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human recombinant lsd1 protein  (BPS Bioscience)


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    Structured Review

    BPS Bioscience human recombinant lsd1 protein
    Human Recombinant Lsd1 Protein, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human recombinant lsd1 protein/product/BPS Bioscience
    Average 90 stars, based on 16 article reviews
    human recombinant lsd1 protein - by Bioz Stars, 2026-02
    90/100 stars

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    Image Search Results


    Structures of published LSD1 inhibitors.

    Journal: Frontiers in Pharmacology

    Article Title: Discovery of highly potent and novel LSD1 inhibitors for the treatment of acute myeloid leukemia: structure-based virtual screening, molecular dynamics simulation, and biological evaluation

    doi: 10.3389/fphar.2025.1510319

    Figure Lengend Snippet: Structures of published LSD1 inhibitors.

    Article Snippet: Recombinant human LSD1 (172–852 aa) and full-length LSD2 were obtained from Sino Biological Inc. and ActiveMotif.

    Techniques:

    Pharmacophore model based on LSD1. (A) Details of pharmacophore model features. Hydrogen-bond donor (F1) is represented by magenta sphere, hydrophobic feature (F2) is depicted by yellow sphere, and aromatic center (F3) is illustrated by brown sphere. Each critical amino acid is represented by a pink stick model and annotated with a three-letter amino acid code. Hydrogen bonds are depicted with black dashed lines. (B) Spatial constraints of the pharmacophore model within the LSD1 active site.

    Journal: Frontiers in Pharmacology

    Article Title: Discovery of highly potent and novel LSD1 inhibitors for the treatment of acute myeloid leukemia: structure-based virtual screening, molecular dynamics simulation, and biological evaluation

    doi: 10.3389/fphar.2025.1510319

    Figure Lengend Snippet: Pharmacophore model based on LSD1. (A) Details of pharmacophore model features. Hydrogen-bond donor (F1) is represented by magenta sphere, hydrophobic feature (F2) is depicted by yellow sphere, and aromatic center (F3) is illustrated by brown sphere. Each critical amino acid is represented by a pink stick model and annotated with a three-letter amino acid code. Hydrogen bonds are depicted with black dashed lines. (B) Spatial constraints of the pharmacophore model within the LSD1 active site.

    Article Snippet: Recombinant human LSD1 (172–852 aa) and full-length LSD2 were obtained from Sino Biological Inc. and ActiveMotif.

    Techniques:

    A flowchart of the identification of LSD1 inhibitors via an integrated strategy of in silico screening and biological evaluation.

    Journal: Frontiers in Pharmacology

    Article Title: Discovery of highly potent and novel LSD1 inhibitors for the treatment of acute myeloid leukemia: structure-based virtual screening, molecular dynamics simulation, and biological evaluation

    doi: 10.3389/fphar.2025.1510319

    Figure Lengend Snippet: A flowchart of the identification of LSD1 inhibitors via an integrated strategy of in silico screening and biological evaluation.

    Article Snippet: Recombinant human LSD1 (172–852 aa) and full-length LSD2 were obtained from Sino Biological Inc. and ActiveMotif.

    Techniques: In Silico

    The inhibitory activities of LTMs 1–6 against  LSD1  and LSD2.

    Journal: Frontiers in Pharmacology

    Article Title: Discovery of highly potent and novel LSD1 inhibitors for the treatment of acute myeloid leukemia: structure-based virtual screening, molecular dynamics simulation, and biological evaluation

    doi: 10.3389/fphar.2025.1510319

    Figure Lengend Snippet: The inhibitory activities of LTMs 1–6 against LSD1 and LSD2.

    Article Snippet: Recombinant human LSD1 (172–852 aa) and full-length LSD2 were obtained from Sino Biological Inc. and ActiveMotif.

    Techniques:

    The predicted docking poses and binding surface of LTM-1 and LTM-3 in the active site of LSD1, respectively. (A) and (B) represent LTM-1; (C, D) represent LTM-3. The structure of LTM-1 is represented by cyan sticks. The structure of LTM-3 is depicted by yellow sticks. Key amino acids in the active site are represented by pink sticks and annotated with three-letter amino acid codes. The surface of the LSD1 protein is rendered with hydrogen bond regions (purple), hydrophobic regions (green), and moderately polar regions (blue).

    Journal: Frontiers in Pharmacology

    Article Title: Discovery of highly potent and novel LSD1 inhibitors for the treatment of acute myeloid leukemia: structure-based virtual screening, molecular dynamics simulation, and biological evaluation

    doi: 10.3389/fphar.2025.1510319

    Figure Lengend Snippet: The predicted docking poses and binding surface of LTM-1 and LTM-3 in the active site of LSD1, respectively. (A) and (B) represent LTM-1; (C, D) represent LTM-3. The structure of LTM-1 is represented by cyan sticks. The structure of LTM-3 is depicted by yellow sticks. Key amino acids in the active site are represented by pink sticks and annotated with three-letter amino acid codes. The surface of the LSD1 protein is rendered with hydrogen bond regions (purple), hydrophobic regions (green), and moderately polar regions (blue).

    Article Snippet: Recombinant human LSD1 (172–852 aa) and full-length LSD2 were obtained from Sino Biological Inc. and ActiveMotif.

    Techniques: Binding Assay

    MD simulation of LSD1 in complex with LTM-1. (A) RMSD of LSD1-LTM-1 complex. (B) RMSF of LSD1 residues in LSD1-LTM-1 complex. (C) Rg of LSD1 in the complex of LSD1-LTM-1. (D) The conformational changes induced upon binding of the LTM-1 (represented in cyan) to the LSD1 protein (represented in green and gray). The data are presented as the mean ± SD, n = 3. Error bars representing the standard deviation are indicated by red dashed lines.

    Journal: Frontiers in Pharmacology

    Article Title: Discovery of highly potent and novel LSD1 inhibitors for the treatment of acute myeloid leukemia: structure-based virtual screening, molecular dynamics simulation, and biological evaluation

    doi: 10.3389/fphar.2025.1510319

    Figure Lengend Snippet: MD simulation of LSD1 in complex with LTM-1. (A) RMSD of LSD1-LTM-1 complex. (B) RMSF of LSD1 residues in LSD1-LTM-1 complex. (C) Rg of LSD1 in the complex of LSD1-LTM-1. (D) The conformational changes induced upon binding of the LTM-1 (represented in cyan) to the LSD1 protein (represented in green and gray). The data are presented as the mean ± SD, n = 3. Error bars representing the standard deviation are indicated by red dashed lines.

    Article Snippet: Recombinant human LSD1 (172–852 aa) and full-length LSD2 were obtained from Sino Biological Inc. and ActiveMotif.

    Techniques: Binding Assay, Standard Deviation