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lrp2 apex2 v5 mouse  (Jackson Laboratory)

 
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    Jackson Laboratory lrp2 apex2 v5 mouse
    NGAL protein immunoblot shows that urine NGALa biomarker of kidney injuryis not elevated in <t>Lrp2</t> APEX2‑‑V5/+ mice. Comparison with the deletion of Lrp2 in the proximal tubule of the kidney. Equal amounts of urine creatinine were loaded onto each lane. F, female M, male.
    Lrp2 Apex2 V5 Mouse, supplied by Jackson Laboratory, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lrp2+apex2+v5+mouse/pmc13140602-202-1-8?v=Jackson+Laboratory
    Average 86 stars, based on 1 article reviews
    lrp2 apex2 v5 mouse - by Bioz Stars, 2026-07
    86/100 stars

    Images

    1) Product Images from "Proximity Labeling Reveals How Lrp2 Interacts with the Endocytic Machine"

    Article Title: Proximity Labeling Reveals How Lrp2 Interacts with the Endocytic Machine

    Journal: Journal of Proteome Research

    doi: 10.1021/acs.jproteome.5c01053

    NGAL protein immunoblot shows that urine NGALa biomarker of kidney injuryis not elevated in Lrp2 APEX2‑‑V5/+ mice. Comparison with the deletion of Lrp2 in the proximal tubule of the kidney. Equal amounts of urine creatinine were loaded onto each lane. F, female M, male.
    Figure Legend Snippet: NGAL protein immunoblot shows that urine NGALa biomarker of kidney injuryis not elevated in Lrp2 APEX2‑‑V5/+ mice. Comparison with the deletion of Lrp2 in the proximal tubule of the kidney. Equal amounts of urine creatinine were loaded onto each lane. F, female M, male.

    Techniques Used: Western Blot, Biomarker Discovery, Comparison

    Proximal tubules are biotinylated in vitro and in vivo. (A) Lrp2 APEX‑V52/+ proximal tubule membrane fractions were biotinylated in vitro in the presence of H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blot using HRP-conjugated streptavidin (1:5000). (B) Renal artery was cannulated and perfused with bromophenol blue (1 mg/mL), producing blue urine filling the bladder. (C) Lrp2 APEX2‑V5/+ kidney was perfused with biotin phenol and H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blotting using HRP-conjugated streptavidin (1:5000). (D) Expression of the LRP2 APEX2‑V5 fusion protein in vivo. Note that Lrp2 and V5 immunoreactivity colocalize with biotinylation, which is detected by apical staining with 488-Avidin in the proximal tubule.
    Figure Legend Snippet: Proximal tubules are biotinylated in vitro and in vivo. (A) Lrp2 APEX‑V52/+ proximal tubule membrane fractions were biotinylated in vitro in the presence of H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blot using HRP-conjugated streptavidin (1:5000). (B) Renal artery was cannulated and perfused with bromophenol blue (1 mg/mL), producing blue urine filling the bladder. (C) Lrp2 APEX2‑V5/+ kidney was perfused with biotin phenol and H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blotting using HRP-conjugated streptavidin (1:5000). (D) Expression of the LRP2 APEX2‑V5 fusion protein in vivo. Note that Lrp2 and V5 immunoreactivity colocalize with biotinylation, which is detected by apical staining with 488-Avidin in the proximal tubule.

    Techniques Used: In Vitro, In Vivo, Membrane, Magnetic Beads, Western Blot, Expressing, Staining, Avidin-Biotin Assay

    Specificity of LRP2 APEX2‑V5/+ . Fresh, unfixed kidney thick sections (0.5 mm) were treated with biotin-phenol. (A) Wild-type kidney sections. Note the absence of both the V5 c-terminal tag and biotinylation (streptavidin staining). (B) Lrp2 APEX2‑V5/+ kidney sections depict both the V5 c-terminal tag and biotinylation (streptavidin staining). Biotinylation exclusively colocalizes with Lrp2 and V5 immunoreactivity in the apical domain of the proximal tubule. Biotinylation is dependent on H 2 O 2 .
    Figure Legend Snippet: Specificity of LRP2 APEX2‑V5/+ . Fresh, unfixed kidney thick sections (0.5 mm) were treated with biotin-phenol. (A) Wild-type kidney sections. Note the absence of both the V5 c-terminal tag and biotinylation (streptavidin staining). (B) Lrp2 APEX2‑V5/+ kidney sections depict both the V5 c-terminal tag and biotinylation (streptavidin staining). Biotinylation exclusively colocalizes with Lrp2 and V5 immunoreactivity in the apical domain of the proximal tubule. Biotinylation is dependent on H 2 O 2 .

