trypsin  (New England Biolabs)


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    New England Biolabs trypsin
    Trypsin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    trypsin  (New England Biolabs)


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    New England Biolabs trypsin
    Trypsin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    trypsin  (New England Biolabs)


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  • 94

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    New England Biolabs trypsin
    Trypsin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/trypsin/product/New England Biolabs
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    trypsin  (New England Biolabs)


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  • 86

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    New England Biolabs trypsin
    Trypsin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    prototype serine endopeptidase trypsin  (New England Biolabs)


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    New England Biolabs prototype serine endopeptidase trypsin
    Prototype Serine Endopeptidase Trypsin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    trypsin  (New England Biolabs)


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  • 94

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    New England Biolabs trypsin
    Trypsin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/trypsin/product/New England Biolabs
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    serum albumin  (New England Biolabs)


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    New England Biolabs serum albumin
    Serum Albumin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human trypsin isoforms  (New England Biolabs)


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    New England Biolabs human trypsin isoforms
    SPINK1 sequence and structure conservation. (A) Phylogenetic analysis of trypsin-targeting SPINK1 homologues. Duplicates indicate different <t>isoforms</t> within the same species. SPINK1 variants featuring arginine as the P1 residue are highlighted in red. (B) Structure of the canonical binding loop (PDB ID: 7QE8 ) colored according to conservation using the multiple sequence alignment from (A). Conservation scores were determined using the ConSurf server. (C) Multiple sequence alignment of selected SPINK1 variants and consensus sequences of (A) subclustered according to P1 residues. (D) Structure of binding pockets in trypsin. The S1 pocket is highlighted in red, the oxyanion hole in blue, and L104 interacting with the P2 residue in gray.
    Human Trypsin Isoforms, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human trypsin isoforms/product/New England Biolabs
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    1) Product Images from "Identification of Kazal Inhibitor Scaffolds with Identical Canonical Binding Loops and Their Effects on Binding Properties"

    Article Title: Identification of Kazal Inhibitor Scaffolds with Identical Canonical Binding Loops and Their Effects on Binding Properties

    Journal: Biochemistry

    doi: 10.1021/acs.biochem.2c00573

    SPINK1 sequence and structure conservation. (A) Phylogenetic analysis of trypsin-targeting SPINK1 homologues. Duplicates indicate different isoforms within the same species. SPINK1 variants featuring arginine as the P1 residue are highlighted in red. (B) Structure of the canonical binding loop (PDB ID: 7QE8 ) colored according to conservation using the multiple sequence alignment from (A). Conservation scores were determined using the ConSurf server. (C) Multiple sequence alignment of selected SPINK1 variants and consensus sequences of (A) subclustered according to P1 residues. (D) Structure of binding pockets in trypsin. The S1 pocket is highlighted in red, the oxyanion hole in blue, and L104 interacting with the P2 residue in gray.
    Figure Legend Snippet: SPINK1 sequence and structure conservation. (A) Phylogenetic analysis of trypsin-targeting SPINK1 homologues. Duplicates indicate different isoforms within the same species. SPINK1 variants featuring arginine as the P1 residue are highlighted in red. (B) Structure of the canonical binding loop (PDB ID: 7QE8 ) colored according to conservation using the multiple sequence alignment from (A). Conservation scores were determined using the ConSurf server. (C) Multiple sequence alignment of selected SPINK1 variants and consensus sequences of (A) subclustered according to P1 residues. (D) Structure of binding pockets in trypsin. The S1 pocket is highlighted in red, the oxyanion hole in blue, and L104 interacting with the P2 residue in gray.

    Techniques Used: Sequencing, Binding Assay

    serum albumin  (New England Biolabs)


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    New England Biolabs serum albumin
    Serum Albumin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    trypsin  (New England Biolabs)


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    New England Biolabs trypsin
    Trypsin, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    trypsination  (New England Biolabs)


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    New England Biolabs trypsination
    Trypsination, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs human trypsin isoforms
    SPINK1 sequence and structure conservation. (A) Phylogenetic analysis of trypsin-targeting SPINK1 homologues. Duplicates indicate different <t>isoforms</t> within the same species. SPINK1 variants featuring arginine as the P1 residue are highlighted in red. (B) Structure of the canonical binding loop (PDB ID: 7QE8 ) colored according to conservation using the multiple sequence alignment from (A). Conservation scores were determined using the ConSurf server. (C) Multiple sequence alignment of selected SPINK1 variants and consensus sequences of (A) subclustered according to P1 residues. (D) Structure of binding pockets in trypsin. The S1 pocket is highlighted in red, the oxyanion hole in blue, and L104 interacting with the P2 residue in gray.
    Human Trypsin Isoforms, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs trypsination
    SPINK1 sequence and structure conservation. (A) Phylogenetic analysis of trypsin-targeting SPINK1 homologues. Duplicates indicate different <t>isoforms</t> within the same species. SPINK1 variants featuring arginine as the P1 residue are highlighted in red. (B) Structure of the canonical binding loop (PDB ID: 7QE8 ) colored according to conservation using the multiple sequence alignment from (A). Conservation scores were determined using the ConSurf server. (C) Multiple sequence alignment of selected SPINK1 variants and consensus sequences of (A) subclustered according to P1 residues. (D) Structure of binding pockets in trypsin. The S1 pocket is highlighted in red, the oxyanion hole in blue, and L104 interacting with the P2 residue in gray.
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    Image Search Results


    SPINK1 sequence and structure conservation. (A) Phylogenetic analysis of trypsin-targeting SPINK1 homologues. Duplicates indicate different isoforms within the same species. SPINK1 variants featuring arginine as the P1 residue are highlighted in red. (B) Structure of the canonical binding loop (PDB ID: 7QE8 ) colored according to conservation using the multiple sequence alignment from (A). Conservation scores were determined using the ConSurf server. (C) Multiple sequence alignment of selected SPINK1 variants and consensus sequences of (A) subclustered according to P1 residues. (D) Structure of binding pockets in trypsin. The S1 pocket is highlighted in red, the oxyanion hole in blue, and L104 interacting with the P2 residue in gray.

    Journal: Biochemistry

    Article Title: Identification of Kazal Inhibitor Scaffolds with Identical Canonical Binding Loops and Their Effects on Binding Properties

    doi: 10.1021/acs.biochem.2c00573

    Figure Lengend Snippet: SPINK1 sequence and structure conservation. (A) Phylogenetic analysis of trypsin-targeting SPINK1 homologues. Duplicates indicate different isoforms within the same species. SPINK1 variants featuring arginine as the P1 residue are highlighted in red. (B) Structure of the canonical binding loop (PDB ID: 7QE8 ) colored according to conservation using the multiple sequence alignment from (A). Conservation scores were determined using the ConSurf server. (C) Multiple sequence alignment of selected SPINK1 variants and consensus sequences of (A) subclustered according to P1 residues. (D) Structure of binding pockets in trypsin. The S1 pocket is highlighted in red, the oxyanion hole in blue, and L104 interacting with the P2 residue in gray.

    Article Snippet: Human trypsin isoforms were expressed in E. coli BL21 (DE3) (New England Biolabs) overnight at 30 °C.

    Techniques: Sequencing, Binding Assay