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biotinylated mal ii  (Vector Laboratories)


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    Structured Review

    Vector Laboratories biotinylated mal ii
    Biotinylated Mal Ii, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 408 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/maackia+amurensis+lectin+ii/Biotinylated+Maackia+Amurensis+Lectin+II+(MAL+II)/bio_rxiv__64898__2026__04__15__718752-82-4-7
    Average 96 stars, based on 408 article reviews
    biotinylated mal ii - by Bioz Stars, 2026-09
    96/100 stars

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    Related Articles

    Staining:

    Article Title: Air-liquid interface model for influenza aerosol exposure in vitro
    Article Snippet: .. Cells were stained with the following primary antibodies: Maackia Amurensis Lectin II (⍺2,3, Biotinylated, 15 μg/mL; B-1265-1; Vector Laboratories, CA, USA) and Sambucus Nigra Lectin (⍺2,6, Fluorescein, 15 μg/mL; F13012 ; Vector Laboratories, CA, USA) for 30 min at room temperature. .. The samples were then incubated with secondary Streptavidin Alexa Fluor 594 conjugate (1/1,000; S32356; ThermoFisher, MA, USA) for 30 min at room temperature.

    Bioprocessing:

    Article Title: ST6Gal1 influences the esophageal squamous cell carcinoma resistance to IFN-γ by regulating the expression of IFN-γ receptor 1.
    Article Snippet: ST6Gal1 ( 2,6-sialyltransferase1), the primary glycosyltransferase catalyzing 2,6-sialylation of N-glycans, plays a pivotal role in the progression of various human cancers.. However, the role of ST6Gal1-mediated 2,6-sialylation in human esophageal squamous cell carcinoma (ESCC) remains poorly understood.. In this study, we established ST6Gal1 knockdown (Kyse450-KD) and overexpressed (Kyse150-OE) ESCC cell models to investigate its functional significance.

    Immunodetection:

    Article Title: Engineering glycosyltransferases into glycan binding proteins using a mammalian surface display platform
    Article Snippet: Recombinant human ST3Gal1 (rhST3Gal1, Product code: 6905-GT-020), Recombinant human P-selectin Fc chimera (P-selectin-Fc, Product code: 137-PS-050), sheep anti-hGCNT1 IgG (Product code: AF7248-SP) and HRP donkey anti-sheep H + L IgG (Product code: HAF016) were from R&D Systems (Minneapolis, MN). .. Unconjugated Peanut Agglutinin (PNA, Product code: L-1070), Maackia Amurensis Lectin II (MALII, Product code: L-1260), Erythrina Cristagalli Lectin (ECL, Product code: L-1140), Phaseolus Vulgaris Leucoagglutinin (PHA-L, Product code: L-1110), and H.O.H (Human on Human) Immunodetection kit (Product code: HOH-3000) were from Vector Laboratories (Newark, CA). ..

    Blocking Assay:

    Article Title: Glycoprotein G enables HSV-2 neuroinvasion and provides protection as a glycosylated vaccine antigen
    Article Snippet: Lectin blot was performed by loading, 2 μg each of EXCT4-mgG-2, EXCT4-mgG-2(−N−O), EXCT4-mgG-2(-N), EXCT4-mgG-2(-O) and EXCT4-mgG-2(-SA) to a NuPAGE Bis-Tris 4-12% gel (Invitrogen) and separated using MOPS buffer (Invitrogen) at 200 V. The separated proteins were transferred to a polyvinylidene difluoride membrane (Immobilon-FL 0.45 μm, (Merck Millipore)) using the SemiDry Transblot SD (Bio-Rad Laboratories). .. Membranes were blocked with block buffer (2% BSA Factor V (Sigma-Aldrich) and 0.1% Tween-20 (VWR chemicals) in PBS (Medicago) followed by incubation with biotinylated lectins; 3 μg/mL Concavalin A (Con A) (Vector Laboratories), 3 μg/mL Jacalin (Vector Laboratories) or 5 μg/mL Maackia Amurensis Lectin II (MAL II, Vector Laboratories) diluted in PBS-BSA-T, at 4 °C for 16-20 hours. .. Next, membranes were washed three times with 0.1% Tween-20 in PBS (Medicago) followed by incubation with Streptavidin-alkaline phosphatase diluted 1:2000 (Southern Biotech) for 1 h at 20-22 °C.

