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polyclonal antibodies targeting cd36 (Innovagen AB)

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Innovagen AB polyclonal antibodies targeting cd36
Polyclonal Antibodies Targeting Cd36, supplied by Innovagen AB, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/polyclonal+antibodies+targeting+cd36/polyclonal+antibodies+targeting+cd36/pm29284680-44-11-12
Average 90 stars, based on 1 article reviews

polyclonal antibodies targeting cd36 - by Bioz Stars, 2026-09

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Article Title: CD36 defines primitive chronic myeloid leukemia cells less responsive to imatinib but vulnerable to antibody-based therapeutic targeting.
Article Snippet: Viable cells were evaluated using CountBright Absolute Counting Beads (Thermo Fisher Inc) and 4',6-diamidino-2-phenylindole (DAPI) on a LSR Fortessa (BD Bioscience) after three days in culture. .. For ADCC assays we used polyclonal antibodies targeting CD36 produced in rabbit (Innovagen, Sweden) and unspecific polyclonal rabbit immunoglobulin G (IgG) isotypes (Abcam) as control. ..

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Figure 1. SR-B1 and CD36 express at the surface of Sf9 cells. Lysates from Sf9 cells infected with SR-B1– or CD36-expressing baculovirus at an MOI of 5 were collected every 24 h post-infection, following incubation with NHS-biotin as described in Experimental procedures. Immunoblot analysis of 40 μl of biotinylated cell surface proteins (top panels) or 15 μg of whole-cell lysates (bottom panels) was performed and receptors were detected using an antibody directed against SR-B1 (approximately 82 kDa) or CD36 (approximately 88 kDa). Immunoblots are representative of four independent infections. SR-B1, scavenger receptor class B type 1; CD36, cluster of differentiation 36; MOI, multiplicity of infection; Sf9, Spodoptera frugiperda.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 1. SR-B1 and CD36 express at the surface of Sf9 cells. Lysates from Sf9 cells infected with SR-B1– or CD36-expressing baculovirus at an MOI of 5 were collected every 24 h post-infection, following incubation with NHS-biotin as described in Experimental procedures. Immunoblot analysis of 40 μl of biotinylated cell surface proteins (top panels) or 15 μg of whole-cell lysates (bottom panels) was performed and receptors were detected using an antibody directed against SR-B1 (approximately 82 kDa) or CD36 (approximately 88 kDa). Immunoblots are representative of four independent infections. SR-B1, scavenger receptor class B type 1; CD36, cluster of differentiation 36; MOI, multiplicity of infection; Sf9, Spodoptera frugiperda.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Infection, Expressing, Incubation, Western Blot

Figure 2. SR-B1–expressing Sf9 cells mediate DiI-HDL binding and DiI-lipid uptake from HDL. Sf9 cells were infected with high-titer baculovirus encoding SR-B1, CD36, or empty vector at an MOI of 5 and immediately plated in 12-well plates. At 72 h post-infection, cells were washed and incubated with 10 μg/ml DiI-HDL in media + 0.5% BSA for 90 min at 4 C to assess binding (A) or at 27 C to assess combined binding and uptake. After 90 min, cells were harvested in PBS/0.5% BSA. MFI was recorded by ﬂow cytometry and DiI uptake (B) was calculated by subtracting the MFI at 4 C from the MFI at 27 C. Data were analyzed by one-way ANOVA and Dunnett’s multiple comparisons, presented as mean ± SD, n = 4 independent infections, with technical replicates performed in duplicate. *p ≤0.05. BSA, bovine serum albumin; CD36, cluster of differentiation 36; DiI, 1,10-dioctadecyl-3,3,30,30-tetramethy- lindocarbocyanine; HDL, high-density lipoprotein; MOI, multiplicity of infection; MST, microscale thermophoresis; Sf9, Spodoptera frugiperda; SR-B1, scav- enger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 2. SR-B1–expressing Sf9 cells mediate DiI-HDL binding and DiI-lipid uptake from HDL. Sf9 cells were infected with high-titer baculovirus encoding SR-B1, CD36, or empty vector at an MOI of 5 and immediately plated in 12-well plates. At 72 h post-infection, cells were washed and incubated with 10 μg/ml DiI-HDL in media + 0.5% BSA for 90 min at 4 C to assess binding (A) or at 27 C to assess combined binding and uptake. After 90 min, cells were harvested in PBS/0.5% BSA. MFI was recorded by ﬂow cytometry and DiI uptake (B) was calculated by subtracting the MFI at 4 C from the MFI at 27 C. Data were analyzed by one-way ANOVA and Dunnett’s multiple comparisons, presented as mean ± SD, n = 4 independent infections, with technical replicates performed in duplicate. *p ≤0.05. BSA, bovine serum albumin; CD36, cluster of differentiation 36; DiI, 1,10-dioctadecyl-3,3,30,30-tetramethy- lindocarbocyanine; HDL, high-density lipoprotein; MOI, multiplicity of infection; MST, microscale thermophoresis; Sf9, Spodoptera frugiperda; SR-B1, scav- enger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Expressing, Binding Assay, Infection, Plasmid Preparation, Incubation, Cytometry, Microscale Thermophoresis

