amicon ultra centrifugal filter  (Millipore)


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  • 99
    Name:
    Amicon Ultra centrifugal filter units
    Description:
    High recovery centrifugal filters for concentrating samples Can be used to concentrate biological samples containing antigens antibodies enzymes nucleic acids or micoorganisms Excellen for use to purify macromolecular components from cell lysates Ideal for desalting and buffer exchanges Swing bucket rotorL 4 000 x g Fixed angle rotor 35 5 000 x g High recovery Ultracel regenerated cellulose membrane in a range of molecular weight cut offs High retentate recovery of 90 Vertical membrane reduces concentration polarization for ultra fast spin times as fast as 10 15 mins Heat sealed membrane minimizes downstream extractables 100 integrity tested for reliable performance Convenient sample monitoring with translucent housing and volume graduations Direct pipettor sample access eliminates processing step to recover concentrate High concentration factors of 80 100X
    Catalog Number:
    z717185
    Price:
    None
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    Structured Review

    Millipore amicon ultra centrifugal filter
    Amicon Ultra centrifugal filter units
    High recovery centrifugal filters for concentrating samples Can be used to concentrate biological samples containing antigens antibodies enzymes nucleic acids or micoorganisms Excellen for use to purify macromolecular components from cell lysates Ideal for desalting and buffer exchanges Swing bucket rotorL 4 000 x g Fixed angle rotor 35 5 000 x g High recovery Ultracel regenerated cellulose membrane in a range of molecular weight cut offs High retentate recovery of 90 Vertical membrane reduces concentration polarization for ultra fast spin times as fast as 10 15 mins Heat sealed membrane minimizes downstream extractables 100 integrity tested for reliable performance Convenient sample monitoring with translucent housing and volume graduations Direct pipettor sample access eliminates processing step to recover concentrate High concentration factors of 80 100X
    https://www.bioz.com/result/amicon ultra centrifugal filter/product/Millipore
    Average 99 stars, based on 66 article reviews
    Price from $9.99 to $1999.99
    amicon ultra centrifugal filter - by Bioz Stars, 2020-08
    99/100 stars

    Images

    1) Product Images from "Structural basis for the interaction of protein S1 with the Escherichia coli ribosome"

    Article Title: Structural basis for the interaction of protein S1 with the Escherichia coli ribosome

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gku1314

    Free S1 NTS binds to the ribosome and interferes with translation of the canonical ompA mRNA. ( A ) Purified S1-depleted 30S ribosomes (30S(-S1)) were incubated in the absence (lanes 1 and 2) or in the presence of FITC labelled S1 NTS (lanes 7 and 8), native protein S1 (lanes 9 and 10) or both (lanes 11 and 12). Likewise, FITC labelled S1 NTS (lanes 3 and 4) or native S1 (lanes 5 and 6) were incubated in the absence of ribosomes. Before (input; lanes 1, 3, 5, 7, 9 and 11) and after ultrafiltration using 100 kDa MWCO Amicon concentrators (Millipore) samples were taken and the presence of the respective proteins and the S1 NTS peptide in the ribosome fraction (ribosome fraction; lanes 2, 4, 6, 8, 10 and 12) was determined by SDS-PAGE. ( B ) In vitro translation of ompA mRNA in the absence (lane 1) or in the presence of a 10- or 50-fold molar excess over ribosomes of S1 NTD (lanes 2 and 3), S1 D1 (lanes 4 and 5) or S1 NTS (lanes 6 and 7), respectively. The assay was performed in triplicate and one representative autoradiograph is shown. Graph representing the quantification of three independent assays is given below. Error bars represent the standard deviation of the mean.
    Figure Legend Snippet: Free S1 NTS binds to the ribosome and interferes with translation of the canonical ompA mRNA. ( A ) Purified S1-depleted 30S ribosomes (30S(-S1)) were incubated in the absence (lanes 1 and 2) or in the presence of FITC labelled S1 NTS (lanes 7 and 8), native protein S1 (lanes 9 and 10) or both (lanes 11 and 12). Likewise, FITC labelled S1 NTS (lanes 3 and 4) or native S1 (lanes 5 and 6) were incubated in the absence of ribosomes. Before (input; lanes 1, 3, 5, 7, 9 and 11) and after ultrafiltration using 100 kDa MWCO Amicon concentrators (Millipore) samples were taken and the presence of the respective proteins and the S1 NTS peptide in the ribosome fraction (ribosome fraction; lanes 2, 4, 6, 8, 10 and 12) was determined by SDS-PAGE. ( B ) In vitro translation of ompA mRNA in the absence (lane 1) or in the presence of a 10- or 50-fold molar excess over ribosomes of S1 NTD (lanes 2 and 3), S1 D1 (lanes 4 and 5) or S1 NTS (lanes 6 and 7), respectively. The assay was performed in triplicate and one representative autoradiograph is shown. Graph representing the quantification of three independent assays is given below. Error bars represent the standard deviation of the mean.

