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biotinylated recombinant human psma  (R&D Systems)


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    R&D Systems biotinylated recombinant human psma
    Biotinylated Recombinant Human Psma, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/biotinylated+recombinant+human+lif/Recombinant+Human+LIF%2C+Biotinylated+Protein/us12534505-1040-9-13
    Average 94 stars, based on 4 article reviews
    biotinylated recombinant human psma - by Bioz Stars, 2026-09
    94/100 stars

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    Related Articles

    Recombinant:

    Article Title: Repositioning Mifepristone as a Leukaemia Inhibitory Factor Receptor Antagonist for the Treatment of Pancreatic Adenocarcinoma.
    Article Snippet: .. Recombinant human LIFR (His Tag) and biotinylated recombinant human LIF were purchased from Sino Biologicals (Sino Biological Europe GmbH, Dusseldorf, Germany) and R&D Systems (Abingdon, UK), respectively, and both were reconstituted as required by the manufacturer. ..

    Article Title: Endotoxin down-regulates monocyte and granulocyte interleukin-6 receptors without influencing gp130 expression in humans.
    Article Snippet: To correct for aspecific staining, we used an appropriate control antibody (murine IgG1; Becton Dickinson). .. Saturation binding of LIF by white blood cells was determined with biotinylated recombinant human LIF (Fluorokine; R&D Systems). ..

    Binding Assay:

    Article Title: Endotoxin down-regulates monocyte and granulocyte interleukin-6 receptors without influencing gp130 expression in humans.
    Article Snippet: To correct for aspecific staining, we used an appropriate control antibody (murine IgG1; Becton Dickinson). .. Saturation binding of LIF by white blood cells was determined with biotinylated recombinant human LIF (Fluorokine; R&D Systems). ..



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    Figure 4. Modelling. (A) hLIFR-ID01 complex. The protein backbone is displayed in ribbon and coloured by distinguishing the five domains (D1–D5). In the zoom view, (I) the ID01 binding mode of mifepristone (displayed as yellow ball and stick), highlighting the “T-inverted” shape; (II) the “T-inverted” shape well-fit with hLIFR surface; (III) the main residues involved in the interactions with the mifepristone; (IV) the hydrophobic (yellow) and hydrogen bond acceptor (red) maps fit with mifepristone. The principal residues are labelled and highlighted in wireframe or CPK(A3), while hydrogen bonds are in dashed black lines. (B) Superimposition between the ID01 best MM/GBSA value pose (black) and the <t>mLIFR-hLIF</t> X-ray (PDB ID: 2Q7N) (cyan). The three loops L1 (255-VSASSG-260), L2 (303-NPGRVTALVGPRAT-316), and L3 (332-KRAEAPTNES-341) are highlighted in yellow, blue, and green, respectively. The red rectangle highlights the clash with the propyne moiety of mifepristone and hLIF. (C) Two-dimensional structures of mifepristone. (D) The root means square fluctuation (RMSF) plot of the three compared systems (ID01 complex, hLIFR-hLIF, and hLIFR) during 100 ns of MDs.
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    Figure 4. Modelling. (A) hLIFR-ID01 complex. The protein backbone is displayed in ribbon and coloured by distinguishing the five domains (D1–D5). In the zoom view, (I) the ID01 binding mode of mifepristone (displayed as yellow ball and stick), highlighting the “T-inverted” shape; (II) the “T-inverted” shape well-fit with hLIFR surface; (III) the main residues involved in the interactions with the mifepristone; (IV) the hydrophobic (yellow) and hydrogen bond acceptor (red) maps fit with mifepristone. The principal residues are labelled and highlighted in wireframe or CPK(A3), while hydrogen bonds are in dashed black lines. (B) Superimposition between the ID01 best MM/GBSA value pose (black) and the <t>mLIFR-hLIF</t> X-ray (PDB ID: 2Q7N) (cyan). The three loops L1 (255-VSASSG-260), L2 (303-NPGRVTALVGPRAT-316), and L3 (332-KRAEAPTNES-341) are highlighted in yellow, blue, and green, respectively. The red rectangle highlights the clash with the propyne moiety of mifepristone and hLIF. (C) Two-dimensional structures of mifepristone. (D) The root means square fluctuation (RMSF) plot of the three compared systems (ID01 complex, hLIFR-hLIF, and hLIFR) during 100 ns of MDs.
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    Image Search Results


    Figure 4. Modelling. (A) hLIFR-ID01 complex. The protein backbone is displayed in ribbon and coloured by distinguishing the five domains (D1–D5). In the zoom view, (I) the ID01 binding mode of mifepristone (displayed as yellow ball and stick), highlighting the “T-inverted” shape; (II) the “T-inverted” shape well-fit with hLIFR surface; (III) the main residues involved in the interactions with the mifepristone; (IV) the hydrophobic (yellow) and hydrogen bond acceptor (red) maps fit with mifepristone. The principal residues are labelled and highlighted in wireframe or CPK(A3), while hydrogen bonds are in dashed black lines. (B) Superimposition between the ID01 best MM/GBSA value pose (black) and the mLIFR-hLIF X-ray (PDB ID: 2Q7N) (cyan). The three loops L1 (255-VSASSG-260), L2 (303-NPGRVTALVGPRAT-316), and L3 (332-KRAEAPTNES-341) are highlighted in yellow, blue, and green, respectively. The red rectangle highlights the clash with the propyne moiety of mifepristone and hLIF. (C) Two-dimensional structures of mifepristone. (D) The root means square fluctuation (RMSF) plot of the three compared systems (ID01 complex, hLIFR-hLIF, and hLIFR) during 100 ns of MDs.

    Journal: Cells

    Article Title: Repositioning Mifepristone as a Leukaemia Inhibitory Factor Receptor Antagonist for the Treatment of Pancreatic Adenocarcinoma.

    doi: 10.3390/cells11213482

    Figure Lengend Snippet: Figure 4. Modelling. (A) hLIFR-ID01 complex. The protein backbone is displayed in ribbon and coloured by distinguishing the five domains (D1–D5). In the zoom view, (I) the ID01 binding mode of mifepristone (displayed as yellow ball and stick), highlighting the “T-inverted” shape; (II) the “T-inverted” shape well-fit with hLIFR surface; (III) the main residues involved in the interactions with the mifepristone; (IV) the hydrophobic (yellow) and hydrogen bond acceptor (red) maps fit with mifepristone. The principal residues are labelled and highlighted in wireframe or CPK(A3), while hydrogen bonds are in dashed black lines. (B) Superimposition between the ID01 best MM/GBSA value pose (black) and the mLIFR-hLIF X-ray (PDB ID: 2Q7N) (cyan). The three loops L1 (255-VSASSG-260), L2 (303-NPGRVTALVGPRAT-316), and L3 (332-KRAEAPTNES-341) are highlighted in yellow, blue, and green, respectively. The red rectangle highlights the clash with the propyne moiety of mifepristone and hLIF. (C) Two-dimensional structures of mifepristone. (D) The root means square fluctuation (RMSF) plot of the three compared systems (ID01 complex, hLIFR-hLIF, and hLIFR) during 100 ns of MDs.

    Article Snippet: Recombinant human LIFR (His Tag) and biotinylated recombinant human LIF were purchased from Sino Biologicals (Sino Biological Europe GmbH, Dusseldorf, Germany) and R&D Systems (Abingdon, UK), respectively, and both were reconstituted as required by the manufacturer.

    Techniques: Binding Assay