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dh5α  (New England Biolabs)


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    New England Biolabs dh5α
    Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 2820 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 2820 article reviews
    dh5α - by Bioz Stars, 2026-06
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    UBA7 variants from individuals with neurodevelopmental disorders alter protein structure (A) Pedigrees of the families studied in this article indicate the affected individuals 1, 2, and 3. A legend is provided for the symbols used. (B) Diagram of UBA7 protein domains and their functions. The location of the identified variants in the structure is indicated. IAD: inactive adenylation domain, AAD: active adenylation domain, FCCH: first catalytic cysteine half-domain, SCCH: second catalytic cysteine half-domain, UFD: ubiquitin-fold domain. (C) Alpha-fold models of UBA7 protein resulting from UBA7 wild type, or p.Trp311∗ and p.Lys709Serfs∗45 variants. The Red helix represents the added residues resulting from the p.Lys709Serfs∗45 frameshift variant. (D) Structure of wild-type UBA7 in complex with UBE2L6 and ISG15 (left; EMB-16891; pdb: 8OIF ). The top-view (middle) and zoomed areas (right) highlight the adenylation pocket and location of the p.Val548Leu mutation shown in red.

    Journal: iScience

    Article Title: ISGylation is disrupted by UBA7 gene variants identified in individuals with neurodevelopmental disorder phenotypes

    doi: 10.1016/j.isci.2026.115454

    Figure Lengend Snippet: UBA7 variants from individuals with neurodevelopmental disorders alter protein structure (A) Pedigrees of the families studied in this article indicate the affected individuals 1, 2, and 3. A legend is provided for the symbols used. (B) Diagram of UBA7 protein domains and their functions. The location of the identified variants in the structure is indicated. IAD: inactive adenylation domain, AAD: active adenylation domain, FCCH: first catalytic cysteine half-domain, SCCH: second catalytic cysteine half-domain, UFD: ubiquitin-fold domain. (C) Alpha-fold models of UBA7 protein resulting from UBA7 wild type, or p.Trp311∗ and p.Lys709Serfs∗45 variants. The Red helix represents the added residues resulting from the p.Lys709Serfs∗45 frameshift variant. (D) Structure of wild-type UBA7 in complex with UBE2L6 and ISG15 (left; EMB-16891; pdb: 8OIF ). The top-view (middle) and zoomed areas (right) highlight the adenylation pocket and location of the p.Val548Leu mutation shown in red.

    Article Snippet: NEB 5-alpha Competent E. coli (DH5α) , New England Biolabs , Cat# C2987.

    Techniques: Ubiquitin Proteomics, Variant Assay, Mutagenesis