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human ncad protein  (Sino Biological)


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  • 93

    Structured Review

    Sino Biological human ncad protein
    (A) Four pairs of <t>anti-Ncad</t> antibody fragments were analyzed by Superdex 75 size-exclusion chromatography. <t>The</t> <t>17aa-linker</t> and the 7aa-linker worked best for the A1 and G6 clones. For the A6 clone, the 7aa-linker diabody formed a mixture of monomer and dimer. For the D6 clone, the 17aa-linker scFv formed a mixture of monomer and dimer. (B) Four random clones from the 18aa-SX-scFv library were reformatted, expressed and purified. The 5aa-linker successfully induced dimerization for all these clones.
    Human Ncad Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+ncad+protein/pmc04607741-88-13-23?v=Sino+Biological
    Average 93 stars, based on 6 article reviews
    human ncad protein - by Bioz Stars, 2026-08
    93/100 stars

    Images

    1) Product Images from "A fully human scFv phage display library for rapid antibody fragment reformatting"

    Article Title: A fully human scFv phage display library for rapid antibody fragment reformatting

    Journal: Protein Engineering, Design and Selection

    doi: 10.1093/protein/gzv024

    (A) Four pairs of anti-Ncad antibody fragments were analyzed by Superdex 75 size-exclusion chromatography. The 17aa-linker and the 7aa-linker worked best for the A1 and G6 clones. For the A6 clone, the 7aa-linker diabody formed a mixture of monomer and dimer. For the D6 clone, the 17aa-linker scFv formed a mixture of monomer and dimer. (B) Four random clones from the 18aa-SX-scFv library were reformatted, expressed and purified. The 5aa-linker successfully induced dimerization for all these clones.
    Figure Legend Snippet: (A) Four pairs of anti-Ncad antibody fragments were analyzed by Superdex 75 size-exclusion chromatography. The 17aa-linker and the 7aa-linker worked best for the A1 and G6 clones. For the A6 clone, the 7aa-linker diabody formed a mixture of monomer and dimer. For the D6 clone, the 17aa-linker scFv formed a mixture of monomer and dimer. (B) Four random clones from the 18aa-SX-scFv library were reformatted, expressed and purified. The 5aa-linker successfully induced dimerization for all these clones.

    Techniques Used: Size-exclusion Chromatography, Clone Assay, Purification



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    Image Search Results


    (A) Four pairs of anti-Ncad antibody fragments were analyzed by Superdex 75 size-exclusion chromatography. The 17aa-linker and the 7aa-linker worked best for the A1 and G6 clones. For the A6 clone, the 7aa-linker diabody formed a mixture of monomer and dimer. For the D6 clone, the 17aa-linker scFv formed a mixture of monomer and dimer. (B) Four random clones from the 18aa-SX-scFv library were reformatted, expressed and purified. The 5aa-linker successfully induced dimerization for all these clones.

    Journal: Protein Engineering, Design and Selection

    Article Title: A fully human scFv phage display library for rapid antibody fragment reformatting

    doi: 10.1093/protein/gzv024

    Figure Lengend Snippet: (A) Four pairs of anti-Ncad antibody fragments were analyzed by Superdex 75 size-exclusion chromatography. The 17aa-linker and the 7aa-linker worked best for the A1 and G6 clones. For the A6 clone, the 7aa-linker diabody formed a mixture of monomer and dimer. For the D6 clone, the 17aa-linker scFv formed a mixture of monomer and dimer. (B) Four random clones from the 18aa-SX-scFv library were reformatted, expressed and purified. The 5aa-linker successfully induced dimerization for all these clones.

    Article Snippet: Phage library selection The 17aa-SSA-scFv library was used for the selections against the human Ncad protein (extracellular domain fused to C-terminal polyhistidine tag, Sino Biological, cat#: 11039-H08H) using previously published methods ( Marks and Bradbury, 2004 ).

    Techniques: Size-exclusion Chromatography, Clone Assay, Purification