    Techniques Used: Purification, Incubation, SDS Page, In Vitro, Autoradiography, Standard Deviation

    2) Product Images from "Bacterial lipoproteins constitute the TLR2-stimulating activity of Serum Amyloid A"

    Article Title: Bacterial lipoproteins constitute the TLR2-stimulating activity of Serum Amyloid A

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    doi: 10.4049/jimmunol.1800503

    Lipopeptides associated with SAA confer its ability to stimulate TNFα production. 100 ng/ml LPS ( A ), 100 ng/ml Pam3CSK4 (Pam, B ), and 1¼g/ml apoSAA ( C ) were incubated with lipoprotein lipase (LPL), and then used to stimulate J774 cells. Culture supernatants were collected 24 hours later and TNFα concentrations were measured by ELISA. Human SAA1 from Origene produced in HEK cells (hSAA1) or ovalbumin (Ova) was unexposed or exposed to Pam3CSK4 (Pam) overnight (control), and some of the preparation was subjected to concentration of proteins > 3 kDa using concentrated using Amicon Ultra centrifugal concentrators (filtered). Control and filtered preparations were used to stimulate J774 cells for 24 hours after which TNFα concentrations in culture media were measured by ELISA (D). Data are mean ± SEM and are representative of three (A-C) or two (D) independent experiments with n = 4 per group. Statistics were analyzed using one-way ANOVA with Dunnett’s test for multiple comparisons (A-C) or two-way ANOVA with Tukey’s test for multiple comparisons (D). **** p
    Figure Legend Snippet: Lipopeptides associated with SAA confer its ability to stimulate TNFα production. 100 ng/ml LPS ( A ), 100 ng/ml Pam3CSK4 (Pam, B ), and 1¼g/ml apoSAA ( C ) were incubated with lipoprotein lipase (LPL), and then used to stimulate J774 cells. Culture supernatants were collected 24 hours later and TNFα concentrations were measured by ELISA. Human SAA1 from Origene produced in HEK cells (hSAA1) or ovalbumin (Ova) was unexposed or exposed to Pam3CSK4 (Pam) overnight (control), and some of the preparation was subjected to concentration of proteins > 3 kDa using concentrated using Amicon Ultra centrifugal concentrators (filtered). Control and filtered preparations were used to stimulate J774 cells for 24 hours after which TNFα concentrations in culture media were measured by ELISA (D). Data are mean ± SEM and are representative of three (A-C) or two (D) independent experiments with n = 4 per group. Statistics were analyzed using one-way ANOVA with Dunnett’s test for multiple comparisons (A-C) or two-way ANOVA with Tukey’s test for multiple comparisons (D). **** p

    Techniques Used: Incubation, Enzyme-linked Immunosorbent Assay, Produced, Concentration Assay

    Related Articles

    Centrifugation:

    Article Title: Source and Purity of Dengue-Viral Preparations Impact Requirement for Enhancing Antibody to Induce Elevated IL-1β Secretion: A Primary Human Monocyte Model
    Article Snippet: .. Briefly, crude supernatants from DENV-infected Vero cells were concentrated by centrifugation at 1500 x g for 20–25 minutes in 15 ml Millipore Amicon Centrifugal Filter Units with a 100-kDa cutoff, allowing components < 100 kDa to pass through but not virus. ..

    Filtration:

    Article Title: Maltose-Binding Protein Enhances Secretion of Recombinant Human Granzyme B Accompanied by In Vivo Processing of a Precursor MBP Fusion Protein
    Article Snippet: .. Likewise GrB activity was determined in MBP-fur-GrB samples containing equivalent protein amounts but enriched for either unprocessed (retentate) or processed MBP-fur-GrB protein (filtrate) by filtration of culture supernatants through Amicon Ultra centrifugal filters with 100 kDa membranes (Millipore, Schwalbach, Germany). .. A highly purified recombinant GrB derivative was included as a positive control.

