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anti sr b1 antibody (Novus Biologicals)

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Novus Biologicals anti sr b1 antibody

Single knockouts of LDLR and <t>SR-B1</t> are unable to protect from LDL-DHA treatment. ( A ) Western blot showing LDLR expression in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin was used as a loading control. ( B ) LDL-DiI association in wild type MDA-MB-231 and LDLR knockout MDA-MB-231s. Association was done under serum starve conditions with a 6-hour treatment of LDL-DiI, cells were then harvested, and uptake was measured by FACS. ( C ) Dose response to LDL-DHA nanoparticles in wild type and knockout MDA-MB-231s. Cells were treated with increasing doses of LDL-DHA (10–100μM) for 72 hours under serum starve conditions. ( D ) LDL-DiI-OA uptake in wild type and LDLR deficient MDA-MB-231 cell lines. Cells were treated with increasing doses of LDL-DiI-OA for 6 hours under serum starve conditions. Fluorescence intensity of DiI was then measured by FACS. ( E ) LDLR and SR-B1 expression by Western blot in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. LDL-DiI-OA uptake in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. Cells were serum starved overnight followed by treatment with LDL-DiI-OA for 2 hours at 37C. The cells were then collected and mean fluorescence intensity quantified using FACS. For excess HDL group, the cells were pre-treated for 30 min with 40-fold excess HDL. The ldlmSR-B1[S] (specific value, Orange trace) represents the difference between ldlmSR-B1[T], total (green trace) and ldlmSR-B1[NS], nonspecific (purple trace) (40-fold excess unlabeled HDL). ( F ) SR-B1 expression by Western blot in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin is used as a loading control. ( G ) LDL-DiI-OA Uptake in SR-B1 knockout and wild type MDA-MB-231 cells. This was done under serum starve conditions followed by 6-hour treatment with increasing doses of LDL-DiI-OA followed by FACS. ( H ) Dose Response to LDL-DHA in SR-B1 knockout and wild type MDA-MB-231s under serum starve conditions with a dose range of 10–100μM for 72 hours. Data is expressed as mean ± SEM. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Anti Sr B1 Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti sr b1 antibody/product/Novus Biologicals
Average 93 stars, based on 1 article reviews

anti sr b1 antibody - by Bioz Stars, 2026-04

93/100 stars

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1) Product Images from "Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes"

