Structured Review

Biochrom fetal bovine serum fbs
Physicochemical properties of Ptx-loaded SPIONs. Notes: ( A ) Hydrodynamic diameter of Ptx-loaded and unloaded particles in water and different cell culture media. ( B ) Dialysis-based release kinetics of SPION-adsorbed Ptx compared with free Ptx. ( C , D ) ζ potential as a function of pH in SPION LA-HSA and SPION LA-HSA-Ptx during ( C ) forward titration and ( D ) backward titration. ( E ) Magnetization curves showing the M(H) data of SPION LA-HSA and SPION LA-HSA-Ptx . ( F ) AC susceptibility spectra of SPION LA-HSA and SPION LA-HSA-Ptx . ( G , H ) Fourier transform infrared spectroscopy spectra of ( G ) SPION LA-HSA , SPION LA-HSA-Ptx , and ( H ) free Ptx. ( I ) Stability of SPION LA-HSA and SPION LA-HSA-Ptx in human blood. SPIONs coated with lauric acid and aminated human serum albumin (SPION LA-HSA-NH2 ) were used as a positive control for nonstable particles. Negative control = corresponding amount of H 2 O instead of water-based ferrofluid. Representative images were recorded using optical bright-field microscopy. Abbreviations: DMEM, <t>Dulbecco’s</t> Modified Eagle’s Medium; EDTA, ethylenediaminetetraacetic acid; <t>FBS,</t> fetal bovine serum; H, applied magnetic field; M φ, magnetization; Ptx, paclitaxel; RPMI, Roswell Park Memorial Institute; SPION, superparamagnetic iron oxide nanoparticles; SPION LA-HSA , lauric acid- and human serum albumin-coated SPIONs; SPION LA-HSA-NH2 , lauric acid- and aminated human serum albumin-coated SPIONs; SPION LA-HSA-Ptx , SPION LA-HSA functionalized with Ptx; Xi, real part of the magnetic susceptibility; Xii, imaginary part of the magnetic susceptibility.
Fetal Bovine Serum Fbs, supplied by Biochrom, used in various techniques. Bioz Stars score: 94/100, based on 217 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fetal bovine serum fbs/product/Biochrom
Average 94 stars, based on 217 article reviews
Price from $9.99 to $1999.99
fetal bovine serum fbs - by Bioz Stars, 2020-07
94/100 stars

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1) Product Images from "Cellular effects of paclitaxel-loaded iron oxide nanoparticles on breast cancer using different 2D and 3D cell culture models"

Article Title: Cellular effects of paclitaxel-loaded iron oxide nanoparticles on breast cancer using different 2D and 3D cell culture models