    Purification:

    Article Title: Use of Synthetic Single-Stranded Oligonucleotides as Artificial Test Soiling for Validation of Surgical Instrument Cleaning Processes
    Article Snippet: .. Therefore, ssDNA_ODN in the eluates was concentrated and purified using Amicon Ultra 0.5 mL 30K centrifugal filters (Millipore GmbH, Schwalbach/Ts., Germany) according to the manufacturer's instructions to prevent an effect on qPCR. .. The used ssDNA_ODN had a length of 90 nucleotides and an approximate molecular weight of 29.7 kDa.

    Real-time Polymerase Chain Reaction:

    Article Title: Use of Synthetic Single-Stranded Oligonucleotides as Artificial Test Soiling for Validation of Surgical Instrument Cleaning Processes
    Article Snippet: .. Therefore, ssDNA_ODN in the eluates was concentrated and purified using Amicon Ultra 0.5 mL 30K centrifugal filters (Millipore GmbH, Schwalbach/Ts., Germany) according to the manufacturer's instructions to prevent an effect on qPCR. .. The used ssDNA_ODN had a length of 90 nucleotides and an approximate molecular weight of 29.7 kDa.

    Concentration Assay:

    Article Title: Improved sensitivity of the urine CAA lateral-flow assay for diagnosing active Schistosoma infections by using larger sample volumes
    Article Snippet: .. This step involves the concentration of the TCA-soluble fraction of urine samples using Amicon Ultra Centrifugal Filter Devices (Millipore Corp.), allowing larger sample input, increasing the volume from 10 μL urine to 250 and 2000 μL, or even 7500 μL. .. The results confirm that the larger sample input identified samples with CAA concentrations well below the 30 pg/mL cutoff threshold as maintained for the standard dry-reagent UCP-LF CAA assay without concentration and requiring only 10 μL urine (UCAA10) [ ].

    Activity Assay:

    Article Title: Maltose-Binding Protein Enhances Secretion of Recombinant Human Granzyme B Accompanied by In Vivo Processing of a Precursor MBP Fusion Protein
    Article Snippet: .. Likewise GrB activity was determined in MBP-fur-GrB samples containing equivalent protein amounts but enriched for either unprocessed (retentate) or processed MBP-fur-GrB protein (filtrate) by filtration of culture supernatants through Amicon Ultra centrifugal filters with 100 kDa membranes (Millipore, Schwalbach, Germany). .. A highly purified recombinant GrB derivative was included as a positive control.

    Expressing:

    Article Title: RANTES/CCL5 Induces Collagen Degradation by Activating MMP-1 and MMP-13 Expression in Human Rheumatoid Arthritis Synovial Fibroblasts
    Article Snippet: .. For some experiments, RASFs were pretreated with the inhibitor of p38 (SB203980; 10 µM), ERK (PD98059; 10 µM), JNK (SP600125; 10 µM), NF-KB (PDTC; 200 µM), or PKCδ (Rottlerin; 10 µM) for 2 h followed by RANTES/CCL5 treatment for 24 h. Culture supernatants were concentrated using Amicon® Ultra centrifugal filters (Millipore) and MMP-1 and MMP-13 expression was determined using Western immunoblotting. ..

    Article Title: Maltose-Binding Protein Enhances Secretion of Recombinant Human Granzyme B Accompanied by In Vivo Processing of a Precursor MBP Fusion Protein
    Article Snippet: .. Yeast culture supernatants were collected after induction of protein expression for 3 days, 10×concentrated using Amicon Ultra centrifugal filters with 10 kDa membranes (Millipore), and dialyzed against PBS. ..

    Article Title: RANTES/CCL5 Induces Collagen Degradation by Activating MMP-1 and MMP-13 Expression in Human Rheumatoid Arthritis Synovial Fibroblasts
    Article Snippet: .. Culture supernatant were concentrated using Amicon® Ultra Centrifugal filters (Millipore) and MMP-1 and MMP-13 expression was determined using Western immunoblotting. .. Transient Transfection of siRNA To study the effect of RANTES/CCL5 knockdown on MMP-1 and MMP-13 production, RASFs were transfected with ON-TARGET plus SMART pool RANTES/CCL5 siRNA (GE Dharmacon, Lafayette, CO, USA) using Lipofectamine® RNAiMAX (Life Technologies) for 48 h and then stimulated with IL-1β (5 ng/ml) for 24 h. Conditioned media was used to study the effect of MMP-1 and MMP-13 production using ELISA.

