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mal  (Vector Laboratories)


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    Vector Laboratories mal
    Mal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/maackia+amurensis/Fluorescein+labeled+Maackia+Amurensis+Lectin+I+(MAL+I)/pm42037410-272-24-27
    Average 93 stars, based on 37 article reviews
    mal - by Bioz Stars, 2026-09
    93/100 stars

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    Related Articles

    Labeling:

    Article Title: Expression of Sialic Acid α2-3 and α2-6 in MCF Cells Upon Stimulation with Lipopolysaccharide
    Article Snippet: .. 2.1 Chemicals and Lectins Lectins from Maackia amurensis and Sambuccus nigra labeled with fluorescein were obtained from Vector Laboratories (Burlingame, CA USA). .. Vectashield [mounting medium with diamidino-2phenylindole (DAPI) fluorescent dye] was from Vector Laboratories Inc. (Burlingame, CA).

    other:

    Article Title: Changes in glycans on platelet microparticles released during storage of apheresis platelets are associated with phosphatidylserine externalization and phagocytosis.
    Article Snippet: Funding information Australian governments fund Australian Red Cross Lifeblood to provide blood, blood products, and services to the Australian community.. This research was also supported by a joint ISTH-EHA Training Fellowship, awarded to DvdW.. Abstract Background: Platelets shed platelet microparticles (PMP) when activated or stored.

    Concentration Assay:

    Article Title: Detecting normal and cancer skin cells via glycosylation and adhesion signatures: A path to enhanced microfluidic phenotyping.
    Article Snippet: Routine observations of the cells were performed using an optical microscope (Olympus, CKX53). .. Plant lectins, including Dolichos Biflorus Agglutinin (DBA, L-1030, Vector Laboratories) and Maackia Amurensis (MAL, L-1260, Vector Laboratories), were dissolved in deionized water (dH2O) at 0.1 mg/mL concentration. .. Rhodamine-labeled DBA (TRIC-DBA, RL-1032, 550/575 nm excitation/emission, Vector Laboratories) and Cyanine 3 labeled MAL (Cy3-MAL, 21761120–1, 550/570 nm excitation/emission, BioWorld) were dissolved in dH2O at 1.0 mg/mL.

    Article Title: Increased expression of sialic acid in cervical biopsies with squamous intraepithelial lesions
    Article Snippet: .. Sambucus nigra (SNA specific for NeuAcα2,6Gal-GalNAc); Maackia amurensis (MAA, specific for NeuAcα2,3Gal); and agglutinins biotinylated were purchased from Vector (Burlingame, CA, USA) and used at a concentration of 5 μg/ml. .. Signal amplification was realized with the TSA biotin system kit from NEN Life Science (Boston, MA, USA).

    Staining:

    Article Title: siRNA Knockdown of Ribosomal Protein Gene RPL19 Abrogates the Aggressive Phenotype of Human Prostate Cancer
    Article Snippet: .. Sections were cut at 5 μm and stained for Neu5Acα2→3Gal- and Neu5Acα2→6Gal- using biotinylated lectins (Vector Laboratories, Peterborough, UK) from Sambucus nigra and Maackia amurensis respectively , . ..



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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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    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