    Techniques Used: Staining

    Localization of LRP2 APEX2‑V5/+ biotinylated proteins. Lrp2 C-terminal-dependent biotinylation in vivo identified cytoplasmic neighbors. Colocalization of biotinylation (detected by 488-avidin) with target proteins and with the V5 tag begins at the tubular pole of the glomerulus at the initiation of the proximal tubule epithelia (top panel). Colocalized protein refers to staining for the proteins named on the left side of the lower panels.
    Figure Legend Snippet: Localization of LRP2 APEX2‑V5/+ biotinylated proteins. Lrp2 C-terminal-dependent biotinylation in vivo identified cytoplasmic neighbors. Colocalization of biotinylation (detected by 488-avidin) with target proteins and with the V5 tag begins at the tubular pole of the glomerulus at the initiation of the proximal tubule epithelia (top panel). Colocalized protein refers to staining for the proteins named on the left side of the lower panels.

    Techniques Used: In Vivo, Avidin-Biotin Assay, Staining

    Immuno-isolation of endosomes containing c-terminal Lrp2 APEX‑V5 . (A) Kidney membrane fractions were prepared on an OptiPrep step gradient (top two steps are shown). (B) Bradford protein assay of each gradient fraction. (C) Lrp2 immunoblot of gradient fractions (with equal protein loading). Lrp2 is concentrated in lanes 6–8. (D) Western blot showing immuno-isolation of Lrp2 APEX‑V5 endosomes from OptiPrep fractions 6–8 using anti-V5 nanobody beads: Lane 1 = OptiPrep fractions; Lane 2 = nanobody bead flow-through; Lane 3 = Capture of V5 + , Lrp2 + , Cubn + , Alb + endosomes. (E) Western blot showing introduction of myoglobin prior to kidney fractionation on OptiPrep step gradients and anti-V5 nanobody bead pulldowns from different pooled OptiPrep fractions (2−3, 4−5, 6−7, 8−9, 10−11). Myoglobin is found in Lrp2 + endosomes along with the Lrp2 endocytic adaptor protein, DAB2.
    Figure Legend Snippet: Immuno-isolation of endosomes containing c-terminal Lrp2 APEX‑V5 . (A) Kidney membrane fractions were prepared on an OptiPrep step gradient (top two steps are shown). (B) Bradford protein assay of each gradient fraction. (C) Lrp2 immunoblot of gradient fractions (with equal protein loading). Lrp2 is concentrated in lanes 6–8. (D) Western blot showing immuno-isolation of Lrp2 APEX‑V5 endosomes from OptiPrep fractions 6–8 using anti-V5 nanobody beads: Lane 1 = OptiPrep fractions; Lane 2 = nanobody bead flow-through; Lane 3 = Capture of V5 + , Lrp2 + , Cubn + , Alb + endosomes. (E) Western blot showing introduction of myoglobin prior to kidney fractionation on OptiPrep step gradients and anti-V5 nanobody bead pulldowns from different pooled OptiPrep fractions (2−3, 4−5, 6−7, 8−9, 10−11). Myoglobin is found in Lrp2 + endosomes along with the Lrp2 endocytic adaptor protein, DAB2.

    Techniques Used: Isolation, Membrane, Bradford Protein Assay, Western Blot, Fractionation



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    lrp2 apex2 v5 mouse  (Jackson Laboratory)
    86
    Jackson Laboratory lrp2 apex2 v5 mouse
    NGAL protein immunoblot shows that urine NGALa biomarker of kidney injuryis not elevated in <t>Lrp2</t> APEX2‑‑V5/+ mice. Comparison with the deletion of Lrp2 in the proximal tubule of the kidney. Equal amounts of urine creatinine were loaded onto each lane. F, female M, male.
    Lrp2 Apex2 V5 Mouse, supplied by Jackson Laboratory, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lrp2+apex2+v5+mouse/pmc13140602-202-1-8?v=Jackson+Laboratory
    Average 86 stars, based on 1 article reviews
    lrp2 apex2 v5 mouse - by Bioz Stars, 2026-07
    86/100 stars
    		  Buy from Supplier

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    NGAL protein immunoblot shows that urine NGALa biomarker of kidney injuryis not elevated in Lrp2 APEX2‑‑V5/+ mice. Comparison with the deletion of Lrp2 in the proximal tubule of the kidney. Equal amounts of urine creatinine were loaded onto each lane. F, female M, male.