    Western Blot:

    Article Title: RANTES/CCL5 Induces Collagen Degradation by Activating MMP-1 and MMP-13 Expression in Human Rheumatoid Arthritis Synovial Fibroblasts
    Article Snippet: .. For some experiments, RASFs were pretreated with the inhibitor of p38 (SB203980; 10 µM), ERK (PD98059; 10 µM), JNK (SP600125; 10 µM), NF-KB (PDTC; 200 µM), or PKCδ (Rottlerin; 10 µM) for 2 h followed by RANTES/CCL5 treatment for 24 h. Culture supernatants were concentrated using Amicon® Ultra centrifugal filters (Millipore) and MMP-1 and MMP-13 expression was determined using Western immunoblotting. ..

    Article Title: RANTES/CCL5 Induces Collagen Degradation by Activating MMP-1 and MMP-13 Expression in Human Rheumatoid Arthritis Synovial Fibroblasts
    Article Snippet: .. Culture supernatant were concentrated using Amicon® Ultra Centrifugal filters (Millipore) and MMP-1 and MMP-13 expression was determined using Western immunoblotting. .. Transient Transfection of siRNA To study the effect of RANTES/CCL5 knockdown on MMP-1 and MMP-13 production, RASFs were transfected with ON-TARGET plus SMART pool RANTES/CCL5 siRNA (GE Dharmacon, Lafayette, CO, USA) using Lipofectamine® RNAiMAX (Life Technologies) for 48 h and then stimulated with IL-1β (5 ng/ml) for 24 h. Conditioned media was used to study the effect of MMP-1 and MMP-13 production using ELISA.

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  • 99
    Millipore ultrafiltered
    Results of ion selective electrode measurements from (a) lumber blocks and (b) sawdust treatments using MCA high treated lumber. In addition, results of periodic sampling for ICP-AES analysis on unfiltered (blocks), 0.45 μm filtered (sawdust), and 3 kDa <t>ultrafiltered</t> samples are presented. Electrode data are culled to report an hourly measurement.
    Ultrafiltered, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ultrafiltered/product/Millipore
    Average 99 stars, based on 22 article reviews
    Price from $9.99 to $1999.99
    ultrafiltered - by Bioz Stars, 2020-08
    99/100 stars
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    99
    Millipore 100 kda cutoff centrifugal filters
    Fractionation of FCM+TNF-α and identification of lumican. ( A ) FCM+TNF-α was collected and analyzed for cytokines. ( B ) FCM+TNF-α was fractionated by centrifugation using <t>100-,</t> 10-, and <t>3-kDa</t> cutoff filters. PBMC were cultured for
    100 Kda Cutoff Centrifugal Filters, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/100 kda cutoff centrifugal filters/product/Millipore
    Average 99 stars, based on 52 article reviews
    Price from $9.99 to $1999.99
    100 kda cutoff centrifugal filters - by Bioz Stars, 2020-08
    99/100 stars
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    84
    Millipore free ssdna
    Protein corona dynamics and structure assessed for binding of key proteins to <t>ssDNA-SWCNTs.</t> A corona exchange assay is employed to determine binding kinetics of a protein panel (each at 80 mg/L final concentration) to (a) (GT) 15 -SWCNTs and (b) (GT) 6 -SWCNTs (5 mg/L final concentration). Small-angle x-ray scattering (SAXS) is applied to gain in-solution structural information of albumin vs. fibrinogen adsorption on (GT) 15 -SWCNTs. (c) Experimental small-angle x-ray scattering (SAXS) profiles for 0.5 g/L (GT) 15 -SWCNTs with and without albumin or fibrinogen, each at 0.5 g/L final concentrations. Mass fractal model fits are included in red together with fit residuals below. (d) SAXS profiles fit to show power law dependencies in the Porod regions, with illustration depicting the mass fractal dimension Dm increasing from approximately 1 to 2.
    Free Ssdna, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/free ssdna/product/Millipore
    Average 84 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    free ssdna - by Bioz Stars, 2020-08
    84/100 stars
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    Image Search Results


    Results of ion selective electrode measurements from (a) lumber blocks and (b) sawdust treatments using MCA high treated lumber. In addition, results of periodic sampling for ICP-AES analysis on unfiltered (blocks), 0.45 μm filtered (sawdust), and 3 kDa ultrafiltered samples are presented. Electrode data are culled to report an hourly measurement.