    Incubation:

    Article Title: Glycoprotein G enables HSV-2 neuroinvasion and provides protection as a glycosylated vaccine antigen
    Article Snippet: Lectin blot was performed by loading, 2 μg each of EXCT4-mgG-2, EXCT4-mgG-2(−N−O), EXCT4-mgG-2(-N), EXCT4-mgG-2(-O) and EXCT4-mgG-2(-SA) to a NuPAGE Bis-Tris 4-12% gel (Invitrogen) and separated using MOPS buffer (Invitrogen) at 200 V. The separated proteins were transferred to a polyvinylidene difluoride membrane (Immobilon-FL 0.45 μm, (Merck Millipore)) using the SemiDry Transblot SD (Bio-Rad Laboratories). .. Membranes were blocked with block buffer (2% BSA Factor V (Sigma-Aldrich) and 0.1% Tween-20 (VWR chemicals) in PBS (Medicago) followed by incubation with biotinylated lectins; 3 μg/mL Concavalin A (Con A) (Vector Laboratories), 3 μg/mL Jacalin (Vector Laboratories) or 5 μg/mL Maackia Amurensis Lectin II (MAL II, Vector Laboratories) diluted in PBS-BSA-T, at 4 °C for 16-20 hours. .. Next, membranes were washed three times with 0.1% Tween-20 in PBS (Medicago) followed by incubation with Streptavidin-alkaline phosphatase diluted 1:2000 (Southern Biotech) for 1 h at 20-22 °C.

    Article Title: Exploring influenza A virus receptor distribution in the lactating mammary gland of domesticated livestock and in human breast tissue.
    Article Snippet: Slides were then blocked with 1× Carbo-Free blocking solution (Vector Laboratories Inc.) for 32 min, followed by a Streptavidin/Biotin Blocking Kit (Vector Laboratories Inc.) with a separate application for 12 min each. .. We incubated the sections for 4 h (fluorescent) or 1 h (chromogenic) at room temperature (RT) with one of the 3 lectins (Sambucus nigra lectin [SNA], Maackia amurensis lectin-I [MAL-I], Maackia amurensis lectin-II [MAL-II]) from Vector Laboratories at the listed concentration in Table 1. ..

    Article Title: Gne deletion in adult mice can cause thrombocytopenia, anemia, myopathy, bleeding, and death.
    Article Snippet: .. Biotinylated peanut agglutinin (PNA, B-1075-5), erythrina cristagalli lectin (ECA, B-1145-5), sambucus nigra lectin (SNA, B-1305-2), and maackia amurensis lectin II (MAA, B-1265-1) (all from Vector Laboratories; Plain City, OH) were added to the appropriate muscle sections along with rat monoclonal anti-laminin 2, α2 chain (L0663; Sigma Aldrich; St Louis, MO) and incubated overnight at 4 °C. .. Cy3-conjugated streptavidin (Jackson ImmunoResearch; West Grove, PA) and AlexaFluor 647-conjugated anti-rat IgG (Invitrogen; Waltham, MA) were added for an hour at room temperature, then slides were coverslipped using ProLong Gold antifade mountant with DAPI (ThermoFisher Scientific; Waltham, MA) and protected from light until imaging.

    Concentration Assay:

    Article Title: Exploring influenza A virus receptor distribution in the lactating mammary gland of domesticated livestock and in human breast tissue.
    Article Snippet: Slides were then blocked with 1× Carbo-Free blocking solution (Vector Laboratories Inc.) for 32 min, followed by a Streptavidin/Biotin Blocking Kit (Vector Laboratories Inc.) with a separate application for 12 min each. .. We incubated the sections for 4 h (fluorescent) or 1 h (chromogenic) at room temperature (RT) with one of the 3 lectins (Sambucus nigra lectin [SNA], Maackia amurensis lectin-I [MAL-I], Maackia amurensis lectin-II [MAL-II]) from Vector Laboratories at the listed concentration in Table 1. ..



