Review

goat anti human ldlr polyclonal antibody (R&D Systems)

R&D Systems is a verified supplier

R&D Systems manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

R&D Systems goat anti human ldlr polyclonal antibody

Determination of <t>LDLR</t> expression in PBMC-derived macrophages from wild-type individuals and patients carrying the exon13_15dup. (A) Left panel, representative dot plot corresponding to macrophages from FMO control, wild-type subjects and heterozygous carrier of the exon13_15dup variant. (B) MFI quantification of the LDLR marker from samples from wild-type individuals (n=7) and patients carrying the exon13_15dup variant (n=3) (****p < 0.0001). FSC, Forward scatter; LDLR, LDL receptor; FMO, LDLR negative labeling; FH, Familial Hypercholesterolemia; He, Heterozygous; FSC, Forward Scatter.

Goat Anti Human Ldlr Polyclonal Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 97 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+human+ldlr/Human+LDLR+Antibody/pmc13002427-45-19-24
Average 93 stars, based on 97 article reviews

goat anti human ldlr polyclonal antibody - by Bioz Stars, 2026-10

93/100 stars

Images

1) Product Images from "Functional analysis from ex-vivo characterization of LDLR exon 13–15 duplication associated to familial hypercholesterolemia"

Article Title: Functional analysis from ex-vivo characterization of LDLR exon 13–15 duplication associated to familial hypercholesterolemia

Journal: Frontiers in Endocrinology

doi: 10.3389/fendo.2026.1733372

Determination of LDLR expression in PBMC-derived macrophages from wild-type individuals and patients carrying the exon13_15dup. (A) Left panel, representative dot plot corresponding to macrophages from FMO control, wild-type subjects and heterozygous carrier of the exon13_15dup variant. (B) MFI quantification of the LDLR marker from samples from wild-type individuals (n=7) and patients carrying the exon13_15dup variant (n=3) (****p < 0.0001). FSC, Forward scatter; LDLR, LDL receptor; FMO, LDLR negative labeling; FH, Familial Hypercholesterolemia; He, Heterozygous; FSC, Forward Scatter.

Figure Legend Snippet: Determination of LDLR expression in PBMC-derived macrophages from wild-type individuals and patients carrying the exon13_15dup. (A) Left panel, representative dot plot corresponding to macrophages from FMO control, wild-type subjects and heterozygous carrier of the exon13_15dup variant. (B) MFI quantification of the LDLR marker from samples from wild-type individuals (n=7) and patients carrying the exon13_15dup variant (n=3) (****p < 0.0001). FSC, Forward scatter; LDLR, LDL receptor; FMO, LDLR negative labeling; FH, Familial Hypercholesterolemia; He, Heterozygous; FSC, Forward Scatter.

Techniques Used: Expressing, Derivative Assay, Control, Variant Assay, Marker, Labeling

Immunocytochemistry of LDLR and subcelular marker in macrophages derived from PBMC of Exon13_15dup patients. (A, C, E) Representative images at 40x magnification of the wild-type and Exon13_15dup genotypes colocalization of LDLR with calreticulin, clathrin and LAMP-1. (B, D, F) Quantification of LDLR marker colocalization in samples from wild-type and patients carrying the variant with the subcellular markers. Colocalization was determined by image deconvolution and Pearson compression measurement using ImageJ. Wild type individuals (n=5)) and patients carrying the exon13_15dup variant (n=3). *= p<0.05, **= p<0.01, ns= non significant.

Figure Legend Snippet: Immunocytochemistry of LDLR and subcelular marker in macrophages derived from PBMC of Exon13_15dup patients. (A, C, E) Representative images at 40x magnification of the wild-type and Exon13_15dup genotypes colocalization of LDLR with calreticulin, clathrin and LAMP-1. (B, D, F) Quantification of LDLR marker colocalization in samples from wild-type and patients carrying the variant with the subcellular markers. Colocalization was determined by image deconvolution and Pearson compression measurement using ImageJ. Wild type individuals (n=5)) and patients carrying the exon13_15dup variant (n=3). *= p<0.05, **= p<0.01, ns= non significant.