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S187886

Physicochemical properties of Ptx-loaded SPIONs. Notes: ( A ) Hydrodynamic diameter of Ptx-loaded and unloaded particles in water and different cell culture media. ( B ) Dialysis-based release kinetics of SPION-adsorbed Ptx compared with free Ptx. ( C , D ) ζ potential as a function of pH in SPION LA-HSA and SPION LA-HSA-Ptx during ( C ) forward titration and ( D ) backward titration. ( E ) Magnetization curves showing the M(H) data of SPION LA-HSA and SPION LA-HSA-Ptx . ( F ) AC susceptibility spectra of SPION LA-HSA and SPION LA-HSA-Ptx . ( G , H ) Fourier transform infrared spectroscopy spectra of ( G ) SPION LA-HSA , SPION LA-HSA-Ptx , and ( H ) free Ptx. ( I ) Stability of SPION LA-HSA and SPION LA-HSA-Ptx in human blood. SPIONs coated with lauric acid and aminated human serum albumin (SPION LA-HSA-NH2 ) were used as a positive control for nonstable particles. Negative control = corresponding amount of H 2 O instead of water-based ferrofluid. Representative images were recorded using optical bright-field microscopy. Abbreviations: DMEM, Dulbecco’s Modified Eagle’s Medium; EDTA, ethylenediaminetetraacetic acid; FBS, fetal bovine serum; H, applied magnetic field; M φ, magnetization; Ptx, paclitaxel; RPMI, Roswell Park Memorial Institute; SPION, superparamagnetic iron oxide nanoparticles; SPION LA-HSA , lauric acid- and human serum albumin-coated SPIONs; SPION LA-HSA-NH2 , lauric acid- and aminated human serum albumin-coated SPIONs; SPION LA-HSA-Ptx , SPION LA-HSA functionalized with Ptx; Xi, real part of the magnetic susceptibility; Xii, imaginary part of the magnetic susceptibility.
Figure Legend Snippet: Physicochemical properties of Ptx-loaded SPIONs. Notes: ( A ) Hydrodynamic diameter of Ptx-loaded and unloaded particles in water and different cell culture media. ( B ) Dialysis-based release kinetics of SPION-adsorbed Ptx compared with free Ptx. ( C , D ) ζ potential as a function of pH in SPION LA-HSA and SPION LA-HSA-Ptx during ( C ) forward titration and ( D ) backward titration. ( E ) Magnetization curves showing the M(H) data of SPION LA-HSA and SPION LA-HSA-Ptx . ( F ) AC susceptibility spectra of SPION LA-HSA and SPION LA-HSA-Ptx . ( G , H ) Fourier transform infrared spectroscopy spectra of ( G ) SPION LA-HSA , SPION LA-HSA-Ptx , and ( H ) free Ptx. ( I ) Stability of SPION LA-HSA and SPION LA-HSA-Ptx in human blood. SPIONs coated with lauric acid and aminated human serum albumin (SPION LA-HSA-NH2 ) were used as a positive control for nonstable particles. Negative control = corresponding amount of H 2 O instead of water-based ferrofluid. Representative images were recorded using optical bright-field microscopy. Abbreviations: DMEM, Dulbecco’s Modified Eagle’s Medium; EDTA, ethylenediaminetetraacetic acid; FBS, fetal bovine serum; H, applied magnetic field; M φ, magnetization; Ptx, paclitaxel; RPMI, Roswell Park Memorial Institute; SPION, superparamagnetic iron oxide nanoparticles; SPION LA-HSA , lauric acid- and human serum albumin-coated SPIONs; SPION LA-HSA-NH2 , lauric acid- and aminated human serum albumin-coated SPIONs; SPION LA-HSA-Ptx , SPION LA-HSA functionalized with Ptx; Xi, real part of the magnetic susceptibility; Xii, imaginary part of the magnetic susceptibility.

Techniques Used: Cell Culture, Titration, Spectroscopy, Positive Control, Negative Control, Microscopy, Modification

2) Product Images from "Complexation with C60 Fullerene Increases Doxorubicin Efficiency against Leukemic Cells In Vitro"

Article Title: Complexation with C60 Fullerene Increases Doxorubicin Efficiency against Leukemic Cells In Vitro

Journal: Nanoscale Research Letters

doi: 10.1186/s11671-019-2894-1

Hydrodynamic size (diameter, nm) of 1 μM С 60 -Dox complexes in RPMI cell culture medium supplemented with 10% FBS at 0 ( a ) and 72-h ( b ) incubation. Intensity (%) percentage of all scattered light intensity
Figure Legend Snippet: Hydrodynamic size (diameter, nm) of 1 μM С 60 -Dox complexes in RPMI cell culture medium supplemented with 10% FBS at 0 ( a ) and 72-h ( b ) incubation. Intensity (%) percentage of all scattered light intensity

Techniques Used: Cell Culture, Incubation

Related Articles

Modification:

Article Title: Cellular effects of paclitaxel-loaded iron oxide nanoparticles on breast cancer using different 2D and 3D cell culture models
Article Snippet: .. Fetal bovine serum (FBS) and Dulbecco’s Modified Eagle’s Medium (DMEM) were provided by Biochrom (Berlin, Germany). .. Human insulin was obtained from Sanofi (Paris, France).

Article Title: Screening of the Open Source Malaria Box Reveals an Early Lead Compound for the Treatment of Alveolar Echinococcosis
Article Snippet: .. Dulbecco’s modified Eagle medium (DMEM) and fetal bovine serum (FBS) were from Biochrom (Berlin, Germany), and all other cell culture reagents were from Gibco-BRL (Zürich, Switzerland). ..