Figure 3. Sf9 cells expressing CD36 increase DiI-oxLDL binding and uptake. Sf9 cells were infected with high-titer baculovirus encoding SR-B1, CD36, or empty vector at an MOI of 5 and immediately plated in 12-well plates. At 72 h post-infection, cells were washed and incubated with 10 μg/ml DiI-oxLDL in media + 0.5% BSA for 90 min at 4 C to assess binding (A) or at 27 C to assess combined binding and uptake. After 90 min, cells were harvested in PBS/0.5% BSA. MFI was recorded by ﬂow cytometry and DiI uptake (B) was calculated by subtracting the MFI at 4 C from the MFI at 27 C. Data were analyzed by one- way ANOVA and Dunnett’s multiple comparisons, presented as mean ± SD, n = 2 independent infections, with technical replicates performed in duplicate. *p ≤0.05 and **p ≤0.01. BSA, bovine serum albumin; CD36, cluster of differentiation 36; DiI, 1,10-dioctadecyl-3,3,30,30-tetramethylindocarbocyanine; MFI, mean ﬂuorescence intensity; MOI, multiplicity of infection; oxLDL, oxidized low-density lipoprotein; Sf9, Spodoptera frugiperda; SR-B1, scavenger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 3. Sf9 cells expressing CD36 increase DiI-oxLDL binding and uptake. Sf9 cells were infected with high-titer baculovirus encoding SR-B1, CD36, or empty vector at an MOI of 5 and immediately plated in 12-well plates. At 72 h post-infection, cells were washed and incubated with 10 μg/ml DiI-oxLDL in media + 0.5% BSA for 90 min at 4 C to assess binding (A) or at 27 C to assess combined binding and uptake. After 90 min, cells were harvested in PBS/0.5% BSA. MFI was recorded by ﬂow cytometry and DiI uptake (B) was calculated by subtracting the MFI at 4 C from the MFI at 27 C. Data were analyzed by one- way ANOVA and Dunnett’s multiple comparisons, presented as mean ± SD, n = 2 independent infections, with technical replicates performed in duplicate. *p ≤0.05 and **p ≤0.01. BSA, bovine serum albumin; CD36, cluster of differentiation 36; DiI, 1,10-dioctadecyl-3,3,30,30-tetramethylindocarbocyanine; MFI, mean ﬂuorescence intensity; MOI, multiplicity of infection; oxLDL, oxidized low-density lipoprotein; Sf9, Spodoptera frugiperda; SR-B1, scavenger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Expressing, Binding Assay, Infection, Plasmid Preparation, Incubation, Cytometry

Figure 4. SR-B1 and CD36 form higher order oligomers in Sf9 Cells. Cell lysates from empty vector (Vec), SR-B1-, or CD36-baculovirus-infected Sf9 cells were collected at 72 h post-infection. Lysates were sonicated and separated by nondenaturing perﬂuorooctanoic acid (PFO)-PAGE on 8% polyacrylamide gels. Immunoblot analysis utilized an antibody against SR- B1 (A) or CD36 (B) was used to detect the formation of monomers (M), dimers (D), and higher order oligomers (HO). Data are representative of immunoblots of lysates from three independent infections. CD36, cluster of differentiation 36; Sf9, Spodoptera frugiperda; SR-B1, scavenger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 4. SR-B1 and CD36 form higher order oligomers in Sf9 Cells. Cell lysates from empty vector (Vec), SR-B1-, or CD36-baculovirus-infected Sf9 cells were collected at 72 h post-infection. Lysates were sonicated and separated by nondenaturing perﬂuorooctanoic acid (PFO)-PAGE on 8% polyacrylamide gels. Immunoblot analysis utilized an antibody against SR- B1 (A) or CD36 (B) was used to detect the formation of monomers (M), dimers (D), and higher order oligomers (HO). Data are representative of immunoblots of lysates from three independent infections. CD36, cluster of differentiation 36; Sf9, Spodoptera frugiperda; SR-B1, scavenger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Plasmid Preparation, Infection, Sonication, Western Blot