    Journal: Environmental toxicology and chemistry

    Article Title: Assessing the Release of Copper from Nanocopper-treated and Conventional Copper-treated Lumber into Marine Waters: (2) Forms and Bioavailability

    doi: 10.1002/etc.4140

    Figure Lengend Snippet: Results of ion selective electrode measurements from (a) lumber blocks and (b) sawdust treatments using MCA high treated lumber. In addition, results of periodic sampling for ICP-AES analysis on unfiltered (blocks), 0.45 μm filtered (sawdust), and 3 kDa ultrafiltered samples are presented. Electrode data are culled to report an hourly measurement.

    Article Snippet: In addition, at time points 1, 7, and 28 da, an additional ultrafiltered (3 kDa Amicon Ultra-15 centrifugal filter device, EMD Millipore) water sample was taken to quantify the presence of dissolved copper.

    Techniques: Sampling

    Fractionation of FCM+TNF-α and identification of lumican. ( A ) FCM+TNF-α was collected and analyzed for cytokines. ( B ) FCM+TNF-α was fractionated by centrifugation using 100-, 10-, and 3-kDa cutoff filters. PBMC were cultured for

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: TNF-α–stimulated fibroblasts secrete lumican to promote fibrocyte differentiation

    doi: 10.1073/pnas.1507387112

    Figure Lengend Snippet: Fractionation of FCM+TNF-α and identification of lumican. ( A ) FCM+TNF-α was collected and analyzed for cytokines. ( B ) FCM+TNF-α was fractionated by centrifugation using 100-, 10-, and 3-kDa cutoff filters. PBMC were cultured for

    Article Snippet: FCM+TNF-α was fractionated using 3-, 10-, and 100-kDa cutoff centrifugal filters (Amicon Ultra, Millipore) as described ( , ).

    Techniques: Fractionation, Centrifugation, Cell Culture

    Processing of MBP-GrB fusion proteins. (A) Variants of the furin recognition motif either containing (furS) or lacking (fur) an additional C-terminal serine residue. (B) Culture supernatants of yeast clones carrying pPIC9-MBP-fur-GrB were collected after induction with methanol for 3 days, and expression and processing of the GrB fusion protein was analyzed by immunoblotting with GrB-specific antibody. (C) Samples enriched for processed (100 kDa filtrate) or unprocessed MBP-fur-GrB protein (100 kDa retentate) were prepared by filtration of culture supernatant of a representative MBP-fur-GrB clone through Amicon filters with 100 kDa membranes, and analyzed by immunoblotting with GrB-specific antibody. Initial MBP-fur-GrB containing supernatant and supernatant from an MBP-furS-GrB clone were included for comparison. Supernatant of yeast cells carrying empty pPIC9 served as a control. The lower apparent molecular weight of processed GrB in (C) when compared to (B) is most likely due to a lower degree of glycosylation (calculated molecular weight for processed GrB in non-glycosylated form: 28.4 kDa). (D) Enzymatic activity of GrB proteins from culture supernatants and kinetics of substrate cleavage were analyzed in a colorimetric peptide cleavage assay. The MBP-fur-GrB or MBP-furS-GrB containing supernatants, and the MBP-fur-GrB samples enriched for processed (100 kDa filtrate) or unprocessed protein (100 kDa retentate) analyzed in (C) were tested as indicated. A purified recombinant GrB derivative (GrB) was included as a positive control. Supernatant of yeast cells carrying empty pPIC9 displayed no GrB activity (data not shown). Means of triplicate samples are shown. Error bars indicate SEM.

    Journal: PLoS ONE

    Article Title: Maltose-Binding Protein Enhances Secretion of Recombinant Human Granzyme B Accompanied by In Vivo Processing of a Precursor MBP Fusion Protein