Incubation:

Article Title: Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability *
Article Snippet: .. For the incubation of SH-SY5Y cells with aggregated Tau protein, cells were maintained in a 96-well plate in DMEM/Ham's F-12 medium supplemented with 15% (v/v) fetal bovine serum (FBS), 2 m m l -glutamine, non-essential amino acids (Biochrom AG), 50 μg/ml gentamicin (PAA Laboratories), and 15 m m HEPES, pH 7.4, in a 5% CO2 environment at 37 °C for 24 h. Afterward, cells were maintained for 24 h in 185 μl of the described medium containing only 2% (v/v) FBS. .. Then 15 μl/well aggregated Tau protein were added to the cells for 48 h. MTT (Sigma) was added in triplicate to cells to a final concentration of 1 mg/ml, and cells were incubated for 2 h. After incubation, cell culture medium with MTT was removed, 200 μl of DMSO and 25 μl of Soerensen's glycine buffer (0.1 m glycine, pH 10.5, 0.1 m NaCl) per well were added, and absorbance values were measured at 550 nm (HT3 microtiter plate reader).

Cell Culture:

Article Title: Screening of the Open Source Malaria Box Reveals an Early Lead Compound for the Treatment of Alveolar Echinococcosis
Article Snippet: .. Dulbecco’s modified Eagle medium (DMEM) and fetal bovine serum (FBS) were from Biochrom (Berlin, Germany), and all other cell culture reagents were from Gibco-BRL (Zürich, Switzerland). ..

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    Biochrom fbs
    BCR ablation leads to reduced metabolic flexibility. (A) Pictures show Mito Tracker Red-CMXRos staining alone (upper panels) and overlaid with transmitted light (lower panels) of WT and KO cells (magnification 63×, scale bar = 5 μm). (B) Cells were plated on d0 with or without oligomycin and cell numbers were assessed on d1 and d2 using the CCK8-kit. Values were normalized to the measurement obtained on d1. Statistical significance was determines using the ANOVA test. N = 7; * P = 0.0213 and 0.0341, ** P = 0.0012. (C) Cells were left untreated or incubated with oligomycin overnight. Cells were resupsended in medium containing pyruvate, glutamine, and glucose, and OCR was measured using Seahorse flux technology. One of three independent experiments is shown. a, oligomycin, b, FCCP, c, rotenone + antimycin. (D) Cells were cultured in glucose free <t>RPMI+</t> dialyzed <t>FBS</t> in the presence of 10 mM glucose, 10 mM galactose, or 10 mM GlutaMAX with or without oligomycin. Cell numbers were assessed using the CCK8 kit after overnight incubation. Results are normalized to the values obtained from the untreated sample cultured with glucose. Differences between the indicated pairs of samples were tested for significance using the unpaired t test. N = 3; * P = 0.0242, ** P = 0.0033 and 0.0059, *** P = 0.0005 and 0.0002. KO, BCR-KO Ramos cells; WT, Ramos wild-type cells.
    Fbs, supplied by Biochrom, used in various techniques. Bioz Stars score: 92/100, based on 563 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fbs/product/Biochrom
    Average 92 stars, based on 563 article reviews
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    BCR ablation leads to reduced metabolic flexibility. (A) Pictures show Mito Tracker Red-CMXRos staining alone (upper panels) and overlaid with transmitted light (lower panels) of WT and KO cells (magnification 63×, scale bar = 5 μm). (B) Cells were plated on d0 with or without oligomycin and cell numbers were assessed on d1 and d2 using the CCK8-kit. Values were normalized to the measurement obtained on d1. Statistical significance was determines using the ANOVA test. N = 7; * P = 0.0213 and 0.0341, ** P = 0.0012. (C) Cells were left untreated or incubated with oligomycin overnight. Cells were resupsended in medium containing pyruvate, glutamine, and glucose, and OCR was measured using Seahorse flux technology. One of three independent experiments is shown. a, oligomycin, b, FCCP, c, rotenone + antimycin. (D) Cells were cultured in glucose free RPMI+ dialyzed FBS in the presence of 10 mM glucose, 10 mM galactose, or 10 mM GlutaMAX with or without oligomycin. Cell numbers were assessed using the CCK8 kit after overnight incubation. Results are normalized to the values obtained from the untreated sample cultured with glucose. Differences between the indicated pairs of samples were tested for significance using the unpaired t test. N = 3; * P = 0.0242, ** P = 0.0033 and 0.0059, *** P = 0.0005 and 0.0002. KO, BCR-KO Ramos cells; WT, Ramos wild-type cells.