Techniques Used: Immunocytochemistry, Marker, Derivative Assay, Variant Assay

Incubation:

Article Title: Methods of treating elevated plasma cholesterol
Article Snippet: Proteins were separated by 8% SDS polyacrylamide gel electrophoresis, blotted on nitrocellulose membranes (Bio-Rad), and blocked for 1 h in Tris-buffered saline-Tween 20 (TBS-T; 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.1% Tween 20) containing 5% nonfat dry milk. .. Membranes were then incubated overnight in TBS-T supplemented with 1% nonfat milk and the indicated antibodies; goat anti-human LDLR (1:1000; catalog no. AF2148, R&D Systems), rabbit anti-actin (1:5000; catalog no. A2066, Sigma-Aldrich). .. Appropriate HRP-conjugated secondary antibodies (1:10,000; GE healthcare) were used for detection using the Western Lightning Ultra chemiluminescence kit (catalog no. NEI112001EA, PerkinElmer Life Sciences) and BioFlex EC Films (catalog no. CLEC810, InterScience).

Article Title: Proteolysis of the low-density lipoprotein receptor in hepatocytes is mediated by BMP1 but not by other astacin proteases.
Article Snippet: .. Membranes were incubated overnight at 4 °C in primary antibody diluted in 2% BSA in PBS-T: goat anti-human LDLR (AF2148), goat anti-mouse LDLR (AF2255; R&D Systems, Minneapolis, MN, USA), chicken anti-LDLR (Ab14056; Abcam, Cambridge, UK) at a dilution of 1 : 1000, and anti-actin antibody (Sigma-Aldrich) at a dilution of 1 : 10 000. .. Membranes were washed in PBS-T and then incubated with the appropriate peroxidaseconjugated secondary antibody, rabbit anti-goat, rabbit antichicken or rabbit anti-mouse (Sigma-Aldrich) at a 1 : 4000 dilution in 2% BSA in PBS-T. Membranes were washed in PBS-T with a final wash in PBS before detection by the enhanced chemiluminescence detection method using Pierce Enhanced Chemiluminescence Western Blotting Substrate (Fisher Thermo Scientific, Cramlington, Northumberland, UK).

Article Title: A virus-like particle-based bivalent PCSK9 vaccine lowers LDL-cholesterol levels in non-human primates
Article Snippet: Protein samples were separated by SDS-PAGE and transferred onto nitrocellulose membranes (Bio-Rad). .. Membranes were probed using goat anti-mouse LDLR at a 1:500 dilution (catalogue number AF2255; R&D Systems) or goat anti-human LDLR at a 1:500 dilution (catalogue number AF2148; R&D Systems) followed by incubation with an anti-goat IgG horseradish peroxidase-conjugated secondary antibody at a 1:1000 dilution (catalogue number HAF107; R&D Systems). .. As a control, blots were also probed with an HRP-labeled rabbit anti-ß-actin monoclonal antibody at a 1:1000 dilution (catalogue number #5152; Cell Signaling Technology).

Article Title: A virus-like particle-based bivalent PCSK9 vaccine lowers LDL-cholesterol levels in non-human primates.
Article Snippet: Protein samples were separated by SDS-PAGE and transferred onto nitrocellulose membranes (Bio-Rad). .. Membranes were probed using goat anti-mouse LDLR at a 1:500 dilution (catalogue number AF2255; R&D Systems) or goat anti-human LDLR at a 1:500 dilution (catalogue number AF2148; R&D Systems) followed by incubation with an anti-goat IgG horseradish peroxidase-conjugated secondary antibody at a 1:1000 dilution (catalogue number HAF107; R&D Systems). .. As a control, blots were also probed with an HRP-labeled rabbit anti-ß-actin monoclonal antibody at a 1:1000 dilution (catalogue number #5152; Cell Signaling Technology).

Article Title: Methods of treating elevated plasma cholesterol
Article Snippet: .. Cells were permeabilized or not with 0.1% Triton X-100/PBS for 10 min, and incubated with 150 mM glycine (to stabilize the aldehydes), incubated for 30 min with 1% BSA (Fraction V, Sigma) containing 0.1% Triton X-100 or not, followed by overnight incubation at 4° C. with goat anti-human LDLR (1:100; R&D Systems, catalog no. AF2148). .. Afterward, cells were incubated for 60 min with corresponding Alexa Fluor-conjugated secondary antibodies (Molecular Probes) and mounted in 90% glycerol containing 5% 1,4-diazabicyclo[2.2.2]octane (Sigma).

