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duplicate with fap  (R&D Systems)


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    Structured Review

    R&D Systems duplicate with fap
    Figure 4. Structural model of the zalfermin <t>(15)</t> <t>FGF21</t> analog and illustration of interactions with albumin and KLB. Numbering of amino acids corresponds to human FGF21. (A) Amino acid sequence with rendition of the fatty-diacid side chain. The naturally occurring disulfide bridge between Cys75 and Cys93 is indicated by a line. Red font represents a mutation relative to human FGF21. The N-terminal is elongated by an alanine residue (−1Ala) and in-sequence mutations include Asn121Gln, Met168Leu, and Ala180Cys. A C18 diacid gGlu- OEG-OEG-C2DA-Ac side chain is attached at position 180. (B) Representative AlphaFold model of 15 shown in blue and potential interaction with albumin (orange) based on albumin−somapacitan cocrystal structure (PDB entry 6QIO). The <t>FAP</t> enzyme is colored gray, with the catalytic site and surrounding residues in magenta.
    Duplicate With Fap, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/duplicate with fap/product/R&D Systems
    Average 93 stars, based on 22 article reviews
    duplicate with fap - by Bioz Stars, 2026-04
    93/100 stars

    Images

    1) Product Images from "Development of Zalfermin, a Long-Acting Proteolytically Stabilized FGF21 Analog."

    Article Title: Development of Zalfermin, a Long-Acting Proteolytically Stabilized FGF21 Analog.

    Journal: Journal of medicinal chemistry

    doi: 10.1021/acs.jmedchem.4c00391

    Figure 4. Structural model of the zalfermin (15) FGF21 analog and illustration of interactions with albumin and KLB. Numbering of amino acids corresponds to human FGF21. (A) Amino acid sequence with rendition of the fatty-diacid side chain. The naturally occurring disulfide bridge between Cys75 and Cys93 is indicated by a line. Red font represents a mutation relative to human FGF21. The N-terminal is elongated by an alanine residue (−1Ala) and in-sequence mutations include Asn121Gln, Met168Leu, and Ala180Cys. A C18 diacid gGlu- OEG-OEG-C2DA-Ac side chain is attached at position 180. (B) Representative AlphaFold model of 15 shown in blue and potential interaction with albumin (orange) based on albumin−somapacitan cocrystal structure (PDB entry 6QIO). The FAP enzyme is colored gray, with the catalytic site and surrounding residues in magenta.
    Figure Legend Snippet: Figure 4. Structural model of the zalfermin (15) FGF21 analog and illustration of interactions with albumin and KLB. Numbering of amino acids corresponds to human FGF21. (A) Amino acid sequence with rendition of the fatty-diacid side chain. The naturally occurring disulfide bridge between Cys75 and Cys93 is indicated by a line. Red font represents a mutation relative to human FGF21. The N-terminal is elongated by an alanine residue (−1Ala) and in-sequence mutations include Asn121Gln, Met168Leu, and Ala180Cys. A C18 diacid gGlu- OEG-OEG-C2DA-Ac side chain is attached at position 180. (B) Representative AlphaFold model of 15 shown in blue and potential interaction with albumin (orange) based on albumin−somapacitan cocrystal structure (PDB entry 6QIO). The FAP enzyme is colored gray, with the catalytic site and surrounding residues in magenta.

    Techniques Used: Sequencing, Mutagenesis, Residue



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    duplicate with fap  (R&D Systems)
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    R&D Systems duplicate with fap
    Figure 4. Structural model of the zalfermin <t>(15)</t> <t>FGF21</t> analog and illustration of interactions with albumin and KLB. Numbering of amino acids corresponds to human FGF21. (A) Amino acid sequence with rendition of the fatty-diacid side chain. The naturally occurring disulfide bridge between Cys75 and Cys93 is indicated by a line. Red font represents a mutation relative to human FGF21. The N-terminal is elongated by an alanine residue (−1Ala) and in-sequence mutations include Asn121Gln, Met168Leu, and Ala180Cys. A C18 diacid gGlu- OEG-OEG-C2DA-Ac side chain is attached at position 180. (B) Representative AlphaFold model of 15 shown in blue and potential interaction with albumin (orange) based on albumin−somapacitan cocrystal structure (PDB entry 6QIO). The <t>FAP</t> enzyme is colored gray, with the catalytic site and surrounding residues in magenta.
    Duplicate With Fap, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Figure 4. Structural model of the zalfermin (15) FGF21 analog and illustration of interactions with albumin and KLB. Numbering of amino acids corresponds to human FGF21. (A) Amino acid sequence with rendition of the fatty-diacid side chain. The naturally occurring disulfide bridge between Cys75 and Cys93 is indicated by a line. Red font represents a mutation relative to human FGF21. The N-terminal is elongated by an alanine residue (−1Ala) and in-sequence mutations include Asn121Gln, Met168Leu, and Ala180Cys. A C18 diacid gGlu- OEG-OEG-C2DA-Ac side chain is attached at position 180. (B) Representative AlphaFold model of 15 shown in blue and potential interaction with albumin (orange) based on albumin−somapacitan cocrystal structure (PDB entry 6QIO). The FAP enzyme is colored gray, with the catalytic site and surrounding residues in magenta.

    Journal: Journal of medicinal chemistry

    Article Title: Development of Zalfermin, a Long-Acting Proteolytically Stabilized FGF21 Analog.

    doi: 10.1021/acs.jmedchem.4c00391

    Figure Lengend Snippet: Figure 4. Structural model of the zalfermin (15) FGF21 analog and illustration of interactions with albumin and KLB. Numbering of amino acids corresponds to human FGF21. (A) Amino acid sequence with rendition of the fatty-diacid side chain. The naturally occurring disulfide bridge between Cys75 and Cys93 is indicated by a line. Red font represents a mutation relative to human FGF21. The N-terminal is elongated by an alanine residue (−1Ala) and in-sequence mutations include Asn121Gln, Met168Leu, and Ala180Cys. A C18 diacid gGlu- OEG-OEG-C2DA-Ac side chain is attached at position 180. (B) Representative AlphaFold model of 15 shown in blue and potential interaction with albumin (orange) based on albumin−somapacitan cocrystal structure (PDB entry 6QIO). The FAP enzyme is colored gray, with the catalytic site and surrounding residues in magenta.

    Article Snippet: Five μM of FGF21 analog was incubated in duplicate with FAP (R&D Systems, 3715-SE-010) at pH 7.4 (50 mM Tris, pH 7.4, 100 mM NaCl, 0.05% Tween20) at 37 °C.

    Techniques: Sequencing, Mutagenesis, Residue