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    α2,3-sialylation is required for BCG-induced osteoclast differentiation and activity (A) Comparison of differentially expressed genes (DEGs) between BCG-infected osteoclasts (RB) and uninfected controls (R). (n = 3 biological replicates per group, differential expression was defined as |FoldChange| > 2 and padj <0.05). (B) Volcano plot of DEGs highlighting genes related to sialic acid biosynthesis. (C) KEGG pathway enrichment analysis of upregulated DEGs in RB cells. (D,E) Immunofluorescence staining of α2,3-SA in mouse calvarial sections <t>using</t> <t>MAL</t> <t>II</t> lectin, with quantification of α2,3-SA fluorescence intensity (n = 5). Intensity density was normalized to the PBS group mean. (F) In vitro osteoclasts subjected to MAL II lectin staining and TRAP staining, with or without sialidase treatment to enzymatically remove α2,3-SA. (G) Quantification of α2,3-SA fluorescence intensity in cultured osteoclasts (n = 5). Intensity density was measured in cellular ROIs after background subtraction and normalized to the RANKL group mean. (H) Quantification of TRAP + multinucleated cells (≥3 nuclei) per field (randomly selected fields, fixed magnification) in vitro (n = 5). (I) mRNA expression levels of osteoclast differentiation markers ( Fos, Mmp9, Nfatc1, and Ocstamp ) in osteoclasts (n = 3). Data are presented as mean ± SD. Statistical significance was determined by two-tailed unpaired Student’s t-test for two-group comparisons (E) and one-way ANOVA followed by Tukey’s post hoc test for three-group comparisons (G–I) .
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    α2,3-sialylation is required for BCG-induced osteoclast differentiation and activity (A) Comparison of differentially expressed genes (DEGs) between BCG-infected osteoclasts (RB) and uninfected controls (R). (n = 3 biological replicates per group, differential expression was defined as |FoldChange| > 2 and padj <0.05). (B) Volcano plot of DEGs highlighting genes related to sialic acid biosynthesis. (C) KEGG pathway enrichment analysis of upregulated DEGs in RB cells. (D,E) Immunofluorescence staining of α2,3-SA in mouse calvarial sections <t>using</t> <t>MAL</t> <t>II</t> lectin, with quantification of α2,3-SA fluorescence intensity (n = 5). Intensity density was normalized to the PBS group mean. (F) In vitro osteoclasts subjected to MAL II lectin staining and TRAP staining, with or without sialidase treatment to enzymatically remove α2,3-SA. (G) Quantification of α2,3-SA fluorescence intensity in cultured osteoclasts (n = 5). Intensity density was measured in cellular ROIs after background subtraction and normalized to the RANKL group mean. (H) Quantification of TRAP + multinucleated cells (≥3 nuclei) per field (randomly selected fields, fixed magnification) in vitro (n = 5). (I) mRNA expression levels of osteoclast differentiation markers ( Fos, Mmp9, Nfatc1, and Ocstamp ) in osteoclasts (n = 3). Data are presented as mean ± SD. Statistical significance was determined by two-tailed unpaired Student’s t-test for two-group comparisons (E) and one-way ANOVA followed by Tukey’s post hoc test for three-group comparisons (G–I) .
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    Vector Laboratories biotinylated maackia amurensis lectin ii (mal ii)
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    α2,3-sialylation is required for BCG-induced osteoclast differentiation and activity (A) Comparison of differentially expressed genes (DEGs) between BCG-infected osteoclasts (RB) and uninfected controls (R). (n = 3 biological replicates per group, differential expression was defined as |FoldChange| > 2 and padj <0.05). (B) Volcano plot of DEGs highlighting genes related to sialic acid biosynthesis. (C) KEGG pathway enrichment analysis of upregulated DEGs in RB cells. (D,E) Immunofluorescence staining of α2,3-SA in mouse calvarial sections <t>using</t> <t>MAL</t> <t>II</t> lectin, with quantification of α2,3-SA fluorescence intensity (n = 5). Intensity density was normalized to the PBS group mean. (F) In vitro osteoclasts subjected to MAL II lectin staining and TRAP staining, with or without sialidase treatment to enzymatically remove α2,3-SA. (G) Quantification of α2,3-SA fluorescence intensity in cultured osteoclasts (n = 5). Intensity density was measured in cellular ROIs after background subtraction and normalized to the RANKL group mean. (H) Quantification of TRAP + multinucleated cells (≥3 nuclei) per field (randomly selected fields, fixed magnification) in vitro (n = 5). (I) mRNA expression levels of osteoclast differentiation markers ( Fos, Mmp9, Nfatc1, and Ocstamp ) in osteoclasts (n = 3). Data are presented as mean ± SD. Statistical significance was determined by two-tailed unpaired Student’s t-test for two-group comparisons (E) and one-way ANOVA followed by Tukey’s post hoc test for three-group comparisons (G–I) .
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    Image Search Results