Image Search Results

Journal: Frontiers in Endocrinology

Article Title: Functional analysis from ex-vivo characterization of LDLR exon 13–15 duplication associated to familial hypercholesterolemia

doi: 10.3389/fendo.2026.1733372

Figure Lengend Snippet: Determination of LDLR expression in PBMC-derived macrophages from wild-type individuals and patients carrying the exon13_15dup. (A) Left panel, representative dot plot corresponding to macrophages from FMO control, wild-type subjects and heterozygous carrier of the exon13_15dup variant. (B) MFI quantification of the LDLR marker from samples from wild-type individuals (n=7) and patients carrying the exon13_15dup variant (n=3) (****p < 0.0001). FSC, Forward scatter; LDLR, LDL receptor; FMO, LDLR negative labeling; FH, Familial Hypercholesterolemia; He, Heterozygous; FSC, Forward Scatter.

Article Snippet: The cells were washed with Tris-PO 4 buffer and incubated overnight at 4°C with the following antibodies: 2 μg/mL goat anti-human LDLR polyclonal antibody (R&D Systems), 20 μg/mL calreticulin and 30 μg/mL lysosomal-associated membrane protein 1 (LAMP1).

Techniques: Expressing, Derivative Assay, Control, Variant Assay, Marker, Labeling

Journal: Frontiers in Endocrinology

Article Title: Functional analysis from ex-vivo characterization of LDLR exon 13–15 duplication associated to familial hypercholesterolemia

doi: 10.3389/fendo.2026.1733372

Figure Lengend Snippet: Immunocytochemistry of LDLR and subcelular marker in macrophages derived from PBMC of Exon13_15dup patients. (A, C, E) Representative images at 40x magnification of the wild-type and Exon13_15dup genotypes colocalization of LDLR with calreticulin, clathrin and LAMP-1. (B, D, F) Quantification of LDLR marker colocalization in samples from wild-type and patients carrying the variant with the subcellular markers. Colocalization was determined by image deconvolution and Pearson compression measurement using ImageJ. Wild type individuals (n=5)) and patients carrying the exon13_15dup variant (n=3). *= p<0.05, **= p<0.01, ns= non significant.

Techniques: Immunocytochemistry, Marker, Derivative Assay, Variant Assay

Characterization of LDLR-specific antibodies. (a) ELISA binding of recombinant Fabs against the cLDLR antigen. Absorbance was read at 450 nm. An anti-CDCP1 Fab 4A06 was used as a negative isotype control. Each sample was tested in biological duplicate and error bars represented standard deviations. (b) Flow cytometry of different Fabs binding to LDLR + MDA-MB-231 cells. Then 50 nM of each Fab was incubated with cells for 30 min and washed twice, followed by AF647 conjugated goat antihuman IgG (H+L) antibody staining for 15 min. (c) Epitope binning of two anti-LDLR Fabs, 142F1 and 142F6, revealed two different epitopes on cLDLR. Biotinylated cLDLR was captured using a streptavidin biosensor and indicated antibodies at a concentration of 200 nM were incubated for 10 min followed by incubation with 50 nM of the second competing antibodies for 5 min. (d) BLI analysis of 142F1 and 142F6 Fabs to estimate their affinities to cLDLR. Biontinylated cLDLR was immobilized via the streptavidin biosensor and varying concentrations of each Fab was injected. Black lines were the experimental trace obtained from the BLI experiments and colored lines were the global fits. (e) Internalization of pH-sensitive Phrodo red-labeled LDL on HeLa cells after 30 min pretreatment with LDL, heparin, or each Fab, respectively. Total integrated intensity is calculated by ROCU × μm 2 /image on the Incucyte software. Each sample was tested in biological triplicate and error bars represent standard deviations. Statistics were calculated by one-way ANOVA and Holm–Sidak multiple comparisons test.