Article Title: Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes

Journal: Breast Cancer : Targets and Therapy

doi: 10.2147/BCTT.S554396

Single knockouts of LDLR and SR-B1 are unable to protect from LDL-DHA treatment. ( A ) Western blot showing LDLR expression in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin was used as a loading control. ( B ) LDL-DiI association in wild type MDA-MB-231 and LDLR knockout MDA-MB-231s. Association was done under serum starve conditions with a 6-hour treatment of LDL-DiI, cells were then harvested, and uptake was measured by FACS. ( C ) Dose response to LDL-DHA nanoparticles in wild type and knockout MDA-MB-231s. Cells were treated with increasing doses of LDL-DHA (10–100μM) for 72 hours under serum starve conditions. ( D ) LDL-DiI-OA uptake in wild type and LDLR deficient MDA-MB-231 cell lines. Cells were treated with increasing doses of LDL-DiI-OA for 6 hours under serum starve conditions. Fluorescence intensity of DiI was then measured by FACS. ( E ) LDLR and SR-B1 expression by Western blot in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. LDL-DiI-OA uptake in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. Cells were serum starved overnight followed by treatment with LDL-DiI-OA for 2 hours at 37C. The cells were then collected and mean fluorescence intensity quantified using FACS. For excess HDL group, the cells were pre-treated for 30 min with 40-fold excess HDL. The ldlmSR-B1[S] (specific value, Orange trace) represents the difference between ldlmSR-B1[T], total (green trace) and ldlmSR-B1[NS], nonspecific (purple trace) (40-fold excess unlabeled HDL). ( F ) SR-B1 expression by Western blot in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin is used as a loading control. ( G ) LDL-DiI-OA Uptake in SR-B1 knockout and wild type MDA-MB-231 cells. This was done under serum starve conditions followed by 6-hour treatment with increasing doses of LDL-DiI-OA followed by FACS. ( H ) Dose Response to LDL-DHA in SR-B1 knockout and wild type MDA-MB-231s under serum starve conditions with a dose range of 10–100μM for 72 hours. Data is expressed as mean ± SEM. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Figure Legend Snippet: Single knockouts of LDLR and SR-B1 are unable to protect from LDL-DHA treatment. ( A ) Western blot showing LDLR expression in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin was used as a loading control. ( B ) LDL-DiI association in wild type MDA-MB-231 and LDLR knockout MDA-MB-231s. Association was done under serum starve conditions with a 6-hour treatment of LDL-DiI, cells were then harvested, and uptake was measured by FACS. ( C ) Dose response to LDL-DHA nanoparticles in wild type and knockout MDA-MB-231s. Cells were treated with increasing doses of LDL-DHA (10–100μM) for 72 hours under serum starve conditions. ( D ) LDL-DiI-OA uptake in wild type and LDLR deficient MDA-MB-231 cell lines. Cells were treated with increasing doses of LDL-DiI-OA for 6 hours under serum starve conditions. Fluorescence intensity of DiI was then measured by FACS. ( E ) LDLR and SR-B1 expression by Western blot in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. LDL-DiI-OA uptake in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. Cells were serum starved overnight followed by treatment with LDL-DiI-OA for 2 hours at 37C. The cells were then collected and mean fluorescence intensity quantified using FACS. For excess HDL group, the cells were pre-treated for 30 min with 40-fold excess HDL. The ldlmSR-B1[S] (specific value, Orange trace) represents the difference between ldlmSR-B1[T], total (green trace) and ldlmSR-B1[NS], nonspecific (purple trace) (40-fold excess unlabeled HDL). ( F ) SR-B1 expression by Western blot in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin is used as a loading control. ( G ) LDL-DiI-OA Uptake in SR-B1 knockout and wild type MDA-MB-231 cells. This was done under serum starve conditions followed by 6-hour treatment with increasing doses of LDL-DiI-OA followed by FACS. ( H ) Dose Response to LDL-DHA in SR-B1 knockout and wild type MDA-MB-231s under serum starve conditions with a dose range of 10–100μM for 72 hours. Data is expressed as mean ± SEM. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Techniques Used: Western Blot, Expressing, Knock-Out, Control, Fluorescence

Inhibition of LDL-DiI-OA with excess LDL and HDL show the balance between LDL and SR-B1. The panel of Breast cancer cells were pre-treated under serum starve conditions with either 200ug LDL 200ug HDL or 200ug LDL+ 200ug HDL, after 1Hr cells were treated with 10ug of LDL-DiI-OA for 6 hours. Fluorescence intensity of DiI was then measured by FACS. Control treatment was done concurrently to normalize data to percentage by dividing total inhibited uptake by control uptake then subtracted from 100% to show total inhibition by treatment condition, each panel show the inhibition plot for each cell with each cell line in the following panels ( A ) MCF7, ( B ) T47D, ( C ) ZR-75-1, ( D ) BT-474, ( E ) SKBR3 ( F ) MDA-MB-468 ( G ) HCC1937 ( H ) MDA-MB-231 ( I ) Hs578T ( J ) SUM-149PT ( K ) MDA-MB-231 LDL-/- and ( L ) MDA-MB-231 SR-B1-/-. Data is expressed as mean ± SEM. *, P<0.05; **, P<0.01; ***, P<0.001 and ****, P<0.0001.

Figure Legend Snippet: Inhibition of LDL-DiI-OA with excess LDL and HDL show the balance between LDL and SR-B1. The panel of Breast cancer cells were pre-treated under serum starve conditions with either 200ug LDL 200ug HDL or 200ug LDL+ 200ug HDL, after 1Hr cells were treated with 10ug of LDL-DiI-OA for 6 hours. Fluorescence intensity of DiI was then measured by FACS. Control treatment was done concurrently to normalize data to percentage by dividing total inhibited uptake by control uptake then subtracted from 100% to show total inhibition by treatment condition, each panel show the inhibition plot for each cell with each cell line in the following panels ( A ) MCF7, ( B ) T47D, ( C ) ZR-75-1, ( D ) BT-474, ( E ) SKBR3 ( F ) MDA-MB-468 ( G ) HCC1937 ( H ) MDA-MB-231 ( I ) Hs578T ( J ) SUM-149PT ( K ) MDA-MB-231 LDL-/- and ( L ) MDA-MB-231 SR-B1-/-. Data is expressed as mean ± SEM. *, P<0.05; **, P<0.01; ***, P<0.001 and ****, P<0.0001.