    α2,3-sialylation is required for BCG-induced osteoclast differentiation and activity (A) Comparison of differentially expressed genes (DEGs) between BCG-infected osteoclasts (RB) and uninfected controls (R). (n = 3 biological replicates per group, differential expression was defined as |FoldChange| > 2 and padj <0.05). (B) Volcano plot of DEGs highlighting genes related to sialic acid biosynthesis. (C) KEGG pathway enrichment analysis of upregulated DEGs in RB cells. (D,E) Immunofluorescence staining of α2,3-SA in mouse calvarial sections using MAL II lectin, with quantification of α2,3-SA fluorescence intensity (n = 5). Intensity density was normalized to the PBS group mean. (F) In vitro osteoclasts subjected to MAL II lectin staining and TRAP staining, with or without sialidase treatment to enzymatically remove α2,3-SA. (G) Quantification of α2,3-SA fluorescence intensity in cultured osteoclasts (n = 5). Intensity density was measured in cellular ROIs after background subtraction and normalized to the RANKL group mean. (H) Quantification of TRAP + multinucleated cells (≥3 nuclei) per field (randomly selected fields, fixed magnification) in vitro (n = 5). (I) mRNA expression levels of osteoclast differentiation markers ( Fos, Mmp9, Nfatc1, and Ocstamp ) in osteoclasts (n = 3). Data are presented as mean ± SD. Statistical significance was determined by two-tailed unpaired Student’s t-test for two-group comparisons (E) and one-way ANOVA followed by Tukey’s post hoc test for three-group comparisons (G–I) .

    Journal: Frontiers in Pharmacology

    Article Title: Mycobacterium tuberculosis infection drives osteoclast overactivation via α2,3-Sialylation to promote pathological bone destruction

    doi: 10.3389/fphar.2026.1738896

    Figure Lengend Snippet: α2,3-sialylation is required for BCG-induced osteoclast differentiation and activity (A) Comparison of differentially expressed genes (DEGs) between BCG-infected osteoclasts (RB) and uninfected controls (R). (n = 3 biological replicates per group, differential expression was defined as |FoldChange| > 2 and padj <0.05). (B) Volcano plot of DEGs highlighting genes related to sialic acid biosynthesis. (C) KEGG pathway enrichment analysis of upregulated DEGs in RB cells. (D,E) Immunofluorescence staining of α2,3-SA in mouse calvarial sections using MAL II lectin, with quantification of α2,3-SA fluorescence intensity (n = 5). Intensity density was normalized to the PBS group mean. (F) In vitro osteoclasts subjected to MAL II lectin staining and TRAP staining, with or without sialidase treatment to enzymatically remove α2,3-SA. (G) Quantification of α2,3-SA fluorescence intensity in cultured osteoclasts (n = 5). Intensity density was measured in cellular ROIs after background subtraction and normalized to the RANKL group mean. (H) Quantification of TRAP + multinucleated cells (≥3 nuclei) per field (randomly selected fields, fixed magnification) in vitro (n = 5). (I) mRNA expression levels of osteoclast differentiation markers ( Fos, Mmp9, Nfatc1, and Ocstamp ) in osteoclasts (n = 3). Data are presented as mean ± SD. Statistical significance was determined by two-tailed unpaired Student’s t-test for two-group comparisons (E) and one-way ANOVA followed by Tukey’s post hoc test for three-group comparisons (G–I) .

    Article Snippet: Biotin MAL-II , Vector laboratories , Cat# B-1265-1.

    Techniques: Activity Assay, Comparison, Infection, Quantitative Proteomics, Immunofluorescence, Staining, Fluorescence, In Vitro, Cell Culture, Expressing, Two Tailed Test