biotinylated aleuria aurantia lectin (Vector Laboratories)

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Vector Laboratories biotinylated aleuria aurantia lectin

(A) TIM-3 expression on KASUMI-3 cells, primary AML blasts, and healthy immune subsets (CIK cells, monocytes, NK cells) assessed by flow cytometry using QuantiBRITE beads. REH (ALL cell line) served as negative control. (B) Short-term killing assay of TIM-3.CAR-CIK cells against CIK (n = 11) or KASUMI-3 (n = 8) cells compared with NT cells. Target cell lysis was evaluated by flow cytometry (E:T 5:1). (C) Short-term killing assay of TIM-3.CAR-CIK cells against monocytes (n = 8) or NK cells (n = 8) compared with NT (E:T 5:1). KASUMI-3 (n = 4) were included as positive control. (D) Immunoblot analysis of TIM-3 in lysates from monocytes, CIK cells, and KASUMI-3 cells following enzymatic treatment with PNGase F or broad neuraminidase, probed with a commercial anti–TIM-3 antibody (TIM-3-cmAb). GAPDH, loading control. Glycan symbols follow SNFG. (E) TIM-3 immunoprecipitates from monocytes, CIK cells, and KASUMI-3 cells treated with PNGase F or O- glycosidase and analyzed by immunoblot with TIM-3-cmAb and <t>lectin</t> far-western with <t>Aleuria</t> aurantia lectin (AAL; fucosylated epitopes). TGX stain-free total protein signal is shown as a loading/normalization control. (F) KASUMI-3 cells treated with vehicle (mock) or the fucosylation inhibitor 2F-peracetyl-fucose (SGN-2FF), followed by PNGase F or neuraminidase treatment and immunoblot/lectin probing with TIM-3-cmAb and AAL. See also Figure S3A . (G) Short-term killing assay of TIM-3.CAR-CIK cells against untreated or SGN-2FF-treated KASUMI-3 cells at various E:T ratios (5:1, 1:1, 0.5:1, 0.25:1 and 0.125:1, n = 8). (H) Affinity kinetics (left) and binding avidity at 1000 pN force (right) of TIM-3.CAR-CIK cells to untreated or defucosylated KASUMI-3 by LUMICKS analysis (n = 6). Immunoblot experiments (D-F) were repeated in three independent biological replicates with similar results. Data are presented as individual values and mean ± SD. Statistical significance was determined with repeated-measures two-way ANOVA with Bonferroni’s post hoc test (B, C) or using paired t test (G, H). ns, not significant; *p = 0.01, **p < 0.001, ***p = 0.0001 and ****p < 0.0001. Illustrations were created with Biorender.com. See also Figure S3 for loading-matched TIM-3 immunoprecipitation controls.

Biotinylated Aleuria Aurantia Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 279 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/aleuria+aurantia+lectin+aal/Biotinylated+Aleuria+Aurantia+Lectin+(AAL)/bio_rxiv__64898__2026__04__22__719217-335-25-31
Average 94 stars, based on 279 article reviews

biotinylated aleuria aurantia lectin - by Bioz Stars, 2026-09

94/100 stars

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1) Product Images from "Differential TIM-3 glycosylation enables specific dual targeting CAR-T therapy in acute myeloid leukemia"

Article Title: Differential TIM-3 glycosylation enables specific dual targeting CAR-T therapy in acute myeloid leukemia