    Journal: Journal of Proteome Research

    Article Title: Proximity Labeling Reveals How Lrp2 Interacts with the Endocytic Machine

    doi: 10.1021/acs.jproteome.5c01053

    Figure Lengend Snippet: NGAL protein immunoblot shows that urine NGALa biomarker of kidney injuryis not elevated in Lrp2 APEX2‑‑V5/+ mice. Comparison with the deletion of Lrp2 in the proximal tubule of the kidney. Equal amounts of urine creatinine were loaded onto each lane. F, female M, male.

    Article Snippet: The LRP2 APEX2‐V5 mouse has been deposited at Jackson Laboratories as JAX Strain name: Lrp2-APEX2; Jax Strain ID: 419746.

    Techniques: Western Blot, Biomarker Discovery, Comparison

    Proximal tubules are biotinylated in vitro and in vivo. (A) Lrp2 APEX‑V52/+ proximal tubule membrane fractions were biotinylated in vitro in the presence of H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blot using HRP-conjugated streptavidin (1:5000). (B) Renal artery was cannulated and perfused with bromophenol blue (1 mg/mL), producing blue urine filling the bladder. (C) Lrp2 APEX2‑V5/+ kidney was perfused with biotin phenol and H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blotting using HRP-conjugated streptavidin (1:5000). (D) Expression of the LRP2 APEX2‑V5 fusion protein in vivo. Note that Lrp2 and V5 immunoreactivity colocalize with biotinylation, which is detected by apical staining with 488-Avidin in the proximal tubule.

    Journal: Journal of Proteome Research

    Article Title: Proximity Labeling Reveals How Lrp2 Interacts with the Endocytic Machine

    doi: 10.1021/acs.jproteome.5c01053

    Figure Lengend Snippet: Proximal tubules are biotinylated in vitro and in vivo. (A) Lrp2 APEX‑V52/+ proximal tubule membrane fractions were biotinylated in vitro in the presence of H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blot using HRP-conjugated streptavidin (1:5000). (B) Renal artery was cannulated and perfused with bromophenol blue (1 mg/mL), producing blue urine filling the bladder. (C) Lrp2 APEX2‑V5/+ kidney was perfused with biotin phenol and H 2 O 2 , and biotinylated proteins were precipitated with streptavidin magnetic beads. The samples were analyzed by Western blotting using HRP-conjugated streptavidin (1:5000). (D) Expression of the LRP2 APEX2‑V5 fusion protein in vivo. Note that Lrp2 and V5 immunoreactivity colocalize with biotinylation, which is detected by apical staining with 488-Avidin in the proximal tubule.

    Article Snippet: The LRP2 APEX2‐V5 mouse has been deposited at Jackson Laboratories as JAX Strain name: Lrp2-APEX2; Jax Strain ID: 419746.

    Techniques: In Vitro, In Vivo, Membrane, Magnetic Beads, Western Blot, Expressing, Staining, Avidin-Biotin Assay

    Specificity of LRP2 APEX2‑V5/+ . Fresh, unfixed kidney thick sections (0.5 mm) were treated with biotin-phenol. (A) Wild-type kidney sections. Note the absence of both the V5 c-terminal tag and biotinylation (streptavidin staining). (B) Lrp2 APEX2‑V5/+ kidney sections depict both the V5 c-terminal tag and biotinylation (streptavidin staining). Biotinylation exclusively colocalizes with Lrp2 and V5 immunoreactivity in the apical domain of the proximal tubule. Biotinylation is dependent on H 2 O 2 .

    Journal: Journal of Proteome Research

    Article Title: Proximity Labeling Reveals How Lrp2 Interacts with the Endocytic Machine

    doi: 10.1021/acs.jproteome.5c01053

    Figure Lengend Snippet: Specificity of LRP2 APEX2‑V5/+ . Fresh, unfixed kidney thick sections (0.5 mm) were treated with biotin-phenol. (A) Wild-type kidney sections. Note the absence of both the V5 c-terminal tag and biotinylation (streptavidin staining). (B) Lrp2 APEX2‑V5/+ kidney sections depict both the V5 c-terminal tag and biotinylation (streptavidin staining). Biotinylation exclusively colocalizes with Lrp2 and V5 immunoreactivity in the apical domain of the proximal tubule. Biotinylation is dependent on H 2 O 2 .