Journal: Journal of the American Chemical Society

Article Title: Hijacking Extracellular Targeted Protein Degrader–Drug Conjugates for Enhanced Drug Delivery

doi: 10.1021/jacs.5c15047

Figure Lengend Snippet: Characterization of LDLR-specific antibodies. (a) ELISA binding of recombinant Fabs against the cLDLR antigen. Absorbance was read at 450 nm. An anti-CDCP1 Fab 4A06 was used as a negative isotype control. Each sample was tested in biological duplicate and error bars represented standard deviations. (b) Flow cytometry of different Fabs binding to LDLR + MDA-MB-231 cells. Then 50 nM of each Fab was incubated with cells for 30 min and washed twice, followed by AF647 conjugated goat antihuman IgG (H+L) antibody staining for 15 min. (c) Epitope binning of two anti-LDLR Fabs, 142F1 and 142F6, revealed two different epitopes on cLDLR. Biotinylated cLDLR was captured using a streptavidin biosensor and indicated antibodies at a concentration of 200 nM were incubated for 10 min followed by incubation with 50 nM of the second competing antibodies for 5 min. (d) BLI analysis of 142F1 and 142F6 Fabs to estimate their affinities to cLDLR. Biontinylated cLDLR was immobilized via the streptavidin biosensor and varying concentrations of each Fab was injected. Black lines were the experimental trace obtained from the BLI experiments and colored lines were the global fits. (e) Internalization of pH-sensitive Phrodo red-labeled LDL on HeLa cells after 30 min pretreatment with LDL, heparin, or each Fab, respectively. Total integrated intensity is calculated by ROCU × μm 2 /image on the Incucyte software. Each sample was tested in biological triplicate and error bars represent standard deviations. Statistics were calculated by one-way ANOVA and Holm–Sidak multiple comparisons test.

Article Snippet: Antibodies used included rabbit anti-human EGFR (Cell Signaling Technology, catalog no. 4267S, 1:1000), rabbit anti-human PD-L1 (Cell Signaling Technology, catalog no. 13684S, 1:1000), rabbit anti-human CXCR4 (Cell Signaling Technology, catalog no. 64837S, 1:1000), rabbit anti-human ERBB2 (Cell Signaling Technology, catalog no. 4290S, 1:1000), rabbit anti-human CDCP1 (Cell Signaling Technology, catalog no. 13794S, 1:1000), mouse anti-human α-tubulin (Cell Signaling Technology, 3873S, 1:3000), goat anti-human LDLR (R&D Systems, catalog no. AF2148, 1:1000), IRDye 800CW goat anti-rabbit IgG (LI-COR Biosciences, catalog no. 926-32211), IRDye 680RD goat anti-mouse IgG (LI-COR Biosciences, catalog no. 926-68070, 1:5000), IRDye 800CW donkey anti-goat IgG (LI-COR Biosciences, catalog no. 926-32214, 1:5000), and peroxidase goat anti-rabbit IgG (H+L) (Jackson ImmunoResearch, catalog no. 111-035-144, 1:5000).

Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Recombinant, Control, Flow Cytometry, Incubation, Staining, Concentration Assay, Injection, Labeling, Software

Generation of LIPTACs for degradation of EGFR. (a) Schematic illustration of LDLR-Ctx LIPTAC bispecific constructs. (b) Western blot showing degradation of total EGFR on HeLa cells following 24 h of treatment with Ctx-LIPTAC or 50 nM control antibodies. Data represents three biological replicates. Percent EGFR levels were quantified by ImageJ relative to PBS control. (c) Changes in surface EGFR based on flow cytometry analysis on MDA-MB-231 cells following 24 h of 50 nM 142F1 isotype IgG, Ctx IgG, Ctx-LIPTAC, or Ctx-KineTAC treatment. Percent EGFR was determined by median fluorescence intensity (MFI) of the PE fluorescence channel of live cells. Each sample was tested in biological triplicate and error bars represented standard deviation. Statistics were calculated by unpaired two-tailed student t test. *** P < 0.001. **** P < 0.0001. (d) Western blot showing degradation of total EGFR on MDA-MB-231 cells after 24 h treatment of 50 nM Ctx, KineTAC, monomeric LDLR isotype, or varying concetrations of LIPTACs. Data represented three biological replicates. (e) EGFR degradation in A431 cells following 24 h of Ctx-LIPTAC1 treatment. Data represents three biological replicates. (f) Flow cytometry analysis showing degradation of surface EGFR on A431 cells following 24 h of Ctx-LIPTACs, 50 nM Ctx IgG, and 50 nM Ctx-KineTAC treatment. Each sample was tested in biological triplicate and error bars represent standard deviations. Statistics were calculated by unpaired two-tailed student t test. *** P < 0.001. **** P < 0.0001. (g) Western blot analysis of EGFR and LDLR in LDLR knockout and control HCC1143 cells after 24 h of 5 nM LIPTAC treatment. Data represent two biological replicates. (h) Fold-change in surface protein abundance in MDA-MB-231 cells following 48 h of treatment with or without 50 nM Ctx-LIPTAC1, as measured by quantitative proteomics analysis. N-Linked cell surface glycoproteins were captured by the cell-surface capture technology and enriched by biocytin hydrazide. Surface proteins were annotated using the SURFY database. (i) Confocal microscopy images of HeLa cells treated with 50 nM of indicated bispecific antibodies or isotype controls for 24 h. Scale bar, 10 μm.