Techniques Used: Inhibition, Fluorescence, Control

Protein expression of LDLR and SR-B1. ( A ) Western blot of LDLR and SR-B1 receptor expression in panel of breast cancer cells under normal growth conditions. Actin was used as a loading control. ( B ) Quantification of LDLR to Actin ratio and ( C ) SR-B1 to Actin ratio. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Figure Legend Snippet: Protein expression of LDLR and SR-B1. ( A ) Western blot of LDLR and SR-B1 receptor expression in panel of breast cancer cells under normal growth conditions. Actin was used as a loading control. ( B ) Quantification of LDLR to Actin ratio and ( C ) SR-B1 to Actin ratio. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Techniques Used: Expressing, Western Blot, Control

Confocal microscopy of LDL-DiI, HDL-DiI, and LDL-DiI-OA uptake. LDL-DiI and HDL-DiI in MDA-MB-231s is shown to highlight LDLR-mediated endocytosis (LDL-DiI) and SR-B1-mediated selective lipid uptake (HDL-DiI). LDL-DiI-OA is shown in Wild Type, LDLR-/-, and shSR-B1 MDA-MB-231 cells, showing how each uptake pathway is perturbed by these knockouts. LDL-DiI-OA treatment in SKBr3 and ZR-75-1 cells shows respective LDLR-dominant and SR-B1 dominant uptake patterns. Cell type and treatment are listed on the left.

Figure Legend Snippet: Confocal microscopy of LDL-DiI, HDL-DiI, and LDL-DiI-OA uptake. LDL-DiI and HDL-DiI in MDA-MB-231s is shown to highlight LDLR-mediated endocytosis (LDL-DiI) and SR-B1-mediated selective lipid uptake (HDL-DiI). LDL-DiI-OA is shown in Wild Type, LDLR-/-, and shSR-B1 MDA-MB-231 cells, showing how each uptake pathway is perturbed by these knockouts. LDL-DiI-OA treatment in SKBr3 and ZR-75-1 cells shows respective LDLR-dominant and SR-B1 dominant uptake patterns. Cell type and treatment are listed on the left.

Techniques Used: Confocal Microscopy

Use of double knockout of LDLR and SR-B1 shows some rescue to LDL-DHA treatment. ( A ) Use of an SR-B1 antibody to inhibit LDL-DiI-OA Uptake in wild-type LDLR Knockout MDA-MB-231s. Cells were treated under serum-starved conditions, then were given a 1-hour pretreatment of an SR-B1 antibody or mock antibody treatment. Continued cotreatment with LDL-DiI-OA was then performed for 6 hours. Cells were then harvested, and DiI fluorescence was measured by FACS. Data is expressed as mean ± SEM. Statistical analysis was done by a paired Student's T -test with pairs comprising of same cell experimental replicates. ( B ) Protein expression of LDLR and SR-B1 in Wild Type, LDLR-/-, shSR-B1, and LDLR-/- shSR-B1 MDA-MB-231 cells. ( C ) LDL-DiI-OA uptake in MDA-MB-231, LDLR-/- and LDLR-/- shSR-B1. ( D ) Confocal image of MDA-MB-231 LDLR-/- -shSR-B1 cells 2 hours following incubation with LDL-DiI-OA. ( E ) Dose response to a 1-, 3-, 6-, and 24-hour pulse of LDL-DHA. After each pulse (with the exception of 24 hours) the media was changed, and the cell viability was read out at 24 hours. Data is expressed as mean ± SEM. Ψ, P= 0.06, *, P<0.05; **, P<0.01; ***, P<0.001 and ****, P<0.0001. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Figure Legend Snippet: Use of double knockout of LDLR and SR-B1 shows some rescue to LDL-DHA treatment. ( A ) Use of an SR-B1 antibody to inhibit LDL-DiI-OA Uptake in wild-type LDLR Knockout MDA-MB-231s. Cells were treated under serum-starved conditions, then were given a 1-hour pretreatment of an SR-B1 antibody or mock antibody treatment. Continued cotreatment with LDL-DiI-OA was then performed for 6 hours. Cells were then harvested, and DiI fluorescence was measured by FACS. Data is expressed as mean ± SEM. Statistical analysis was done by a paired Student's T -test with pairs comprising of same cell experimental replicates. ( B ) Protein expression of LDLR and SR-B1 in Wild Type, LDLR-/-, shSR-B1, and LDLR-/- shSR-B1 MDA-MB-231 cells. ( C ) LDL-DiI-OA uptake in MDA-MB-231, LDLR-/- and LDLR-/- shSR-B1. ( D ) Confocal image of MDA-MB-231 LDLR-/- -shSR-B1 cells 2 hours following incubation with LDL-DiI-OA. ( E ) Dose response to a 1-, 3-, 6-, and 24-hour pulse of LDL-DHA. After each pulse (with the exception of 24 hours) the media was changed, and the cell viability was read out at 24 hours. Data is expressed as mean ± SEM. Ψ, P= 0.06, *, P<0.05; **, P<0.01; ***, P<0.001 and ****, P<0.0001. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Techniques Used: Double Knockout, Knock-Out, Fluorescence, Expressing, Incubation, Western Blot