Journal: bioRxiv

doi: 10.64898/2026.04.22.719217

Figure Legend Snippet: (A) TIM-3 expression on KASUMI-3 cells, primary AML blasts, and healthy immune subsets (CIK cells, monocytes, NK cells) assessed by flow cytometry using QuantiBRITE beads. REH (ALL cell line) served as negative control. (B) Short-term killing assay of TIM-3.CAR-CIK cells against CIK (n = 11) or KASUMI-3 (n = 8) cells compared with NT cells. Target cell lysis was evaluated by flow cytometry (E:T 5:1). (C) Short-term killing assay of TIM-3.CAR-CIK cells against monocytes (n = 8) or NK cells (n = 8) compared with NT (E:T 5:1). KASUMI-3 (n = 4) were included as positive control. (D) Immunoblot analysis of TIM-3 in lysates from monocytes, CIK cells, and KASUMI-3 cells following enzymatic treatment with PNGase F or broad neuraminidase, probed with a commercial anti–TIM-3 antibody (TIM-3-cmAb). GAPDH, loading control. Glycan symbols follow SNFG. (E) TIM-3 immunoprecipitates from monocytes, CIK cells, and KASUMI-3 cells treated with PNGase F or O- glycosidase and analyzed by immunoblot with TIM-3-cmAb and lectin far-western with Aleuria aurantia lectin (AAL; fucosylated epitopes). TGX stain-free total protein signal is shown as a loading/normalization control. (F) KASUMI-3 cells treated with vehicle (mock) or the fucosylation inhibitor 2F-peracetyl-fucose (SGN-2FF), followed by PNGase F or neuraminidase treatment and immunoblot/lectin probing with TIM-3-cmAb and AAL. See also Figure S3A . (G) Short-term killing assay of TIM-3.CAR-CIK cells against untreated or SGN-2FF-treated KASUMI-3 cells at various E:T ratios (5:1, 1:1, 0.5:1, 0.25:1 and 0.125:1, n = 8). (H) Affinity kinetics (left) and binding avidity at 1000 pN force (right) of TIM-3.CAR-CIK cells to untreated or defucosylated KASUMI-3 by LUMICKS analysis (n = 6). Immunoblot experiments (D-F) were repeated in three independent biological replicates with similar results. Data are presented as individual values and mean ± SD. Statistical significance was determined with repeated-measures two-way ANOVA with Bonferroni’s post hoc test (B, C) or using paired t test (G, H). ns, not significant; *p = 0.01, **p < 0.001, ***p = 0.0001 and ****p < 0.0001. Illustrations were created with Biorender.com. See also Figure S3 for loading-matched TIM-3 immunoprecipitation controls.

Techniques Used: Expressing, Flow Cytometry, Negative Control, Lysis, Positive Control, Western Blot, Control, Glycoproteomics, Staining, Binding Assay, Immunoprecipitation

(A) Immunoblot profiling of TIM-3 glycoforms in monocytes, CIK cells, and KASUMI-3 lysates using a recombinant scFv-derived monoclonal antibody (TIM-3scFv-mAb) following enzymatic treatment with PNGase F or broad neuraminidase. GAPDH, loading control. (B) TIM-3 immunoprecipitates from healthy monocytes, KASUMI-3 cells, and primary AML blasts treated with neuraminidase and/or PNGase F and analyzed by lectin and antibody probing: Ricinus communis agglutinin I (RCA-I; terminal β-galactose/LacNAc motifs), CA19-9 (sialyl-Lewis A), CSLEX1 (sialyl-Lewis X), and TIM-3scFv-mAb. See also Figure S3B . (C) High-resolution immunoblot of TIM-3 species detected by TIM-3scFv-mAb in CIK cells, primary AML blasts, and KASUMI-3 cells. GAPDH, loading control. See also Figure S3C . (D) RT-qPCR expression profiling of glycosyltransferases (FUT7, FUT8, ST3GAL3, ST3GAL4, ST3GAL6) in monocytes, KASUMI-3 cells, and primary AML blasts. Data are plotted as fold-change relative to monocytes and normalized to 18S RNA; individual points denote biological samples where applicable. (E) Schematic model summarizing a glycoform-biased recognition framework in which AML-associated remodeling of TIM-3 N -glycans contributes to preferential TIM-3.CAR recognition of AML-enriched TIM-3 glycoforms. Representative N -glycan structures are proposed for TIM-3 in AML blasts, monocytes and CIK cells based on enzymatic perturbation and lectin/antibody probing. Sugar moieties drawn with dashed outlines indicate features not directly resolved/assigned. Glycan symbols follow SNFG. Immunoblot and lectin/antibody blot experiments (A-C) were repeated in three independent biological replicates with similar results. Illustrations were created with Biorender.com. See also Figure S3 for additional lectin/antibody probing of TIM-3 glycoforms and terminal galactose exposure.

Figure Legend Snippet: (A) Immunoblot profiling of TIM-3 glycoforms in monocytes, CIK cells, and KASUMI-3 lysates using a recombinant scFv-derived monoclonal antibody (TIM-3scFv-mAb) following enzymatic treatment with PNGase F or broad neuraminidase. GAPDH, loading control. (B) TIM-3 immunoprecipitates from healthy monocytes, KASUMI-3 cells, and primary AML blasts treated with neuraminidase and/or PNGase F and analyzed by lectin and antibody probing: Ricinus communis agglutinin I (RCA-I; terminal β-galactose/LacNAc motifs), CA19-9 (sialyl-Lewis A), CSLEX1 (sialyl-Lewis X), and TIM-3scFv-mAb. See also Figure S3B . (C) High-resolution immunoblot of TIM-3 species detected by TIM-3scFv-mAb in CIK cells, primary AML blasts, and KASUMI-3 cells. GAPDH, loading control. See also Figure S3C . (D) RT-qPCR expression profiling of glycosyltransferases (FUT7, FUT8, ST3GAL3, ST3GAL4, ST3GAL6) in monocytes, KASUMI-3 cells, and primary AML blasts. Data are plotted as fold-change relative to monocytes and normalized to 18S RNA; individual points denote biological samples where applicable. (E) Schematic model summarizing a glycoform-biased recognition framework in which AML-associated remodeling of TIM-3 N -glycans contributes to preferential TIM-3.CAR recognition of AML-enriched TIM-3 glycoforms. Representative N -glycan structures are proposed for TIM-3 in AML blasts, monocytes and CIK cells based on enzymatic perturbation and lectin/antibody probing. Sugar moieties drawn with dashed outlines indicate features not directly resolved/assigned. Glycan symbols follow SNFG. Immunoblot and lectin/antibody blot experiments (A-C) were repeated in three independent biological replicates with similar results. Illustrations were created with Biorender.com. See also Figure S3 for additional lectin/antibody probing of TIM-3 glycoforms and terminal galactose exposure.

