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hnk1  (Developmental Studies Hybridoma Bank)


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    Structured Review

    Developmental Studies Hybridoma Bank hnk1
    Hnk1, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 91/100, based on 198 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hnk/anti-HNK-1+oligosaccharide/us12545891-796-15-18
    Average 91 stars, based on 198 article reviews
    hnk1 - by Bioz Stars, 2026-10
    91/100 stars

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    Related Articles

    Incubation:

    Article Title: How do avian embryos resume development following diapause? A new role for TGF-β in regulating pluripotency-related genes
    Article Snippet: .. PBS-or BMP4-soaked beads were implanted in the embryos’ trunk neural tube for 24 h. The embryos were then fixed in 4% PFA, rinsed in PBS, permeabilized in PBS + 0.2% (v/v) Triton X-100 (CAS 9002-93-1, Sigma), blocked in 10% normal goat serum in PBS for 2 h and incubated with HNK-1 primary antibody (diluted 1:500; Developmental Studies Hybridoma Bank, AB-531908) overnight at 4 °C. .. Embryos were washed several times in PBS, and incubated with fluorescent secondary antibody (diluted 1:300 in PBS; goat anti-mouse, Alexa488, Thermo Fisher Scientific, Catalog No. A32723) overnight at 4 °C.

    Article Title: Signals from the brain induce variation in avian facial shape
    Article Snippet: .. The sections were incubated in HNK-1 monoclonal antibody (Developmental Studies Hybridoma Bank, Iowa City; diluted 1:300). .. HNK-1 binding was visualized using a donkey-anti-mouse IgM Rhodamine-TRITC antibody (Molecular Probes), and sections were counterstained using Bis-benzimide.

    Construct:

    Article Title: Skeletal Muscle Differentiation and Fusion Are Regulated by the BAR-containing Rho-GTPase-activating Protein (Rho-GAP), GRAF1
    Article Snippet: .. Commercial Antibodies and cDNA Constructs—Antibodies used were ERK-CT (Upstate), myosin heavy chain (MHC, Abcam), skeletal -actin (SKA, Sigma), -actinin (Sigma), troponin T (CT3, Developmental Studies Hybridoma Bank), tropomyosin (CH1, Developmental Studies Hybridoma Bank), 12-101 (Developmental Studies Hybridoma Bank), HNK (ZN12; Developmental Studies Hybridoma Bank), and p21 (Santa Cruz Biotechnology). .. Xenopus and human GRAF1 cDNAs were obtained from Open Biosystems and were directionally subcloned into cDNA3.1-FLAGor pRK5-Myc epitopetagged vectors using 5 -BamHI and 3 -EcoRI restriction sites that were generated by PCR.

    Article Title: Skeletal Muscle Differentiation and Fusion Are Regulated by the BAR-containing Rho-GTPase-activating Protein (Rho-GAP), GRAF1
    Article Snippet: .. Commercial Antibodies and cDNA Constructs Antibodies used were ERK-CT (Upstate), myosin heavy chain (MHC, Abcam), skeletal α-actin (SKA, Sigma), α-actinin (Sigma), troponin T (CT3, Developmental Studies Hybridoma Bank), tropomyosin (CH1, Developmental Studies Hybridoma Bank), 12-101 (Developmental Studies Hybridoma Bank), HNK (ZN12; Developmental Studies Hybridoma Bank), and p21 (Santa Cruz Biotechnology). .. Xenopus and human GRAF1 cDNAs were obtained from Open Biosystems and were directionally subcloned into cDNA3.1-FLAG or pRK5-Myc epitope-tagged vectors using 5′-BamHI and 3′-EcoRI restriction sites that were generated by PCR.

    Immunopeptidomics:

    Article Title: Skeletal Muscle Differentiation and Fusion Are Regulated by the BAR-containing Rho-GTPase-activating Protein (Rho-GAP), GRAF1
    Article Snippet: .. Commercial Antibodies and cDNA Constructs—Antibodies used were ERK-CT (Upstate), myosin heavy chain (MHC, Abcam), skeletal -actin (SKA, Sigma), -actinin (Sigma), troponin T (CT3, Developmental Studies Hybridoma Bank), tropomyosin (CH1, Developmental Studies Hybridoma Bank), 12-101 (Developmental Studies Hybridoma Bank), HNK (ZN12; Developmental Studies Hybridoma Bank), and p21 (Santa Cruz Biotechnology). .. Xenopus and human GRAF1 cDNAs were obtained from Open Biosystems and were directionally subcloned into cDNA3.1-FLAGor pRK5-Myc epitopetagged vectors using 5 -BamHI and 3 -EcoRI restriction sites that were generated by PCR.