    Journal: Life Science Alliance

    Article Title: Immunoglobulin expression in the endoplasmic reticulum shapes the metabolic fitness of B lymphocytes

    doi: 10.26508/lsa.202000700

    Figure Lengend Snippet: BCR ablation leads to reduced metabolic flexibility. (A) Pictures show Mito Tracker Red-CMXRos staining alone (upper panels) and overlaid with transmitted light (lower panels) of WT and KO cells (magnification 63×, scale bar = 5 μm). (B) Cells were plated on d0 with or without oligomycin and cell numbers were assessed on d1 and d2 using the CCK8-kit. Values were normalized to the measurement obtained on d1. Statistical significance was determines using the ANOVA test. N = 7; * P = 0.0213 and 0.0341, ** P = 0.0012. (C) Cells were left untreated or incubated with oligomycin overnight. Cells were resupsended in medium containing pyruvate, glutamine, and glucose, and OCR was measured using Seahorse flux technology. One of three independent experiments is shown. a, oligomycin, b, FCCP, c, rotenone + antimycin. (D) Cells were cultured in glucose free RPMI+ dialyzed FBS in the presence of 10 mM glucose, 10 mM galactose, or 10 mM GlutaMAX with or without oligomycin. Cell numbers were assessed using the CCK8 kit after overnight incubation. Results are normalized to the values obtained from the untreated sample cultured with glucose. Differences between the indicated pairs of samples were tested for significance using the unpaired t test. N = 3; * P = 0.0242, ** P = 0.0033 and 0.0059, *** P = 0.0005 and 0.0002. KO, BCR-KO Ramos cells; WT, Ramos wild-type cells.

    Article Snippet: 0.6 × 106 or 1 × 106 cells were incubated in 1 ml RPMI (Thermo Fisher Scientific) + 1% FBS (Biochrom AG) + 15 μl Indo-1 solution at 37°C for 45 min.

    Techniques: Staining, Incubation, Cell Culture

    Amino acid starvation causes TSC2 lysosomal localization in a Rag-dependent manner (A,C) TSC2 accumulates on lysosomes upon amino acid deprivation. Confocal micrograph of HEK293FT cells (A) or MEFs (C) treated +/− all amino acids in the presence of dialyzed FBS for the indicated times, stained for TSC2 (green) and the lysosomal marker LAMP2 (red). LAMP2 aggregates do not show TSC2 accumulation in the +aa condition. (B) TSC2 quickly relocalizes away from lysosomes upon amino acid readdition. HEK293FT cells, starved for amino acids in the presence of dialyzed serum for 4h, then re-supplied with amino acid-containing media for 5 minutes. Cells stained and imaged as in (A).

    Journal: Cell

    Article Title: Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2

    doi: 10.1016/j.cell.2014.01.024

    Figure Lengend Snippet: Amino acid starvation causes TSC2 lysosomal localization in a Rag-dependent manner (A,C) TSC2 accumulates on lysosomes upon amino acid deprivation. Confocal micrograph of HEK293FT cells (A) or MEFs (C) treated +/− all amino acids in the presence of dialyzed FBS for the indicated times, stained for TSC2 (green) and the lysosomal marker LAMP2 (red). LAMP2 aggregates do not show TSC2 accumulation in the +aa condition. (B) TSC2 quickly relocalizes away from lysosomes upon amino acid readdition. HEK293FT cells, starved for amino acids in the presence of dialyzed serum for 4h, then re-supplied with amino acid-containing media for 5 minutes. Cells stained and imaged as in (A).

    Article Snippet: HEK293FT cells (Invitrogen) and mouse embryonic fibroblasts were cultured in high glucose DMEM, supplemented with 10% FBS (Biochrom), except PTEN−/− MEFS which were also supplemented with 2mM Glutamine.

    Techniques: Staining, Marker

    Lysosomal recruitment of TSC2 depends on the Rag proteins (A-A’) Lysosomal localization of TSC2 upon amino acid removal requires the LAMTOR complex. Confocal micrograph of p14/LAMTOR2 knock-out MEFs (A), or control p14 knock-out MEFs reconstituted to express an EGFP-p14 fusion (A’), treated +/− amino acids for 1h in the presence of dialyzed FBS. Lysosomes marked either with anti-LAMP2 antibody or with the lysosomaly localized EGFP-p14. (B) Lysosomal localization of TSC2 upon amino acid removal requires the Rag proteins. MEFs transfected with control siRNA against Renilla luciferase or siRNAs targeting the various Rag proteins, treated +/− amino acids for 1h in the presence of dialyzed FBS. Cells stained and imaged as in (A). (C) Lysosomal localization of TSC2 upon amino acid removal requires that the Rag proteins change to the inactive conformation. MEFs transfected with control siRNA or siRNAs targeting components of the GATOR1 complex DEPDC5, NPRL2, or NPRL3 required for the Rag proteins to become inactive upon amino acid removal. Cells stained and imaged as in (A).