Techniques Used: Western Blot, Recombinant, Derivative Assay, Control, Quantitative RT-PCR, Expressing, Glycoproteomics

Immunopeptidomics:

Article Title: Studying Macromolecular Composition in Cell-Cell Interfaces Using 3D Membrane Reconstitution Systems.
Article Snippet: We used the following recombinant proteins obtained from Sino Biological: human CD2 (His-Tag,10982-H08H), CD58/ human LFA-3 (His-Tag, 12409-H08H), PD1/human PDCD1 (His-Tag,10377-H08H), PD-L1/human B7-H1/ CD274 (His-Tag, 10084-H08H), CD80/human B7-1 (His-Tag, 10698-H08H), human CTLA-4 (His-Tag,11159-H08H), NCR3/human NKp30 (His-Tag, 10480-H08H), human B7-H6 (His-Tag, 16140-H08H), human SLAMF6/human Ly108 (His-Tag, 11945-H08H), human CD84 (His-Tag, 10100-H08H), human SIRP αV2 (His-Tag, 30014-H08H), human CD47 (His-Tag, 12283-H08H), CD45 (ECD, His-Tag, 14197- H08H). .. We also used the proteins: CD43/ human leukosialin (His-Tag, CD3-H52H9, ACROBiosystems), MUC1-Alexa Fluor 488 (kindly provided by Carolyn Shurer), MHC class I H-2Db presenting the LCMV-derived gp33 peptide (KAVYNFATM) [ 37, 38 ], MHC class I (HLA-A*02:01) presenting the tumor-associated antigen NY-ESO1-9 V peptide (SLLMWITQV; from now on 9 V) [ 39 ], MHC class I (HLA-A*02:01) presenting the NY-ESO1-3P9V peptide variant (SLPMWITQV; from now on 3P9V), P14 TCR [ 38 ], 1G4 TCR [ 39 ], Wheat Germ Agglutinin (WGA) Alexa Fluor 647 Conjugate (ThermoFisherScientific), Aleuria Aurantia Lectin (AAL) (L-1390-2, Vector Labs), Sambucus Nigra-I-Agglutinin (SNA) (L-1300-5, Vector Labs), Maackia Amurensis-II Lectin (MAL-II) (L-1260-2, Vector Labs). .. We used Alexa Fluor 488 or 647 NHS Ester (Succinimidyl Ester) (ThermoFisher Scientific) for protein labeling.

Article Title: Studying macromolecular composition in cell-cell interfaces using 3D membrane reconstitution systems
Article Snippet: We used the following recombinant proteins obtained from Sino Biological: human CD2 (His-Tag,10982-H08H), CD58/ human LFA-3 (His-Tag, 12409-H08H), PD1/human PDCD1 (His-Tag,10377-H08H), PD-L1/human B7-H1/ CD274 (His-Tag, 10084-H08H), CD80/human B7-1 (His-Tag, 10698-H08H), human CTLA-4 (His-Tag,11159-H08H), NCR3/human NKp30 (His-Tag, 10480-H08H), human B7-H6 (His-Tag, 16140-H08H), human SLAMF6/human Ly108 (His-Tag, 11945-H08H), human CD84 (His-Tag, 10100-H08H), human SIRPαV2 (His-Tag, 30014-H08H), human CD47 (His-Tag, 12283-H08H), CD45 (ECD, His-Tag, 14197-H08H). .. We also used the proteins: CD43/ human leukosialin (His-Tag, CD3-H52H9, ACROBiosystems), MUC1-Alexa FluorTM 488 (kindly provided by Carolyn Shurer), MHC class I H-2D b presenting the LCMV-derived gp33 peptide (KAVYNFATM) ( ; ), MHC class I (HLA-A*02:01) presenting the tumour-associated antigen NY-ESO1-9V peptide (SLLMWITQV; from now on 9V) , MHC class I (HLA-A*02:01) presenting the NY-ESO1-3P9V peptide variant (SLPMWITQV; from now on 3P9V), P14 TCR , 1G4 TCR , Wheat Germ Agglutinin (WGA) Alexa FluorTM 647 Conjugate (ThermoFisherScientific), Aleuria Aurantia Lectin (AAL) (L-1390-2, Vector Labs), Sambucus Nigra-I-Agglutinin (SNA) (L-1300-5, Vector Labs), Maackia Amurensis-II Lectin (MAL-II) (L-1260-2, Vector Labs). .. We used Alexa FluorTM 488 or 647 NHS Ester (Succinimidyl Ester) (ThermoFisher Scientific) for protein labelling.