Image Search Results

S-nitrosylation of HINT1 aggravates ox-LDL induced foam cell formation through upregulating scavenger receptor A1 and CD36. (A) Representative images and quantification of oil red O staining in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). Scale bar: 50 μm. (B) Representative images and quantification of lipid droplet staining in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). Scale bar: 5 μm. (C) Total cholesterol level in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (D) Representative images and quantification of Dil-ox-LDL uptake in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without Dil-ox-LDL (40 μg/mL) ( n = 6). Scale bar: 20 μm. (E) Cholesterol efflux to HDL was evaluated in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A and treated with or without ox-LDL (100 μg/mL) ( n = 6). (F) Western blot analysis of SR-A1, CD36 and LOX-1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (G) Western blot analysis of SR-B1, ABCA1 and ABCG1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (H) qPCR analysis of SR-A1, CD36 and LOX-1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (I) qPCR analysis of SR-B1, ABCA1 and ABCG1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). Data are presented as mean ± SEM. One-way ANOVA was used in A–C and E–I. Unpaired t -test was used in D.

Journal: Redox Biology

Article Title: S-nitrosylation of HINT1 in macrophages aggravates foam cell formation and atherosclerosis

doi: 10.1016/j.redox.2026.104063

Figure Lengend Snippet: S-nitrosylation of HINT1 aggravates ox-LDL induced foam cell formation through upregulating scavenger receptor A1 and CD36. (A) Representative images and quantification of oil red O staining in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). Scale bar: 50 μm. (B) Representative images and quantification of lipid droplet staining in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). Scale bar: 5 μm. (C) Total cholesterol level in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (D) Representative images and quantification of Dil-ox-LDL uptake in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without Dil-ox-LDL (40 μg/mL) ( n = 6). Scale bar: 20 μm. (E) Cholesterol efflux to HDL was evaluated in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A and treated with or without ox-LDL (100 μg/mL) ( n = 6). (F) Western blot analysis of SR-A1, CD36 and LOX-1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (G) Western blot analysis of SR-B1, ABCA1 and ABCG1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (H) qPCR analysis of SR-A1, CD36 and LOX-1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). (I) qPCR analysis of SR-B1, ABCA1 and ABCG1 in HINT1 KO BMDMs transfected with Lenti-WT or Lenti-C84A followed by treatment with or without ox-LDL (100 μg/mL) ( n = 6). Data are presented as mean ± SEM. One-way ANOVA was used in A–C and E–I. Unpaired t -test was used in D.