Figure 5. Schematic representation of scavenger receptor puriﬁcation protocol. Sf9 cells were infected with baculovirus encoding SR-B1 or CD36, each ﬂanked on the C terminus by a H10 histidine and FLAG tag. Lysates were solubilized with LMNG/CHS detergent (ﬁnal concentration: 0.025% LMNG, 0.005% CHS) and tagged proteins were enriched by ﬂow through a TALON cobalt afﬁnity column. Tags and glycosylations can then be enzymatically removed. Final contaminants were removed by an additional ﬂow through an afﬁnity and desalting column. CD36, cluster of differentiation 36; CHS, cholesteryl hemi- succinate; LMNG, lauryl maltose neopentyl glycol; Sf9, Spodoptera frugiperda; SR-B1, scavenger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 5. Schematic representation of scavenger receptor puriﬁcation protocol. Sf9 cells were infected with baculovirus encoding SR-B1 or CD36, each ﬂanked on the C terminus by a H10 histidine and FLAG tag. Lysates were solubilized with LMNG/CHS detergent (ﬁnal concentration: 0.025% LMNG, 0.005% CHS) and tagged proteins were enriched by ﬂow through a TALON cobalt afﬁnity column. Tags and glycosylations can then be enzymatically removed. Final contaminants were removed by an additional ﬂow through an afﬁnity and desalting column. CD36, cluster of differentiation 36; CHS, cholesteryl hemi- succinate; LMNG, lauryl maltose neopentyl glycol; Sf9, Spodoptera frugiperda; SR-B1, scavenger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Infection, FLAG-tag, Concentration Assay

Figure 6. Puriﬁcation protocol yields pure SR-B1 and CD36. Samples (15 μl) were collected at various points in the puriﬁcation protocol and were separated by SDS-PAGE. Sample quality was veriﬁed by Coomassie blue (A and B) and immunoblot analysis (C and D). Size-exclusion chromatography for SR- B1 (E) or CD36 (F) was also performed. Blots are representative of four independent puriﬁcations. CD36, cluster of differentiation 36; FT, ﬂow-through; SR-B1, scavenger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 6. Puriﬁcation protocol yields pure SR-B1 and CD36. Samples (15 μl) were collected at various points in the puriﬁcation protocol and were separated by SDS-PAGE. Sample quality was veriﬁed by Coomassie blue (A and B) and immunoblot analysis (C and D). Size-exclusion chromatography for SR- B1 (E) or CD36 (F) was also performed. Blots are representative of four independent puriﬁcations. CD36, cluster of differentiation 36; FT, ﬂow-through; SR-B1, scavenger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: SDS Page, Western Blot, Size-exclusion Chromatography

Figure 7. SR-B1 and CD36 remain stable up to 6 weeks post-puriﬁcation. Puriﬁed SR-B1 and CD36 stability was measured up to 6 weeks post-puri- ﬁcation by Prometheus NT.48. Protein unfolding as a function of increasing temperature was monitored by assessing changes in intrinsic tryptophan ﬂuorescence at 330 and 350 nm at 20% power over a temperature gradient from 20C to 90C. Destabilization events for SR-B1 in detergent micelles occurred at 54.7C and 68.6C (A) and at 58.3C and 68.6C for CD36 (B). The destabilization temperatures were calculated by taking the ratio of the ﬁrst derivative values of the sample ﬂuorescence at 350 and 330 nm. Data represent two readings per construct per time point. Details of the thermal shift assay can be found in Experimental procedures. CD36, cluster of differentiation 36; SR-B1, scavenger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 7. SR-B1 and CD36 remain stable up to 6 weeks post-puriﬁcation. Puriﬁed SR-B1 and CD36 stability was measured up to 6 weeks post-puri- ﬁcation by Prometheus NT.48. Protein unfolding as a function of increasing temperature was monitored by assessing changes in intrinsic tryptophan ﬂuorescence at 330 and 350 nm at 20% power over a temperature gradient from 20C to 90C. Destabilization events for SR-B1 in detergent micelles occurred at 54.7C and 68.6C (A) and at 58.3C and 68.6C for CD36 (B). The destabilization temperatures were calculated by taking the ratio of the ﬁrst derivative values of the sample ﬂuorescence at 350 and 330 nm. Data represent two readings per construct per time point. Details of the thermal shift assay can be found in Experimental procedures. CD36, cluster of differentiation 36; SR-B1, scavenger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Construct, Thermal Shift Assay