Variant Assay:

Whole Genome Amplification:

Article Title: Single-cell mapping of the glycocalyx in the adult human and mouse ocular surface
Article Snippet: .. Unconjugated lectins—including Aleuria aurantia lectin (AAL), Maclura pomifera agglutinin 17 (MPA), Maackia amurensis agglutinin I (MAA I), Concanavalin A (ConA), Datura stramonium 18 agglutinin (DSA), wheat germ agglutinin (WGA), peanut agglutinin (PNA), and Erythrina cristagalli 19 agglutinin (ECA)—as well as biotinylated Sambucus nigra agglutinin I (SNA I), were obtained from 20 Vector Laboratories (Newark, CA, USA). .. DNA oligonucleotides for lectin conjugation were 21 synthesized by Integrated DNA Technologies (Coralville, IA, USA).

Membrane:

Article Title: Extracellular vesicles display distinct glycosignatures in high-grade serous ovarian carcinoma.
Article Snippet: The samples were boiled at 95 ◦C for 5 min. Proteins were separated on a 5–20% SuperSepTM Ace SDS-PAGE gel (FujiFilm) at 100 V and 30 mA for 1 h Afterwards, the gels were transferred onto a PVDF membrane (BioRad) using the Trans-blot SD semi-dry transfer cell (BioRad) at 10 V for 1 h The transferred membrane was blocked with 10 ml Carbo-Free blocking buffer (1:10 dilution, Vector Laboratories) and incubated for 1 h on a shaker. .. The membrane was incubated with 10 ml Concanavalin A (ConA), Aleuria Aurantia Lectin (AAL), Sambucus Nigra Agglutinin (SNA) or Maackia Amurensis Lectin II (MAL II) (1:2000 dilution, all from Vector Laboratories) in Carbo-Free blocking buffer at 4 ◦C overnight. ..

Article Title: Extracellular vesicles display distinct glycosignatures in high-grade serous ovarian carcinoma
Article Snippet: The samples were boiled at 95 °C for 5 min. Proteins were separated on a 5–20% SuperSepTM Ace SDS-PAGE gel (FujiFilm) at 100 V and 30 mA for 1 h Afterwards, the gels were transferred onto a PVDF membrane (BioRad) using the Trans-blot SD semi-dry transfer cell (BioRad) at 10 V for 1 h The transferred membrane was blocked with 10 ml Carbo-Free blocking buffer (1:10 dilution, Vector Laboratories) and incubated for 1 h on a shaker. .. The membrane was incubated with 10 ml Concanavalin A (ConA), Aleuria Aurantia Lectin (AAL), Sambucus Nigra Agglutinin (SNA) or Maackia Amurensis Lectin II (MAL II) (1:2000 dilution, all from Vector Laboratories) in Carbo-Free blocking buffer at 4 °C overnight. ..

Incubation:

Article Title: Fucosylation of hemocyanin is critical for antibacterial immunity in Penaeus vannamei.
Article Snippet: Posttranslational modifications (PTMs) play a pivotal role in expanding the function of immune related proteins, especially during pathogen infections.. However, the precise impact of PTMs on the functional diversity of proteins such as respiratory glycoproteins and hemocyanins remains incompletely understood.. In this study, we investigated the fucosylation modification of Penaeus vannamei hemocyanin (PvHMC) and its impact on antibacterial immunity.

Blocking Assay:

Staining:

Article Title: Golgi pH elevation due to loss of V-ATPase subunit V0a2 function correlates with tissue-specific glycosylation changes and globozoospermia.
Article Snippet: .. The first staining step with Aleuria Aurantia Lectin (AAL), Fluorescein (FL-1391-1) (Vector Laboratories, Newark, USA) was performed with dilution (1:100). ..

Review