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phospho trka tyr490 polyclonal antibody  (Bioss)


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    Bioss phospho trka tyr490 polyclonal antibody
    Phospho Trka Tyr490 Polyclonal Antibody, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/trka/TrkA+(Tyr490)+Polyclonal+Antibody/10__1016_slash_j__foodres__2026__119089-123-7-12
    Average 94 stars, based on 2 article reviews
    phospho trka tyr490 polyclonal antibody - by Bioz Stars, 2026-09
    94/100 stars

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    Western Blot:

    Article Title: Nociceptive sensory neuron-derived NGF orchestrates a fibrotic mesenchymal stromal cell neurogenic niche to drive tendon pathological fibrosis
    Article Snippet: .. The adhesion grading scale and healing grading scale were assessed as before. (Supplementary Fig. ; Supplementary Fig. ) The primary antibodies used in this section were as follows: α-smooth muscle actin (αSMA, Cell Signaling, 19245 and 48938, 1:200); calcitonin gene-related peptide (CGRP, Cell Signaling, 14959, 1:200); nerve growth factor (NGF, Abcam, 52918, 1:150); neuron nucleus (NeuN, Cell Signaling, 94403 s, 1:100); Nestin (Aves Labs, NES, 1:200); TrkA (BIOSS, bs-0193R, 1:200); and Hif1α (NOVUS, H1alpha67, 1:300); Prrx1(NOVUS, NBP1-06067, 1:200); Collagen 1(Abcam, 138492, 1:200 for IF, 1:500 for WB); Collagen 3(Abcam, 184993, 1:200 for IF, 1:500 for WB); PGP9.5(Cell Signaling, 60702, 1:200); VHL(Abcam, 140989, 1:500); Engrailed-1(Sigma, AB5732, 1:200). ..

    Article Title: Nociceptive sensory neuron-derived NGF orchestrates a fibrotic mesenchymal stromal cell neurogenic niche to drive tendon pathological fibrosis.
    Article Snippet: .. The adhesion grading scale and healing grading scale were assessed as before. (SF 17A; SF 18A) The primary antibodies used in this section were as follows: α-smooth muscle actin (αSMA, Cell Signaling, 19245 and 48938, 1:200); calcitonin gene-related peptide (CGRP, Cell Signaling, 14959, 1:200); nerve growth factor (NGF, Abcam, 52918, 1:150); neuron nucleus (NeuN, Cell Signaling, 94403s, 1:100); Nestin (Aves Labs, NES, 1:200); TrkA (BIOSS, bs-0193R, 1:200); and Hif1α (NOVUS, H1alpha67, 1:300); Prrx1(NOVUS, NBP1-06067, 1:200); Collagen 1(Abcam, 138492, 1:200 for IF, 1:500 for WB); Collagen 3(Abcam, 184993, 1:200 for IF, 1:500 for WB); PGP9.5(Cell Signaling, 60702, 1:200); VHL(Abcam, 140989, 1:500);Engrailed-1(Sigma, AB5732, 1:200). ..



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    Image Search Results


    (a) Binding affinities of mAb 42F5-15 measured for human and mouse TrkA reveals strong affinity for human ortholog. (b) Structure based sequence alignment of TrkA orthologs (human and mouse) generated by superposition of structures of TrkA IgC2 domain is shown. Qualitative electrostatic surface map of TrkA Ig-C2 and 43F5-15 Fab is drawn to illustrate the presence of charge complementarity between (c) E331-R100 pair at TrkA ECD /42F5-15 Fab interface (human) and absence of the same between (d) Q333-R100 pair at putative TrkA ECD /42F5-15 Fab interface (mouse). The red and blue color of electrostatic surface map corresponds to negative and positive charges, respectively. Dashed lines at the at the TrkA ECD /42F5-15 Fab interface indicate hydrogen bonds (cyan) and ionic (orange) interactions. (e) Structure based sequence alignment of Trk isoforms (TrkA, TrkB, and TrkC) generated by superposition of structures of Trk IgC2 domain is shown. (b, e) Conserved residues are marked in white on a red background while similar residues are in red. Residues in blue frame depict similarity across groups. Secondary structural elements and residue numbering indicated above the alignment are extracted from the structure of TrkA IgC2 domain as observed in TrkA ECD /42F5-15 Fab complex. TrkA IgC2 residues that bind 42F5-15 Fab (epitope), as inferred from structural analysis of TrkA ECD /42F5-15 Fab complex, are indicated by colored circles below the alignment. Black and pink circles indicate conserved and variable residues at mAb 42F5-15 epitope positions across TrkA orthologs (b) and Trk isoforms (e).

    Journal: bioRxiv

    Article Title: Structural basis for direct NGF/TrkA blockade by an analgesic antibody

    doi: 10.64898/2026.06.30.735605

    Figure Lengend Snippet: (a) Binding affinities of mAb 42F5-15 measured for human and mouse TrkA reveals strong affinity for human ortholog. (b) Structure based sequence alignment of TrkA orthologs (human and mouse) generated by superposition of structures of TrkA IgC2 domain is shown. Qualitative electrostatic surface map of TrkA Ig-C2 and 43F5-15 Fab is drawn to illustrate the presence of charge complementarity between (c) E331-R100 pair at TrkA ECD /42F5-15 Fab interface (human) and absence of the same between (d) Q333-R100 pair at putative TrkA ECD /42F5-15 Fab interface (mouse). The red and blue color of electrostatic surface map corresponds to negative and positive charges, respectively. Dashed lines at the at the TrkA ECD /42F5-15 Fab interface indicate hydrogen bonds (cyan) and ionic (orange) interactions. (e) Structure based sequence alignment of Trk isoforms (TrkA, TrkB, and TrkC) generated by superposition of structures of Trk IgC2 domain is shown. (b, e) Conserved residues are marked in white on a red background while similar residues are in red. Residues in blue frame depict similarity across groups. Secondary structural elements and residue numbering indicated above the alignment are extracted from the structure of TrkA IgC2 domain as observed in TrkA ECD /42F5-15 Fab complex. TrkA IgC2 residues that bind 42F5-15 Fab (epitope), as inferred from structural analysis of TrkA ECD /42F5-15 Fab complex, are indicated by colored circles below the alignment. Black and pink circles indicate conserved and variable residues at mAb 42F5-15 epitope positions across TrkA orthologs (b) and Trk isoforms (e).

    Article Snippet: Mouse TrkA Protein was purchased from MedChemExpress (#HY-P76116).

    Techniques: Binding Assay, Sequencing, Generated, Residue