1005 biotinylated lectin vvl vector laboratories Search Results


94
Vector Laboratories ulex europaeus agglutinin uea
The principal carbohydrate patterns recognized by the 4 lectins tested.
Ulex Europaeus Agglutinin Uea, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Vector Laboratories biotinylated con a
The principal carbohydrate patterns recognized by the 4 lectins tested.
Biotinylated Con A, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
Vector Laboratories biotinylated
The principal carbohydrate patterns recognized by the 4 lectins tested.
Biotinylated, supplied by Vector Laboratories, 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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95
Vector Laboratories tomato lectin
Glycan epitopes in D. immitis . a A summary of neutral and anionic N-glycan structures highlighting major antennal modifications; for a fuller set of defined structures refer to Supplementary Table . b The presence of HexNAc and phosphorylcholine residues in L3 larvae was probed using CGL3 (red) and TEPC 15 (green) by indirect fluorescence microscopy; also shown are the DAPI staining (for DNA) and DIC (differential interference contrast) images and the scale bar corresponds to 10 µm. c MALDI-TOF–MS of the AEAB-labelled neutral N-glycome before and after hydrofluoric acid treatment indicating loss of antennal fucose and phosphorylcholine residues. d The binding of Coprinopsis galectin (CGL3; 10 µg/ml), wheat <t>germ</t> <t>agglutinin</t> (WGA; 10 µg/ml) and human mannose binding <t>lectin</t> (MBL) to the Dirofilaria glycans increases after hydrofluoric acid treatment, while that to anti-phosphorylcholine (TEPC 15 IgA monoclonal) decreases. The charts indicate the uncorrected fluorescence values with the standard deviations (mean of 10 spots; analysed with an unpaired two-tailed parametric t -test with a 95% confidence level) as well as a negative control (spotting buffer only; example array scans are shown for the WGA and MBL data). Note that previous data indicate that CGL3 can recognise LacdiNAc, whereas WGA is known to bind HexNAc n motifs and MBL to a wide range of glycans including those with terminal mannose or N -acetylglucosamine residues. Refer to Supplementary Figures – and for (i) western blotting and further micrograph data (including controls) on epitopes recognised by CGL3 and TEPC 15, (ii) a summary of MS data on proteins affinity purified on CGL3- and TEPC 15-Sepharose, (iii) further MBL binding experiments (before and after endoglycosidase H treatment) to the immobilised glycome pools and fractionated immobilised glycans as well as data on other lectin interactions to the natural glycans and to defined di- and tri-saccharides
Tomato Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/1005+biotinylated+lectin+vvl+vector+laboratories/Biotinylated+Lycopersicon+Esculentum+(Tomato)+Lectin+(LEL%2C+TL)/pmc06325117-249-35-37
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93
Vector Laboratories biotinylated lectin
Glycan epitopes in D. immitis . a A summary of neutral and anionic N-glycan structures highlighting major antennal modifications; for a fuller set of defined structures refer to Supplementary Table . b The presence of HexNAc and phosphorylcholine residues in L3 larvae was probed using CGL3 (red) and TEPC 15 (green) by indirect fluorescence microscopy; also shown are the DAPI staining (for DNA) and DIC (differential interference contrast) images and the scale bar corresponds to 10 µm. c MALDI-TOF–MS of the AEAB-labelled neutral N-glycome before and after hydrofluoric acid treatment indicating loss of antennal fucose and phosphorylcholine residues. d The binding of Coprinopsis galectin (CGL3; 10 µg/ml), wheat <t>germ</t> <t>agglutinin</t> (WGA; 10 µg/ml) and human mannose binding <t>lectin</t> (MBL) to the Dirofilaria glycans increases after hydrofluoric acid treatment, while that to anti-phosphorylcholine (TEPC 15 IgA monoclonal) decreases. The charts indicate the uncorrected fluorescence values with the standard deviations (mean of 10 spots; analysed with an unpaired two-tailed parametric t -test with a 95% confidence level) as well as a negative control (spotting buffer only; example array scans are shown for the WGA and MBL data). Note that previous data indicate that CGL3 can recognise LacdiNAc, whereas WGA is known to bind HexNAc n motifs and MBL to a wide range of glycans including those with terminal mannose or N -acetylglucosamine residues. Refer to Supplementary Figures – and for (i) western blotting and further micrograph data (including controls) on epitopes recognised by CGL3 and TEPC 15, (ii) a summary of MS data on proteins affinity purified on CGL3- and TEPC 15-Sepharose, (iii) further MBL binding experiments (before and after endoglycosidase H treatment) to the immobilised glycome pools and fractionated immobilised glycans as well as data on other lectin interactions to the natural glycans and to defined di- and tri-saccharides
Biotinylated Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Vector Laboratories biotin conjugated concanavalin a
PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated <t>Con</t> <t>A</t> (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.
Biotin Conjugated Concanavalin A, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/1005+biotinylated+lectin+vvl+vector+laboratories/Unconjugated+Concanavalin+A+(Con+A)/pmc00025675-133-0-5
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96
Vector Laboratories streptavidin/biotin blocking kit
PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated <t>Con</t> <t>A</t> (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.
Streptavidin/Biotin Blocking Kit, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/1005+biotinylated+lectin+vvl+vector+laboratories/Streptavidin%2FBiotin+Blocking+Kit/custom%40sp-2002%4010%2E1101%2F2020%2E08%2E20%2E260430
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98
AvesLabs biotinylated goat anti chicken igy
PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated <t>Con</t> <t>A</t> (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.
Biotinylated Goat Anti Chicken Igy, supplied by AvesLabs, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Vector Laboratories biotinylated galanthus nivalis lectin (gnl)
PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated <t>Con</t> <t>A</t> (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.
Biotinylated Galanthus Nivalis Lectin (Gnl), supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Vector Laboratories biotinylated wheat germ agglutinin (wga)
PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated <t>Con</t> <t>A</t> (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.
Biotinylated Wheat Germ Agglutinin (Wga), supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/1005+biotinylated+lectin+vvl+vector+laboratories/Biotinylated+Wheat+Germ+Agglutinin+(WGA)/custom%40b-1025%4034106226
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91
Vector Laboratories biotinylated maclura pomifera lectin (mpl)
PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated <t>Con</t> <t>A</t> (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.
Biotinylated Maclura Pomifera Lectin (Mpl), supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


The principal carbohydrate patterns recognized by the 4 lectins tested.

Journal: Scientific Reports

Article Title: Targeting cell-derived markers to improve the detection of invisible biological traces for the purpose of genetic-based criminal identification

doi: 10.1038/s41598-023-45366-y

Figure Lengend Snippet: The principal carbohydrate patterns recognized by the 4 lectins tested.

Article Snippet: Samples were incubated for 20 min in a humidity chamber using a biotinylated lectin solution (at final concentration 10 µg/ml): Concanavalin A (ConA), Peanut agglutinin (PNA), Elderberry lectin (SNA), and Ulex europaeus agglutinin (UEA) (B-1005, B-1075, B-1305, and B-1065 respectively, Vector Laboratories, USA).

Techniques:

Glycan epitopes in D. immitis . a A summary of neutral and anionic N-glycan structures highlighting major antennal modifications; for a fuller set of defined structures refer to Supplementary Table . b The presence of HexNAc and phosphorylcholine residues in L3 larvae was probed using CGL3 (red) and TEPC 15 (green) by indirect fluorescence microscopy; also shown are the DAPI staining (for DNA) and DIC (differential interference contrast) images and the scale bar corresponds to 10 µm. c MALDI-TOF–MS of the AEAB-labelled neutral N-glycome before and after hydrofluoric acid treatment indicating loss of antennal fucose and phosphorylcholine residues. d The binding of Coprinopsis galectin (CGL3; 10 µg/ml), wheat germ agglutinin (WGA; 10 µg/ml) and human mannose binding lectin (MBL) to the Dirofilaria glycans increases after hydrofluoric acid treatment, while that to anti-phosphorylcholine (TEPC 15 IgA monoclonal) decreases. The charts indicate the uncorrected fluorescence values with the standard deviations (mean of 10 spots; analysed with an unpaired two-tailed parametric t -test with a 95% confidence level) as well as a negative control (spotting buffer only; example array scans are shown for the WGA and MBL data). Note that previous data indicate that CGL3 can recognise LacdiNAc, whereas WGA is known to bind HexNAc n motifs and MBL to a wide range of glycans including those with terminal mannose or N -acetylglucosamine residues. Refer to Supplementary Figures – and for (i) western blotting and further micrograph data (including controls) on epitopes recognised by CGL3 and TEPC 15, (ii) a summary of MS data on proteins affinity purified on CGL3- and TEPC 15-Sepharose, (iii) further MBL binding experiments (before and after endoglycosidase H treatment) to the immobilised glycome pools and fractionated immobilised glycans as well as data on other lectin interactions to the natural glycans and to defined di- and tri-saccharides

Journal: Nature Communications

Article Title: Highly modified and immunoactive N-glycans of the canine heartworm

doi: 10.1038/s41467-018-07948-7

Figure Lengend Snippet: Glycan epitopes in D. immitis . a A summary of neutral and anionic N-glycan structures highlighting major antennal modifications; for a fuller set of defined structures refer to Supplementary Table . b The presence of HexNAc and phosphorylcholine residues in L3 larvae was probed using CGL3 (red) and TEPC 15 (green) by indirect fluorescence microscopy; also shown are the DAPI staining (for DNA) and DIC (differential interference contrast) images and the scale bar corresponds to 10 µm. c MALDI-TOF–MS of the AEAB-labelled neutral N-glycome before and after hydrofluoric acid treatment indicating loss of antennal fucose and phosphorylcholine residues. d The binding of Coprinopsis galectin (CGL3; 10 µg/ml), wheat germ agglutinin (WGA; 10 µg/ml) and human mannose binding lectin (MBL) to the Dirofilaria glycans increases after hydrofluoric acid treatment, while that to anti-phosphorylcholine (TEPC 15 IgA monoclonal) decreases. The charts indicate the uncorrected fluorescence values with the standard deviations (mean of 10 spots; analysed with an unpaired two-tailed parametric t -test with a 95% confidence level) as well as a negative control (spotting buffer only; example array scans are shown for the WGA and MBL data). Note that previous data indicate that CGL3 can recognise LacdiNAc, whereas WGA is known to bind HexNAc n motifs and MBL to a wide range of glycans including those with terminal mannose or N -acetylglucosamine residues. Refer to Supplementary Figures – and for (i) western blotting and further micrograph data (including controls) on epitopes recognised by CGL3 and TEPC 15, (ii) a summary of MS data on proteins affinity purified on CGL3- and TEPC 15-Sepharose, (iii) further MBL binding experiments (before and after endoglycosidase H treatment) to the immobilised glycome pools and fractionated immobilised glycans as well as data on other lectin interactions to the natural glycans and to defined di- and tri-saccharides

Article Snippet: The slides were incubated with either dilutions of dog sera (one control and two infected), biotinylated fungal CGL3 and CCL2 (see above) or biotinylated forms of wheat germ agglutinin, Aleuria aurantia lectin, concanavalin A or tomato lectin (Vector Laboratories; B1025, B1395, B1005 and B1175), murine TEPC 15 IgA monoclonal (Sigma-Aldrich; M1421), recombinant human mannose binding lectin (Biotechne; 9085-MB-050) or natural human C-reactive protein (MPBio; 215231505) followed by the relevant secondary and/or tertiary antibodies.

Techniques: Fluorescence, Microscopy, Staining, Binding Assay, Two Tailed Test, Negative Control, Western Blot, Affinity Purification

PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated Con A (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.

Journal:

Article Title: Phosphoinositide Signaling Pathways in Nuclei Are Associated with Nuclear Speckles Containing Pre-mRNA Processing Factors

doi:

Figure Lengend Snippet: PIPKs and PIP2 were not associated with invaginations of the nuclear envelope. Invaginations of the nuclear envelope can transverse nuclei (Fricker et al., 1997 ) and produce a series of dots (arrows) seen here in thin optical sections of methanol-fixed human 2RA fibroblasts labeled with biotin-conjugated Con A (a lectin that binds mannose residues of nuclear envelope glycoproteins). Thin optical sections of the triple-labeling with anti-PIPKIα (A) or anti-PIPKIIα (E) polyclonal antibodies, Con A (C and G) and anti-PIP2 mAb AM212 (B and F) are shown. The overlay of PIPK and Con A staining patterns is shown in yellow (D and H). Bar, 10 μm.

Article Snippet: Biotin-conjugated concanavalin A (Con A; Vector Laboratories, Burlingame, CA) was used after methanol fixation like a primary antibody and was detected with Texas Red–conjugated streptavidin ( Jackson ImmunoResearch ).

Techniques: Labeling, Staining