Article Snippet: Antibodys against CD36 (18836-1-AP), SR-B1 (21277-1-AP), ABCA1 (26564-1-AP), ABCG1 (13578-1-AP), USF-2 (16614-1-AP), GAPDH (60004-1-lg), β-actin (66009-1-lg), and Tubulin (11224-1-AP) for western blotting, His-tag (66005-1-lg), Flag-tag (20543-1-AP), and HA-tag (51064-2-AP; 66006-2-lg) for western blotting and immunoprecipitation assay were obtained from Proteintech (Chicago, IL, USA); antibody against HINT1 (sc-271790), SR-A1 (sc-166184) for immunoprecipitation assay and immunofluorescence, CD36 (sc-7309) for immunofluorescence, USF2 (sc-293443) for immunoprecipitation assay were obtained from Santa Cruz Biotechnology (CA, USA).

Techniques: Staining, Transfection, Western Blot

Journal: Breast Cancer : Targets and Therapy

Article Title: Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes

doi: 10.2147/BCTT.S554396

Figure Lengend Snippet: Single knockouts of LDLR and SR-B1 are unable to protect from LDL-DHA treatment. ( A ) Western blot showing LDLR expression in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin was used as a loading control. ( B ) LDL-DiI association in wild type MDA-MB-231 and LDLR knockout MDA-MB-231s. Association was done under serum starve conditions with a 6-hour treatment of LDL-DiI, cells were then harvested, and uptake was measured by FACS. ( C ) Dose response to LDL-DHA nanoparticles in wild type and knockout MDA-MB-231s. Cells were treated with increasing doses of LDL-DHA (10–100μM) for 72 hours under serum starve conditions. ( D ) LDL-DiI-OA uptake in wild type and LDLR deficient MDA-MB-231 cell lines. Cells were treated with increasing doses of LDL-DiI-OA for 6 hours under serum starve conditions. Fluorescence intensity of DiI was then measured by FACS. ( E ) LDLR and SR-B1 expression by Western blot in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. LDL-DiI-OA uptake in CHO-K1, LDLA7 and LDLA7-mSRB1 cells. Cells were serum starved overnight followed by treatment with LDL-DiI-OA for 2 hours at 37C. The cells were then collected and mean fluorescence intensity quantified using FACS. For excess HDL group, the cells were pre-treated for 30 min with 40-fold excess HDL. The ldlmSR-B1[S] (specific value, Orange trace) represents the difference between ldlmSR-B1[T], total (green trace) and ldlmSR-B1[NS], nonspecific (purple trace) (40-fold excess unlabeled HDL). ( F ) SR-B1 expression by Western blot in wild type, LDLR and SR-B1 knockout MDA-MB-231s under normal growth conditions. Actin is used as a loading control. ( G ) LDL-DiI-OA Uptake in SR-B1 knockout and wild type MDA-MB-231 cells. This was done under serum starve conditions followed by 6-hour treatment with increasing doses of LDL-DiI-OA followed by FACS. ( H ) Dose Response to LDL-DHA in SR-B1 knockout and wild type MDA-MB-231s under serum starve conditions with a dose range of 10–100μM for 72 hours. Data is expressed as mean ± SEM. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Article Snippet: Anti-SR-B1 antibody was from Novus (#NB400-104).

Techniques: Western Blot, Expressing, Knock-Out, Control, Fluorescence

Journal: Breast Cancer : Targets and Therapy

Article Title: Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes

doi: 10.2147/BCTT.S554396

Figure Lengend Snippet: Inhibition of LDL-DiI-OA with excess LDL and HDL show the balance between LDL and SR-B1. The panel of Breast cancer cells were pre-treated under serum starve conditions with either 200ug LDL 200ug HDL or 200ug LDL+ 200ug HDL, after 1Hr cells were treated with 10ug of LDL-DiI-OA for 6 hours. Fluorescence intensity of DiI was then measured by FACS. Control treatment was done concurrently to normalize data to percentage by dividing total inhibited uptake by control uptake then subtracted from 100% to show total inhibition by treatment condition, each panel show the inhibition plot for each cell with each cell line in the following panels ( A ) MCF7, ( B ) T47D, ( C ) ZR-75-1, ( D ) BT-474, ( E ) SKBR3 ( F ) MDA-MB-468 ( G ) HCC1937 ( H ) MDA-MB-231 ( I ) Hs578T ( J ) SUM-149PT ( K ) MDA-MB-231 LDL-/- and ( L ) MDA-MB-231 SR-B1-/-. Data is expressed as mean ± SEM. *, P<0.05; **, P<0.01; ***, P<0.001 and ****, P<0.0001.