Journal: Journal of the American Chemical Society

Article Title: Hijacking Extracellular Targeted Protein Degrader–Drug Conjugates for Enhanced Drug Delivery

doi: 10.1021/jacs.5c15047

Figure Lengend Snippet: Generation of LIPTACs for degradation of EGFR. (a) Schematic illustration of LDLR-Ctx LIPTAC bispecific constructs. (b) Western blot showing degradation of total EGFR on HeLa cells following 24 h of treatment with Ctx-LIPTAC or 50 nM control antibodies. Data represents three biological replicates. Percent EGFR levels were quantified by ImageJ relative to PBS control. (c) Changes in surface EGFR based on flow cytometry analysis on MDA-MB-231 cells following 24 h of 50 nM 142F1 isotype IgG, Ctx IgG, Ctx-LIPTAC, or Ctx-KineTAC treatment. Percent EGFR was determined by median fluorescence intensity (MFI) of the PE fluorescence channel of live cells. Each sample was tested in biological triplicate and error bars represented standard deviation. Statistics were calculated by unpaired two-tailed student t test. *** P < 0.001. **** P < 0.0001. (d) Western blot showing degradation of total EGFR on MDA-MB-231 cells after 24 h treatment of 50 nM Ctx, KineTAC, monomeric LDLR isotype, or varying concetrations of LIPTACs. Data represented three biological replicates. (e) EGFR degradation in A431 cells following 24 h of Ctx-LIPTAC1 treatment. Data represents three biological replicates. (f) Flow cytometry analysis showing degradation of surface EGFR on A431 cells following 24 h of Ctx-LIPTACs, 50 nM Ctx IgG, and 50 nM Ctx-KineTAC treatment. Each sample was tested in biological triplicate and error bars represent standard deviations. Statistics were calculated by unpaired two-tailed student t test. *** P < 0.001. **** P < 0.0001. (g) Western blot analysis of EGFR and LDLR in LDLR knockout and control HCC1143 cells after 24 h of 5 nM LIPTAC treatment. Data represent two biological replicates. (h) Fold-change in surface protein abundance in MDA-MB-231 cells following 48 h of treatment with or without 50 nM Ctx-LIPTAC1, as measured by quantitative proteomics analysis. N-Linked cell surface glycoproteins were captured by the cell-surface capture technology and enriched by biocytin hydrazide. Surface proteins were annotated using the SURFY database. (i) Confocal microscopy images of HeLa cells treated with 50 nM of indicated bispecific antibodies or isotype controls for 24 h. Scale bar, 10 μm.

Techniques: Construct, Western Blot, Control, Flow Cytometry, Fluorescence, Standard Deviation, Two Tailed Test, Knock-Out, Quantitative Proteomics, Confocal Microscopy

Review

goat anti human ldlr polyclonal antibody (R&D Systems)

Structured Review

Images

1) Product Images from "Functional analysis from ex-vivo characterization of LDLR exon 13–15 duplication associated to familial hypercholesterolemia"

Related Articles

Incubation:

Similar Products

Image Search Results