    doi: 10.1371/journal.pone.0014404

    Figure Lengend Snippet: Processing of MBP-GrB fusion proteins. (A) Variants of the furin recognition motif either containing (furS) or lacking (fur) an additional C-terminal serine residue. (B) Culture supernatants of yeast clones carrying pPIC9-MBP-fur-GrB were collected after induction with methanol for 3 days, and expression and processing of the GrB fusion protein was analyzed by immunoblotting with GrB-specific antibody. (C) Samples enriched for processed (100 kDa filtrate) or unprocessed MBP-fur-GrB protein (100 kDa retentate) were prepared by filtration of culture supernatant of a representative MBP-fur-GrB clone through Amicon filters with 100 kDa membranes, and analyzed by immunoblotting with GrB-specific antibody. Initial MBP-fur-GrB containing supernatant and supernatant from an MBP-furS-GrB clone were included for comparison. Supernatant of yeast cells carrying empty pPIC9 served as a control. The lower apparent molecular weight of processed GrB in (C) when compared to (B) is most likely due to a lower degree of glycosylation (calculated molecular weight for processed GrB in non-glycosylated form: 28.4 kDa). (D) Enzymatic activity of GrB proteins from culture supernatants and kinetics of substrate cleavage were analyzed in a colorimetric peptide cleavage assay. The MBP-fur-GrB or MBP-furS-GrB containing supernatants, and the MBP-fur-GrB samples enriched for processed (100 kDa filtrate) or unprocessed protein (100 kDa retentate) analyzed in (C) were tested as indicated. A purified recombinant GrB derivative (GrB) was included as a positive control. Supernatant of yeast cells carrying empty pPIC9 displayed no GrB activity (data not shown). Means of triplicate samples are shown. Error bars indicate SEM.

    Article Snippet: Likewise GrB activity was determined in MBP-fur-GrB samples containing equivalent protein amounts but enriched for either unprocessed (retentate) or processed MBP-fur-GrB protein (filtrate) by filtration of culture supernatants through Amicon Ultra centrifugal filters with 100 kDa membranes (Millipore, Schwalbach, Germany).

    Techniques: Clone Assay, Expressing, Filtration, Molecular Weight, Activity Assay, Cleavage Assay, Purification, Recombinant, Positive Control

    Protein corona dynamics and structure assessed for binding of key proteins to ssDNA-SWCNTs. A corona exchange assay is employed to determine binding kinetics of a protein panel (each at 80 mg/L final concentration) to (a) (GT) 15 -SWCNTs and (b) (GT) 6 -SWCNTs (5 mg/L final concentration). Small-angle x-ray scattering (SAXS) is applied to gain in-solution structural information of albumin vs. fibrinogen adsorption on (GT) 15 -SWCNTs. (c) Experimental small-angle x-ray scattering (SAXS) profiles for 0.5 g/L (GT) 15 -SWCNTs with and without albumin or fibrinogen, each at 0.5 g/L final concentrations. Mass fractal model fits are included in red together with fit residuals below. (d) SAXS profiles fit to show power law dependencies in the Porod regions, with illustration depicting the mass fractal dimension Dm increasing from approximately 1 to 2.

    Journal: bioRxiv

    Article Title: Protein Corona Composition and Dynamics on Carbon Nanotubes in Blood Plasma and Cerebrospinal Fluid

    doi: 10.1101/2020.01.13.905356

    Figure Lengend Snippet: Protein corona dynamics and structure assessed for binding of key proteins to ssDNA-SWCNTs. A corona exchange assay is employed to determine binding kinetics of a protein panel (each at 80 mg/L final concentration) to (a) (GT) 15 -SWCNTs and (b) (GT) 6 -SWCNTs (5 mg/L final concentration). Small-angle x-ray scattering (SAXS) is applied to gain in-solution structural information of albumin vs. fibrinogen adsorption on (GT) 15 -SWCNTs. (c) Experimental small-angle x-ray scattering (SAXS) profiles for 0.5 g/L (GT) 15 -SWCNTs with and without albumin or fibrinogen, each at 0.5 g/L final concentrations. Mass fractal model fits are included in red together with fit residuals below. (d) SAXS profiles fit to show power law dependencies in the Porod regions, with illustration depicting the mass fractal dimension Dm increasing from approximately 1 to 2.

    Article Snippet: Supernatant containing the product was collected. ssDNA-SWCNTs were spin-filtered to remove free ssDNA (Amicon Ultra-0.5 mL centrifugal filters with 100 kDa MWCO, Millipore Sigma) by washing with Milli-Q water two times (8 krcf for 5 min) then reversing the spin filter and centrifuging to recover sample (1 krcf for 5 min). ssDNA-SWCNT concentration was determined via sample absorbance at 632 nm (NanoVue Plus, GE Healthcare Life Sciences) and the extinction coefficient ε632nm =0.036 L cm mg−1 . ssDNA-SWCNTs were stored at 4°C until use and then diluted to a working concentration of 100 mg/L in 0.1 M PBS.

    Techniques: Binding Assay, Concentration Assay, Adsorption