monensin sodium salt  (Millipore)

 
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    Name:
    Monensin sodium salt
    Description:
    Chemical structure polyether
    Catalog Number:
    m5273
    Price:
    None
    Applications:
    Monensin sodium salt has been used:. for the intracellular staining of cytokines. to study its effects on the regulation of nuclear factor-κ B (NF-κB ) activation. as a positive control to study its effects on in vitro rumen fermentation
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    Structured Review

    Millipore monensin sodium salt
    Monensin sodium salt
    Chemical structure polyether
    https://www.bioz.com/result/monensin sodium salt/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    monensin sodium salt - by Bioz Stars, 2021-03
    99/100 stars

    Images

    1) Product Images from "Assembly and Budding of Ebolavirus"

    Article Title: Assembly and Budding of Ebolavirus

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.0020099

    VLP Budding Is Dependent on Microtubules 10 μM nocodazole (noc), 1 μM taxol (tax), 10 μg/ml cytochalasin D (cytD), or 5 μM monensin (mon) was added to cells 3 h after they were transfected with plasmids expressing (A) NP, VP24, VP35, and VP40, or (B) VP40 alone. At 16 h post-transfection, proteins in the cell lysates and supernatants were separated by SDS-PAGE and examined by Western blotting with anti-NP and anti-VP40 antibodies. Following nocodazol or taxol treatment, the amounts of both VP40 and NP (A) or VP40 (B) in the supernatants (i.e., efficiency of VLPs budding) were reduced. cont, mock-treated control.
    Figure Legend Snippet: VLP Budding Is Dependent on Microtubules 10 μM nocodazole (noc), 1 μM taxol (tax), 10 μg/ml cytochalasin D (cytD), or 5 μM monensin (mon) was added to cells 3 h after they were transfected with plasmids expressing (A) NP, VP24, VP35, and VP40, or (B) VP40 alone. At 16 h post-transfection, proteins in the cell lysates and supernatants were separated by SDS-PAGE and examined by Western blotting with anti-NP and anti-VP40 antibodies. Following nocodazol or taxol treatment, the amounts of both VP40 and NP (A) or VP40 (B) in the supernatants (i.e., efficiency of VLPs budding) were reduced. cont, mock-treated control.

    Techniques Used: Transfection, Expressing, SDS Page, Western Blot

    2) Product Images from "Na+/K+ pump interacts with the h-current to control bursting activity in central pattern generator neurons of leeches"

    Article Title: Na+/K+ pump interacts with the h-current to control bursting activity in central pattern generator neurons of leeches