Figure 9. Puriﬁed CD36 binds to oxLDL and HDL. MST was used to assess binding of Cy5-labeled SR-B1 to various ligands. Measurements were per- formed on the Monolith NT.115 BLUE/RED at 25 C using 40% MST power and laser on/off times of 0 and 21 s. Each point is representative of a single point in a 16-point titration. Apparent Kd values for glycosylated CD36 binding to oxLDL (A, R2 = 0.765) and HDL (B, R2 = 0.845) were calculated by nonlinear regression analysis, assuming one-site speciﬁc binding, of the normalized thermophoresis at increasing ligand concentrations, using GraphPad Prism. Curves are representative of at least two independent puriﬁcations, ligand preparations, and labelings. Further information about MST methods can be found in Experimental procedures. CD36, cluster of differentiation 36; HDL, high-density lipoprotein; MST, microscale thermo- phoresis; oxLDL, oxidized low-density lipoprotein; SR-B1, scavenger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 9. Puriﬁed CD36 binds to oxLDL and HDL. MST was used to assess binding of Cy5-labeled SR-B1 to various ligands. Measurements were per- formed on the Monolith NT.115 BLUE/RED at 25 C using 40% MST power and laser on/off times of 0 and 21 s. Each point is representative of a single point in a 16-point titration. Apparent Kd values for glycosylated CD36 binding to oxLDL (A, R2 = 0.765) and HDL (B, R2 = 0.845) were calculated by nonlinear regression analysis, assuming one-site speciﬁc binding, of the normalized thermophoresis at increasing ligand concentrations, using GraphPad Prism. Curves are representative of at least two independent puriﬁcations, ligand preparations, and labelings. Further information about MST methods can be found in Experimental procedures. CD36, cluster of differentiation 36; HDL, high-density lipoprotein; MST, microscale thermo- phoresis; oxLDL, oxidized low-density lipoprotein; SR-B1, scavenger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Binding Assay, Labeling, Titration

Figure 10. Glycosylation status of SR-B1 and CD36 does not impact ligand binding. Human full-length CD36 or SR-B1 were deglycosylated by PNGase F, as demonstrated by differences in migration by SDS-PAGE (insets). Proteins were subsequently labeled with Cy5 for MST experiments and performed as described in Figures 7 and 8. Apparent Kd values for deglycosylated SR-B1 binding to HDL (A, R2 = 0.952) and deglycosylated CD36 binding to oxLDL (B, R2 = 0.799) were calculated by nonlinear regression analysis, assuming one-site speciﬁc binding, of the normalized thermophoresis at increasing ligand con- centrations, using GraphPad Prism. MST curves of glycosylated proteins were calculated by nonlinear regression analysis, assuming one-site speciﬁc binding, of the normalized thermophoresis at increasing ligand concentrations, using GraphPad Prism. Curves are representative of at least two inde- pendent puriﬁcations, ligand preparations, and labelings. Further information about MST methods can be found in Experimental procedures. CD36, cluster of differentiation 36; HDL, high-density lipoprotein; MST, microscale thermophoresis; oxLDL, oxidized low-density lipoprotein; SR-B1, scavenger receptor class B type 1.

Journal: The Journal of biological chemistry

Article Title: Development and validation of a purification system for functional full-length human SR-B1 and CD36.

doi: 10.1016/j.jbc.2023.105187

Figure Lengend Snippet: Figure 10. Glycosylation status of SR-B1 and CD36 does not impact ligand binding. Human full-length CD36 or SR-B1 were deglycosylated by PNGase F, as demonstrated by differences in migration by SDS-PAGE (insets). Proteins were subsequently labeled with Cy5 for MST experiments and performed as described in Figures 7 and 8. Apparent Kd values for deglycosylated SR-B1 binding to HDL (A, R2 = 0.952) and deglycosylated CD36 binding to oxLDL (B, R2 = 0.799) were calculated by nonlinear regression analysis, assuming one-site speciﬁc binding, of the normalized thermophoresis at increasing ligand con- centrations, using GraphPad Prism. MST curves of glycosylated proteins were calculated by nonlinear regression analysis, assuming one-site speciﬁc binding, of the normalized thermophoresis at increasing ligand concentrations, using GraphPad Prism. Curves are representative of at least two inde- pendent puriﬁcations, ligand preparations, and labelings. Further information about MST methods can be found in Experimental procedures. CD36, cluster of differentiation 36; HDL, high-density lipoprotein; MST, microscale thermophoresis; oxLDL, oxidized low-density lipoprotein; SR-B1, scavenger receptor class B type 1.

Article Snippet: Rabbit polyclonal antibodies targeting CD36 were purchased from Novus Biologicals.

Techniques: Glycoproteomics, Ligand Binding Assay, Migration, SDS Page, Labeling, Binding Assay, Microscale Thermophoresis

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