    Journal: Cell

    Article Title: Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2

    doi: 10.1016/j.cell.2014.01.024

    Figure Lengend Snippet: Lysosomal recruitment of TSC2 depends on the Rag proteins (A-A’) Lysosomal localization of TSC2 upon amino acid removal requires the LAMTOR complex. Confocal micrograph of p14/LAMTOR2 knock-out MEFs (A), or control p14 knock-out MEFs reconstituted to express an EGFP-p14 fusion (A’), treated +/− amino acids for 1h in the presence of dialyzed FBS. Lysosomes marked either with anti-LAMP2 antibody or with the lysosomaly localized EGFP-p14. (B) Lysosomal localization of TSC2 upon amino acid removal requires the Rag proteins. MEFs transfected with control siRNA against Renilla luciferase or siRNAs targeting the various Rag proteins, treated +/− amino acids for 1h in the presence of dialyzed FBS. Cells stained and imaged as in (A). (C) Lysosomal localization of TSC2 upon amino acid removal requires that the Rag proteins change to the inactive conformation. MEFs transfected with control siRNA or siRNAs targeting components of the GATOR1 complex DEPDC5, NPRL2, or NPRL3 required for the Rag proteins to become inactive upon amino acid removal. Cells stained and imaged as in (A).

    Article Snippet: HEK293FT cells (Invitrogen) and mouse embryonic fibroblasts were cultured in high glucose DMEM, supplemented with 10% FBS (Biochrom), except PTEN−/− MEFS which were also supplemented with 2mM Glutamine.

    Techniques: Knock-Out, Transfection, Luciferase, Staining

    TSC2 is required for mTOR to localize away from lysosomes upon amino acid removal in a Rheb dependent manner (A-B) mTOR is released from lysosomes upon amino acid removal in control (A) but not TSC2-null MEFs (A’). This is rescued by re-expressing TSC2 + EGFP (to mark transfected cells) but not EGFP alone in the TSC-null MEFs (B). Note that the cell expressing TSC2 and GFP no longer has mTOR accumulated on lysosomes, whereas the surrounding, non-transfected cells retain lysosomally localized mTOR. (C) Defective release of mTOR from lysosomes upon amino acid withdrawal in TSC2-null MEFs is rescued by knocking down Rheb. TSC2-null MEFs transfected with either Rheb siRNAs (upper panels) or control siRNAs (lower panels) treated 1h with +/− amino acid containing medium in the presence of dialyzed FBS.

    Journal: Cell

    Article Title: Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2

    doi: 10.1016/j.cell.2014.01.024

    Figure Lengend Snippet: TSC2 is required for mTOR to localize away from lysosomes upon amino acid removal in a Rheb dependent manner (A-B) mTOR is released from lysosomes upon amino acid removal in control (A) but not TSC2-null MEFs (A’). This is rescued by re-expressing TSC2 + EGFP (to mark transfected cells) but not EGFP alone in the TSC-null MEFs (B). Note that the cell expressing TSC2 and GFP no longer has mTOR accumulated on lysosomes, whereas the surrounding, non-transfected cells retain lysosomally localized mTOR. (C) Defective release of mTOR from lysosomes upon amino acid withdrawal in TSC2-null MEFs is rescued by knocking down Rheb. TSC2-null MEFs transfected with either Rheb siRNAs (upper panels) or control siRNAs (lower panels) treated 1h with +/− amino acid containing medium in the presence of dialyzed FBS.

    Article Snippet: HEK293FT cells (Invitrogen) and mouse embryonic fibroblasts were cultured in high glucose DMEM, supplemented with 10% FBS (Biochrom), except PTEN−/− MEFS which were also supplemented with 2mM Glutamine.

