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biotinylated hfcrn  (ACROBiosystems)


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    ACROBiosystems biotinylated hfcrn
    Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn <t>(hFcRn)</t> binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.
    Biotinylated Hfcrn, supplied by ACROBiosystems, used in various techniques. Bioz Stars score: 95/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fcm-h82w4-25ug/pm37408314-152-0-2?v=ACROBiosystems
    Average 95 stars, based on 10 article reviews
    biotinylated hfcrn - by Bioz Stars, 2026-08
    95/100 stars

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    1) Product Images from "Improved antibody pharmacokinetics by disruption of contiguous positive surface potential and charge reduction using alternate human framework."

    Article Title: Improved antibody pharmacokinetics by disruption of contiguous positive surface potential and charge reduction using alternate human framework.

    Journal: mAbs

    doi: 10.1080/19420862.2023.2232087

    Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn (hFcRn) binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.
    Figure Legend Snippet: Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn (hFcRn) binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Residue



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    Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn <t>(hFcRn)</t> binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.
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    Image Search Results


    Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn (hFcRn) binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.

    Journal: mAbs

    Article Title: Improved antibody pharmacokinetics by disruption of contiguous positive surface potential and charge reduction using alternate human framework.

    doi: 10.1080/19420862.2023.2232087

    Figure Lengend Snippet: Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn (hFcRn) binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.

    Article Snippet: Biotinylated hFcRn (AcroBiosystems, cat # FCMH82W4) was immobilized on flow-cell 2 (fc2) of flowchannels 1 to 8 of a streptavidin (SA) sensor chip (Cytiva, cat# BR-1005-31) to reach a final surface density of approximatively 150 RU.

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