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protein mbp tagged endo hf  (New England Biolabs)


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    New England Biolabs protein mbp tagged endo hf
    Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by <t>Endo</t> Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.
    Protein Mbp Tagged Endo Hf, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 690 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Structural basis of EGF-repeat O -glucosylation by the protein O -glucosyltransferase POGLUT2"

    Article Title: Structural basis of EGF-repeat O -glucosylation by the protein O -glucosyltransferase POGLUT2

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2026.111361

    Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by Endo Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.
    Figure Legend Snippet: Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by Endo Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.

    Techniques Used: Functional Assay, Sequencing, Residue, Activity Assay, Negative Control, SDS Page, Purification, Filtration, Chromatography



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    Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by <t>Endo</t> Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.
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    New England Biolabs mbp tagged protein
    Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by <t>Endo</t> Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.
    Mbp Tagged Protein, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    protein mbp tagged otud4 constructs  (Merck & Co)
    86
    Merck & Co protein mbp tagged otud4 constructs
    Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by <t>Endo</t> Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.
    Protein Mbp Tagged Otud4 Constructs, supplied by Merck & Co, 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/protein mbp tagged otud4 constructs/product/Merck & Co
    Average 86 stars, based on 1 article reviews
    protein mbp tagged otud4 constructs - by Bioz Stars, 2026-06
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    mbp tagged proteins  (New England Biolabs)
    99
    New England Biolabs mbp tagged proteins
    Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by <t>Endo</t> Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.
    Mbp Tagged Proteins, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mbp tagged proteins/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    mbp tagged proteins - by Bioz Stars, 2026-06
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    Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by Endo Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.

    Journal: The Journal of Biological Chemistry

    Article Title: Structural basis of EGF-repeat O -glucosylation by the protein O -glucosyltransferase POGLUT2

    doi: 10.1016/j.jbc.2026.111361

    Figure Lengend Snippet: Functional and structural characterization of human POGLUT2 . A , O -glucosylation sites within epidermal growth factor–like (EGF) repeats. POGLUT1 (Rumi in Drosophila ) adds O -Glc to serine within the C 1 –C 2 consensus sequence C 1 -X- S -X-(P/A)-C 2 . POGLUT2/3 adds O -Glc to serine residue within the C 3 –C 4 consensus sequence C 3 -X-N-T-X-G- S -F-X-C 4 . EOGT (EGF domain–specific O -GlcNAc transferase) catalyzes O -GlcNAc addition to serine or threonine within the C 5 –C 6 consensus sequence C 5 -X-X-G-X-( S/T )-G-X-X-C 6 . Six conserved cysteine residues (C1–C6) form three disulfide bonds, indicated by solid lines . B , sequence alignment of representative EGF-repeat substrates of POGLUT2/3 (human Notch3 EGF10, hN3EGF10; human Notch1 EGF11, hN1EGF11; human Notch4 EGF11, hN4EGF11), POGLUT1 (human Notch1 EGF12 and 13, hN1EGF12 and hN1EGF13; human factor IX EGF, hFA9EGF) and EOGT (human Notch1 EGF20, hN1EGF20). C , enzymatic activity of POGLUT2 with different EGF repeats as acceptor substrates (hN3EGF10, hN1EGF11, and hN4EGF11). hFA9EGF (POGLUT1 substrate) and hN1EGF20 (EOGT substrate) serve as negative control. Data represent mean ± SD from three independent assays. D , preparation of homogeneous POGLUT2. SDS-PAGE analysis shows removal of heterogeneous N -glycans by Endo Hf digestion. The resulting deglycosylated POGLUT2 was further purified by gel-filtration chromatography (Superdex 200 Increase 10/300 GL). E , schematic of the domain organization of POGLUT2. Three pairs of disulfide bonds are depicted by yellow lines . F , overall structure of POGLUT2. Cartoon representation highlights A-domain ( green ), B-domain ( pink ), and filamin domain ( dark gray ). The disulfide bonds are depicted as cyan sticks . G , surface representation of POGLUT2 in the top view . H , close-up view of interdomain interactions between the filamin domain and A-domain, as indicated by the box in ( F ). POGLUT2, protein O-glucosyltransferase 2.

    Article Snippet: To remove N -glycans, the target protein was incubated with maltose-binding protein (MBP)–tagged Endo Hf (NEB) at a 1:100 (w/w) enzyme-to-protein ratio overnight at 4 °C.

    Techniques: Functional Assay, Sequencing, Residue, Activity Assay, Negative Control, SDS Page, Purification, Filtration, Chromatography