    Article Snippet: The LRP2 APEX2‐V5 mouse has been deposited at Jackson Laboratories as JAX Strain name: Lrp2-APEX2; Jax Strain ID: 419746.

    Techniques: Staining

    Localization of LRP2 APEX2‑V5/+ biotinylated proteins. Lrp2 C-terminal-dependent biotinylation in vivo identified cytoplasmic neighbors. Colocalization of biotinylation (detected by 488-avidin) with target proteins and with the V5 tag begins at the tubular pole of the glomerulus at the initiation of the proximal tubule epithelia (top panel). Colocalized protein refers to staining for the proteins named on the left side of the lower panels.

    Journal: Journal of Proteome Research

    Article Title: Proximity Labeling Reveals How Lrp2 Interacts with the Endocytic Machine

    doi: 10.1021/acs.jproteome.5c01053

    Figure Lengend Snippet: Localization of LRP2 APEX2‑V5/+ biotinylated proteins. Lrp2 C-terminal-dependent biotinylation in vivo identified cytoplasmic neighbors. Colocalization of biotinylation (detected by 488-avidin) with target proteins and with the V5 tag begins at the tubular pole of the glomerulus at the initiation of the proximal tubule epithelia (top panel). Colocalized protein refers to staining for the proteins named on the left side of the lower panels.

    Article Snippet: The LRP2 APEX2‐V5 mouse has been deposited at Jackson Laboratories as JAX Strain name: Lrp2-APEX2; Jax Strain ID: 419746.

    Techniques: In Vivo, Avidin-Biotin Assay, Staining

    Immuno-isolation of endosomes containing c-terminal Lrp2 APEX‑V5 . (A) Kidney membrane fractions were prepared on an OptiPrep step gradient (top two steps are shown). (B) Bradford protein assay of each gradient fraction. (C) Lrp2 immunoblot of gradient fractions (with equal protein loading). Lrp2 is concentrated in lanes 6–8. (D) Western blot showing immuno-isolation of Lrp2 APEX‑V5 endosomes from OptiPrep fractions 6–8 using anti-V5 nanobody beads: Lane 1 = OptiPrep fractions; Lane 2 = nanobody bead flow-through; Lane 3 = Capture of V5 + , Lrp2 + , Cubn + , Alb + endosomes. (E) Western blot showing introduction of myoglobin prior to kidney fractionation on OptiPrep step gradients and anti-V5 nanobody bead pulldowns from different pooled OptiPrep fractions (2−3, 4−5, 6−7, 8−9, 10−11). Myoglobin is found in Lrp2 + endosomes along with the Lrp2 endocytic adaptor protein, DAB2.

    Journal: Journal of Proteome Research

    Article Title: Proximity Labeling Reveals How Lrp2 Interacts with the Endocytic Machine

    doi: 10.1021/acs.jproteome.5c01053

    Figure Lengend Snippet: Immuno-isolation of endosomes containing c-terminal Lrp2 APEX‑V5 . (A) Kidney membrane fractions were prepared on an OptiPrep step gradient (top two steps are shown). (B) Bradford protein assay of each gradient fraction. (C) Lrp2 immunoblot of gradient fractions (with equal protein loading). Lrp2 is concentrated in lanes 6–8. (D) Western blot showing immuno-isolation of Lrp2 APEX‑V5 endosomes from OptiPrep fractions 6–8 using anti-V5 nanobody beads: Lane 1 = OptiPrep fractions; Lane 2 = nanobody bead flow-through; Lane 3 = Capture of V5 + , Lrp2 + , Cubn + , Alb + endosomes. (E) Western blot showing introduction of myoglobin prior to kidney fractionation on OptiPrep step gradients and anti-V5 nanobody bead pulldowns from different pooled OptiPrep fractions (2−3, 4−5, 6−7, 8−9, 10−11). Myoglobin is found in Lrp2 + endosomes along with the Lrp2 endocytic adaptor protein, DAB2.

    Article Snippet: The LRP2 APEX2‐V5 mouse has been deposited at Jackson Laboratories as JAX Strain name: Lrp2-APEX2; Jax Strain ID: 419746.

    Techniques: Isolation, Membrane, Bradford Protein Assay, Western Blot, Fractionation