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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