    Journal: eLife

    doi: 10.7554/eLife.19322

    Hyperpolarization of the oscillator heart interneurons and suppression of their spiking activity by intracellular leakage of Na + from an electrode and by monensin. ( A 1 ) An extracellular (blue) trace of one oscillator heart interneuron and an intracellular (vermilion) trace of a contralateral oscillator heart interneuron that was impaled with a K + -filled intracellular electrode. ( A 2 ) Impalement of an oscillator heart interneuron with a Na + -filled electrode gradually suppressed its spiking activity and hyperpolarized the neuron. There was no change in the bursting activity of the extracellularly recorded neurons in the ( A 1 ) K + and ( A 2 ) Na + recordings. ( A 3 ) During the first ten minutes, the average base potential of Na + -loaded neurons (closed circles) was significantly more hyperpolarized than the base potential of K + -loaded neurons (open circles). Such differences persisted well into the 15th and 20th minute. The data are represented as mean ± SEM, with the asterisk (*) representing significant differences between the K + and Na + base potentials (split-plot ANOVA, F 1,8 = 1847.7, p=0.006). ( B 1 ) Extracellular (blue) and intracellular (vermilion) traces from a pair of oscillator heart interneurons that were initially bathed in control saline and showed normal alternating bursting. ( B 2 ) When the oscillator heart interneurons were bathed in Ca 2+ -free saline with 2 mM Cs + and 1.8 mM Mn 2+ , they produced a more tonic firing pattern that was interspersed with synchronized oscillations. ( B 3 ) When the oscillator heart interneurons were subsequently treated with 10 µM monensin in the same Ca 2+ -free saline, the spiking activity of both oscillator heart interneurons were suppressed and the membrane potential of the intracellularly recoded neuron gradually hyperpolarized. DOI: http://dx.doi.org/10.7554/eLife.19322.003
    Figure Legend Snippet: Hyperpolarization of the oscillator heart interneurons and suppression of their spiking activity by intracellular leakage of Na + from an electrode and by monensin. ( A 1 ) An extracellular (blue) trace of one oscillator heart interneuron and an intracellular (vermilion) trace of a contralateral oscillator heart interneuron that was impaled with a K + -filled intracellular electrode. ( A 2 ) Impalement of an oscillator heart interneuron with a Na + -filled electrode gradually suppressed its spiking activity and hyperpolarized the neuron. There was no change in the bursting activity of the extracellularly recorded neurons in the ( A 1 ) K + and ( A 2 ) Na + recordings. ( A 3 ) During the first ten minutes, the average base potential of Na + -loaded neurons (closed circles) was significantly more hyperpolarized than the base potential of K + -loaded neurons (open circles). Such differences persisted well into the 15th and 20th minute. The data are represented as mean ± SEM, with the asterisk (*) representing significant differences between the K + and Na + base potentials (split-plot ANOVA, F 1,8 = 1847.7, p=0.006). ( B 1 ) Extracellular (blue) and intracellular (vermilion) traces from a pair of oscillator heart interneurons that were initially bathed in control saline and showed normal alternating bursting. ( B 2 ) When the oscillator heart interneurons were bathed in Ca 2+ -free saline with 2 mM Cs + and 1.8 mM Mn 2+ , they produced a more tonic firing pattern that was interspersed with synchronized oscillations. ( B 3 ) When the oscillator heart interneurons were subsequently treated with 10 µM monensin in the same Ca 2+ -free saline, the spiking activity of both oscillator heart interneurons were suppressed and the membrane potential of the intracellularly recoded neuron gradually hyperpolarized. DOI: http://dx.doi.org/10.7554/eLife.19322.003

    Techniques Used: Activity Assay, Produced

    Monensin stimulates the outward Na + /K + pump current. ( A 1 ) Membrane current trace from an oscillator heart interneuron with its membrane potential ( V m ) voltage-clamped at −45 mV (see inset) in Ca 2+ -free saline with 1.8 mM Mn 2+ plus 2 mM Cs. Changes in the neuron’s membrane current ( I m ) were observed under three experimental treatments: pre-monensin saline for five minutes, 10 µM monensin for 10 min, and 10 µM monensin plus 100 µM strophanthidin (SPTD) for another five minutes. ( A 2 ) A scatterplot of membrane currents from five preparations, with each green dashed line representing a mean for each of the three experimental treatments. Monensin induced a significant outward current relative to pre-monensin saline. Monensin plus strophanthidin induced a significant inward current relative to pre-monensin or monensin saline. The asterisks (*) represent significance from the pre-monensin saline whereas the hashtag (#) represents significance from the monensin saline (Tukey’s test, p
    Figure Legend Snippet: Monensin stimulates the outward Na + /K + pump current. ( A 1 ) Membrane current trace from an oscillator heart interneuron with its membrane potential ( V m ) voltage-clamped at −45 mV (see inset) in Ca 2+ -free saline with 1.8 mM Mn 2+ plus 2 mM Cs. Changes in the neuron’s membrane current ( I m ) were observed under three experimental treatments: pre-monensin saline for five minutes, 10 µM monensin for 10 min, and 10 µM monensin plus 100 µM strophanthidin (SPTD) for another five minutes. ( A 2 ) A scatterplot of membrane currents from five preparations, with each green dashed line representing a mean for each of the three experimental treatments. Monensin induced a significant outward current relative to pre-monensin saline. Monensin plus strophanthidin induced a significant inward current relative to pre-monensin or monensin saline. The asterisks (*) represent significance from the pre-monensin saline whereas the hashtag (#) represents significance from the monensin saline (Tukey’s test, p