Article Snippet: Anti-SR-B1 antibody was from Novus (#NB400-104).

Techniques: Inhibition, Fluorescence, Control

Journal: Breast Cancer : Targets and Therapy

Article Title: Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes

doi: 10.2147/BCTT.S554396

Figure Lengend Snippet: Protein expression of LDLR and SR-B1. ( A ) Western blot of LDLR and SR-B1 receptor expression in panel of breast cancer cells under normal growth conditions. Actin was used as a loading control. ( B ) Quantification of LDLR to Actin ratio and ( C ) SR-B1 to Actin ratio. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Article Snippet: Anti-SR-B1 antibody was from Novus (#NB400-104).

Techniques: Expressing, Western Blot, Control

Journal: Breast Cancer : Targets and Therapy

Article Title: Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes

doi: 10.2147/BCTT.S554396

Figure Lengend Snippet: Confocal microscopy of LDL-DiI, HDL-DiI, and LDL-DiI-OA uptake. LDL-DiI and HDL-DiI in MDA-MB-231s is shown to highlight LDLR-mediated endocytosis (LDL-DiI) and SR-B1-mediated selective lipid uptake (HDL-DiI). LDL-DiI-OA is shown in Wild Type, LDLR-/-, and shSR-B1 MDA-MB-231 cells, showing how each uptake pathway is perturbed by these knockouts. LDL-DiI-OA treatment in SKBr3 and ZR-75-1 cells shows respective LDLR-dominant and SR-B1 dominant uptake patterns. Cell type and treatment are listed on the left.

Article Snippet: Anti-SR-B1 antibody was from Novus (#NB400-104).

Techniques: Confocal Microscopy

Journal: Breast Cancer : Targets and Therapy

Article Title: Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes

doi: 10.2147/BCTT.S554396

Figure Lengend Snippet: Use of double knockout of LDLR and SR-B1 shows some rescue to LDL-DHA treatment. ( A ) Use of an SR-B1 antibody to inhibit LDL-DiI-OA Uptake in wild-type LDLR Knockout MDA-MB-231s. Cells were treated under serum-starved conditions, then were given a 1-hour pretreatment of an SR-B1 antibody or mock antibody treatment. Continued cotreatment with LDL-DiI-OA was then performed for 6 hours. Cells were then harvested, and DiI fluorescence was measured by FACS. Data is expressed as mean ± SEM. Statistical analysis was done by a paired Student's T -test with pairs comprising of same cell experimental replicates. ( B ) Protein expression of LDLR and SR-B1 in Wild Type, LDLR-/-, shSR-B1, and LDLR-/- shSR-B1 MDA-MB-231 cells. ( C ) LDL-DiI-OA uptake in MDA-MB-231, LDLR-/- and LDLR-/- shSR-B1. ( D ) Confocal image of MDA-MB-231 LDLR-/- -shSR-B1 cells 2 hours following incubation with LDL-DiI-OA. ( E ) Dose response to a 1-, 3-, 6-, and 24-hour pulse of LDL-DHA. After each pulse (with the exception of 24 hours) the media was changed, and the cell viability was read out at 24 hours. Data is expressed as mean ± SEM. Ψ, P= 0.06, *, P<0.05; **, P<0.01; ***, P<0.001 and ****, P<0.0001. Western Blot Molecular weights: LDLR (Upper 140 kD, Lower 92 kD); SR-B1 (82kD); and actin (42 kD).

Article Snippet: Anti-SR-B1 antibody was from Novus (#NB400-104).

Techniques: Double Knockout, Knock-Out, Fluorescence, Expressing, Incubation, Western Blot

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1) Product Images from "Dual Receptor Targeting Ensures Uptake and Anticancer Efficacy of Low-Density Lipoprotein-Docosahexaenoic Acid Nanoparticles Across Breast Cancer Cell Subtypes"

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