    Techniques: Expressing, Transfection

    Physicochemical properties of Ptx-loaded SPIONs. Notes: ( A ) Hydrodynamic diameter of Ptx-loaded and unloaded particles in water and different cell culture media. ( B ) Dialysis-based release kinetics of SPION-adsorbed Ptx compared with free Ptx. ( C , D ) ζ potential as a function of pH in SPION LA-HSA and SPION LA-HSA-Ptx during ( C ) forward titration and ( D ) backward titration. ( E ) Magnetization curves showing the M(H) data of SPION LA-HSA and SPION LA-HSA-Ptx . ( F ) AC susceptibility spectra of SPION LA-HSA and SPION LA-HSA-Ptx . ( G , H ) Fourier transform infrared spectroscopy spectra of ( G ) SPION LA-HSA , SPION LA-HSA-Ptx , and ( H ) free Ptx. ( I ) Stability of SPION LA-HSA and SPION LA-HSA-Ptx in human blood. SPIONs coated with lauric acid and aminated human serum albumin (SPION LA-HSA-NH2 ) were used as a positive control for nonstable particles. Negative control = corresponding amount of H 2 O instead of water-based ferrofluid. Representative images were recorded using optical bright-field microscopy. Abbreviations: DMEM, Dulbecco’s Modified Eagle’s Medium; EDTA, ethylenediaminetetraacetic acid; FBS, fetal bovine serum; H, applied magnetic field; M φ, magnetization; Ptx, paclitaxel; RPMI, Roswell Park Memorial Institute; SPION, superparamagnetic iron oxide nanoparticles; SPION LA-HSA , lauric acid- and human serum albumin-coated SPIONs; SPION LA-HSA-NH2 , lauric acid- and aminated human serum albumin-coated SPIONs; SPION LA-HSA-Ptx , SPION LA-HSA functionalized with Ptx; Xi, real part of the magnetic susceptibility; Xii, imaginary part of the magnetic susceptibility.

    Journal: International Journal of Nanomedicine

    Article Title: Cellular effects of paclitaxel-loaded iron oxide nanoparticles on breast cancer using different 2D and 3D cell culture models

    doi: 10.2147/IJN.S187886

    Figure Lengend Snippet: Physicochemical properties of Ptx-loaded SPIONs. Notes: ( A ) Hydrodynamic diameter of Ptx-loaded and unloaded particles in water and different cell culture media. ( B ) Dialysis-based release kinetics of SPION-adsorbed Ptx compared with free Ptx. ( C , D ) ζ potential as a function of pH in SPION LA-HSA and SPION LA-HSA-Ptx during ( C ) forward titration and ( D ) backward titration. ( E ) Magnetization curves showing the M(H) data of SPION LA-HSA and SPION LA-HSA-Ptx . ( F ) AC susceptibility spectra of SPION LA-HSA and SPION LA-HSA-Ptx . ( G , H ) Fourier transform infrared spectroscopy spectra of ( G ) SPION LA-HSA , SPION LA-HSA-Ptx , and ( H ) free Ptx. ( I ) Stability of SPION LA-HSA and SPION LA-HSA-Ptx in human blood. SPIONs coated with lauric acid and aminated human serum albumin (SPION LA-HSA-NH2 ) were used as a positive control for nonstable particles. Negative control = corresponding amount of H 2 O instead of water-based ferrofluid. Representative images were recorded using optical bright-field microscopy. Abbreviations: DMEM, Dulbecco’s Modified Eagle’s Medium; EDTA, ethylenediaminetetraacetic acid; FBS, fetal bovine serum; H, applied magnetic field; M φ, magnetization; Ptx, paclitaxel; RPMI, Roswell Park Memorial Institute; SPION, superparamagnetic iron oxide nanoparticles; SPION LA-HSA , lauric acid- and human serum albumin-coated SPIONs; SPION LA-HSA-NH2 , lauric acid- and aminated human serum albumin-coated SPIONs; SPION LA-HSA-Ptx , SPION LA-HSA functionalized with Ptx; Xi, real part of the magnetic susceptibility; Xii, imaginary part of the magnetic susceptibility.

    Article Snippet: Fetal bovine serum (FBS) and Dulbecco’s Modified Eagle’s Medium (DMEM) were provided by Biochrom (Berlin, Germany).

    Techniques: Cell Culture, Titration, Spectroscopy, Positive Control, Negative Control, Microscopy, Modification