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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/lif+biotinylated/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, 2026-11
    94/100 stars

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    Recombinant:

    Article Title: Exploring Boswellia serrata Triterpenes: A New Frontier in Leukemia Inhibitory Factor Receptor Modulation
    Article Snippet: .. Recombinant human LIFR (His-Tag) and LIF (biotinylated) 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. .. Inhibition of LIFR/LIF binding was measured by Alpha Screen, in white, low-volume, 384-well AlphaPlates (Revvity, Italy) using a final volume of 15 μL and an assay buffer containing 25 mM Hepes (pH 7.4), 100 mM NaCl, and 0.005% Kathon.

    Article Title: Harnessing the Estradienone Scaffold to Develop Dual GPBAR1 and LIFR Modulators for Liver Fibrosis
    Article Snippet: .. Recombinant human LIFR (His-Tag) and LIF (biotinylated) 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. .. Inhibition of LIFR/LIF binding was measured by AlphaScreen, in white, low-volume, 384-well AlphaPlates (PerkinElmer, Waltham, MA, USA) using a final volume of 15 μL and an assay buffer containing 25 mM Hepes (pH 7.4), 100 mM NaCl, and 0.005% Kathon.

    Article Title: Harnessing the Estradienone Scaffold to Develop Dual GPBAR1 and LIFR Modulators for Liver Fibrosis.
    Article Snippet: .. Recombinant human LIFR (His-Tag) and LIF (biotinylated) 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. .. Inhibition of LIFR/LIF binding was measured by AlphaScreen, in white, low-volume, 384-well AlphaPlates (PerkinElmer, Waltham, MA, USA) using a final volume of 15 μL and an assay buffer containing 25 mM Hepes (pH 7.4), 100 mM NaCl, and 0.005% Kathon.



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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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    ELISA analysis of recombinant antibody binding to hLIF and mLIF

    Journal: BMC Immunology

    Article Title: Antagonist anti-LIF antibody derived from naive human scFv phage library inhibited tumor growth in mice

    doi: 10.1186/s12865-024-00636-w

    Figure Lengend Snippet: ELISA analysis of recombinant antibody binding to hLIF and mLIF

    Article Snippet: The other recombinant protein sources were as follows: human LIF (Z02681, Genscript, China), biotinylated human LIF (LIF-H82E2, Acrobiosystems, China), mouse LIF (250-02, PeproTech, USA), cynomolgus LIF (RP1074Y-100, Kingfisher Biotech, USA), human LIFR-his (10,628-H08H, Sino Biological, China), and human gp130-his (10,974-HCCH, Sino Biological, China).

    Techniques: Enzyme-linked Immunosorbent Assay, Recombinant, Binding Assay

    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