23–A737 (containing a His tag). Agrin and LRP4 were detected by an anti-HA antibody and an anti-His antibody, respectively. (B) MuSK phosphorylation induced by agrin variants. Fully differentiated myotubes were treated with wild-type or mutant agrin at 100 nM. MuSK was immunoprecipitated with anti-MuSK polyclonal antibody, and phosphorylation was detected by immunoblotting with anti-phosphotyrosine antibody 4G10. The bar graph shows mean ± SD, n = 3; (*) P < 0.05 in comparison with the wild-type agrin. (C) Representative images of AChR clustering (red dots) on C2C12 myotubes induced by wild-type LG3, LG3-N1783A, or LG3-H1795L. (D) Quantitative analyses of AChR clustering assay for agrin variants. Data are mean ± SD based on three independent experiments.

Article Snippet: Rat neural agrin LG3 (residues Leu 1759–Pro 1948), containing the z8 (ELTNEIPA) sequence, was subcloned into a modified pAcGP67 vector (BD Biosciences) that harbors an N-terminal six-histidine (6His) tag and a HRV 3C protease cleavage site.

Techniques: Mutagenesis, Immunoprecipitation, Western Blot