    Article Title: Skeletal Muscle Differentiation and Fusion Are Regulated by the BAR-containing Rho-GTPase-activating Protein (Rho-GAP), GRAF1
    Article Snippet: .. Antibodies used were ERK-CT (Upstate), myosin heavy chain (MHC, Abcam), skeletal α-actin (SKA, Sigma), α-actinin (Sigma), troponin T (CT3, Developmental Studies Hybridoma Bank), tropomyosin (CH1, Developmental Studies Hybridoma Bank), 12-101 (Developmental Studies Hybridoma Bank), HNK (ZN12; Developmental Studies Hybridoma Bank), and p21 (Santa Cruz Biotechnology). .. Xenopus and human GRAF1 cDNAs were obtained from Open Biosystems and were directionally subcloned into cDNA3.1-FLAG or pRK5-Myc epitope-tagged vectors using 5′-BamHI and 3′-EcoRI restriction sites that were generated by PCR.

    Article Title: Skeletal Muscle Differentiation and Fusion Are Regulated by the BAR-containing Rho-GTPase-activating Protein (Rho-GAP), GRAF1
    Article Snippet: .. Commercial Antibodies and cDNA Constructs Antibodies used were ERK-CT (Upstate), myosin heavy chain (MHC, Abcam), skeletal α-actin (SKA, Sigma), α-actinin (Sigma), troponin T (CT3, Developmental Studies Hybridoma Bank), tropomyosin (CH1, Developmental Studies Hybridoma Bank), 12-101 (Developmental Studies Hybridoma Bank), HNK (ZN12; Developmental Studies Hybridoma Bank), and p21 (Santa Cruz Biotechnology). .. Xenopus and human GRAF1 cDNAs were obtained from Open Biosystems and were directionally subcloned into cDNA3.1-FLAG or pRK5-Myc epitope-tagged vectors using 5′-BamHI and 3′-EcoRI restriction sites that were generated by PCR.



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    Expression of neural <t>glyco-epitope</t> <t>HNK-1</t> in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.
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    Expression of neural <t>glyco-epitope</t> <t>HNK-1</t> in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.
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    Expression of neural <t>glyco-epitope</t> <t>HNK-1</t> in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.
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    The two-dimensional (2D) structure of <t>Honokiol</t> (A), and 3D structure of Bax (B).
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    Sartorius AG syringe filter
    The two-dimensional (2D) structure of <t>Honokiol</t> (A), and 3D structure of Bax (B).
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    Image Search Results


    Expression of neural glyco-epitope HNK-1 in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.

    Journal: The Journal of Biological Chemistry

    Article Title: A neural glycan HNK-1 is transferred to recipient cells via small extracellular vesicles

    doi: 10.1016/j.jbc.2026.111144

    Figure Lengend Snippet: Expression of neural glyco-epitope HNK-1 in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.

    Article Snippet: The following antibodies were used: mouse anti-GAPDH (Merck Millipore; MAB374), mouse HNK-1 mAb (ATCC; clone Leu7), rabbit anti-FLAG (Cell Signaling Technologies; 14,793), rabbit anti-GFP (MBL; 598), mouse anti-CD81 (Santa Cruz; sc-166029), mouse anti-myc (millipore; 05–724), rabbit anti-TSG101 (abcam; ab125011), HRP-anti-mouse IgG (GE Healthcare; NA931 V), HRP-anti-rabbit IgG (GE Healthcare; NA934 V), HRP-anti-mouse IgM (Invitrogen; 62–6802), Alexa546-anti-rabbit IgG (Invitrogen; A10040), and Alexa488-anti-mouse IgM (Invitrogen; A21042).

    Techniques: Expressing, Cell Culture, Transfection, Plasmid Preparation, Western Blot

    The two-dimensional (2D) structure of Honokiol (A), and 3D structure of Bax (B).

    Journal: Poultry Science

    Article Title: Honokiol antagonizes cadmium-induced ultrastructural nuclear variation and mitochondrial dysfunction of hepatocytes through targeting Bax protein

    doi: 10.1016/j.psj.2026.106557

    Figure Lengend Snippet: The two-dimensional (2D) structure of Honokiol (A), and 3D structure of Bax (B).

    Article Snippet: Honokiol (HNK) was procured from Shanghai Yuanye Technology Co., Ltd (Shanghai, China), while cadmium chloride (CdCl 2 ) was supplied by Sigma-Aldrich (St. Louis, USA).

    Techniques: