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biotin conjugated lectins  (Vector Laboratories)


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    Structured Review

    Vector Laboratories biotin conjugated lectins
    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) <t>lectins.</t> (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
    Biotin Conjugated Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lectin+biotin+conjugate/Lectin+Kit+III%2C+Biotinylated/pmc12614588-53-1-21
    Average 93 stars, based on 62 article reviews
    biotin conjugated lectins - by Bioz Stars, 2026-10
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    Images

    1) Product Images from "UDP-glucuronic acid availability underlies sex difference in renal expression of nonsulfated Human Natural Killer-1 (HNK-1) glycans"

    Article Title: UDP-glucuronic acid availability underlies sex difference in renal expression of nonsulfated Human Natural Killer-1 (HNK-1) glycans

    Journal: PLOS One

    doi: 10.1371/journal.pone.0335730

    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) lectins. (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
    Figure Legend Snippet: (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) lectins. (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.

    Techniques Used: Membrane, Control, Expressing, Western Blot

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    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) <t>lectins.</t> (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
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    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) <t>lectins.</t> (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
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    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) <t>lectins.</t> (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
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    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) <t>lectins.</t> (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
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    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) <t>lectins.</t> (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
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    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) <t>lectins.</t> (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.
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    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) lectins. (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.

    Journal: PLOS One

    Article Title: UDP-glucuronic acid availability underlies sex difference in renal expression of nonsulfated Human Natural Killer-1 (HNK-1) glycans

    doi: 10.1371/journal.pone.0335730

    Figure Lengend Snippet: (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) lectins. (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.

    Article Snippet: When biotin-conjugated lectins were used, HRP labeling was carried out according to the manufacturer’s instructions provided with VECSTAIN ABC Kit (Cat#PK-4000, Vector Laboratories, Newark, CA, USA).

    Techniques: Membrane, Control, Expressing, Western Blot

    (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) lectins. (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.

    Journal: PLOS One

    Article Title: UDP-glucuronic acid availability underlies sex difference in renal expression of nonsulfated Human Natural Killer-1 (HNK-1) glycans

    doi: 10.1371/journal.pone.0335730

    Figure Lengend Snippet: (A) Renal membrane fractions from wild-type mouse kidneys were immunoblotted with the M6749 monoclonal antibody and anti-β-actin monoclonal antibody. β-actin was used as a loading control. All other blots in this figure were performed using the same loading amounts as in (A) . (B) Relative expression levels of nonsulfated HNK-1 glycans (M6749) were quantified based on the band intensities in (A) , normalized to β-actin. (C, E) Renal membrane fractions were blotted with RCA120 (C) and MAM (E) lectins. (D, F) Band signals in (C) and (E) were quantified relative to β-actin. (G) Immunoblots of renal membrane fractions using antibodies against APN and MEP1A. Bands marked by closed and open triangles correspond to the bands shown in (A) . (H, I) Expression levels of nonsulfated HNK-1 glycans associated with APN (H) and MEP1A (I) were quantified from the band intensities indicated by closed and open triangles. All graphs represent mean ± SEM (male, n = 3; female, n = 3). Statistical analysis was performed using Student’s t -test. *: p < 0.05, ***: p < 0.001, n.s.: not significant. “M” and “F” in figures indicate Male and Female, respectively.

    Article Snippet: For lectin blotting, membranes were blocked with Blocking One (Cat#03953–95, Nacalai Tesque) and incubated with HRP- or biotin-conjugated lectins diluted in 5% Blocking One in PBST.

    Techniques: Membrane, Control, Expressing, Western Blot