    Techniques Used:

    A biophysical model of oscillator heart interneurons that mimics three experimental treatments with monensin. ( A 1 ) Sample traces of simulated activity by oscillator heart interneurons functioning as a half center oscillator in normal saline, which were observed when parameters g ¯ h = 4.9 nS and M = 0 s −1 . ( A 2 ) Simulated activity of oscillator heart interneurons with a Na + /K + pump stimulated by monensin (monensin saline), observed when g ¯ h = 4.9 nS and M = 2.2 × 10 −3 s −1 . ( A 3 ) Simulated activity of a half-center oscillator with blocked h -current and pump stimulated by monensin (monensin plus Cs + saline), observed when g ¯ h = 0.1 nS and M = 1.9 × 10 −4 s −1 . Sample traces representing membrane potentials ( V m ) of both left (L, blue) and right (R, vermilion) oscillator heart interneurons as well as h -current ( I h , yellow), pump current ( I pump , reddish purple), and intracellular Na + concentration [Na] i (black) belonging to the right oscillator heart interneuron. ( B 1 ) A scatterplot depicting incremental shortening of the period as the monensin rate constant increases towards 2.2 × 10 −3 s −1 in a model of a half-center oscillator with the h -current present. Spiking activity was suppressed at rate constant values larger than 2.2 × 10 −3 s −1 . ( B 2 ) In a simulation of a half-center oscillator, the average pump current over the entire burst cycle was fixed at 155.5 pA, which resulted in a longer period, burst duration, and interburst interval. Intracellular Na + concentration [Na] i appeared to increase and decrease more slowly relative to a ( A 1 ) normal half-center oscillator with a dynamic pump current. ( B 3 ) Fixing the average pump current over the entire burst cycle to 144.4 pA (a value lower than 155.5 pA) produced irregular bouts of bursting. DOI: http://dx.doi.org/10.7554/eLife.19322.011
    Figure Legend Snippet: A biophysical model of oscillator heart interneurons that mimics three experimental treatments with monensin. ( A 1 ) Sample traces of simulated activity by oscillator heart interneurons functioning as a half center oscillator in normal saline, which were observed when parameters g ¯ h = 4.9 nS and M = 0 s −1 . ( A 2 ) Simulated activity of oscillator heart interneurons with a Na + /K + pump stimulated by monensin (monensin saline), observed when g ¯ h = 4.9 nS and M = 2.2 × 10 −3 s −1 . ( A 3 ) Simulated activity of a half-center oscillator with blocked h -current and pump stimulated by monensin (monensin plus Cs + saline), observed when g ¯ h = 0.1 nS and M = 1.9 × 10 −4 s −1 . Sample traces representing membrane potentials ( V m ) of both left (L, blue) and right (R, vermilion) oscillator heart interneurons as well as h -current ( I h , yellow), pump current ( I pump , reddish purple), and intracellular Na + concentration [Na] i (black) belonging to the right oscillator heart interneuron. ( B 1 ) A scatterplot depicting incremental shortening of the period as the monensin rate constant increases towards 2.2 × 10 −3 s −1 in a model of a half-center oscillator with the h -current present. Spiking activity was suppressed at rate constant values larger than 2.2 × 10 −3 s −1 . ( B 2 ) In a simulation of a half-center oscillator, the average pump current over the entire burst cycle was fixed at 155.5 pA, which resulted in a longer period, burst duration, and interburst interval. Intracellular Na + concentration [Na] i appeared to increase and decrease more slowly relative to a ( A 1 ) normal half-center oscillator with a dynamic pump current. ( B 3 ) Fixing the average pump current over the entire burst cycle to 144.4 pA (a value lower than 155.5 pA) produced irregular bouts of bursting. DOI: http://dx.doi.org/10.7554/eLife.19322.011

    Techniques Used: Activity Assay, Concentration Assay, Produced

    The cycle-to-cycle effects of monensin on the period of oscillator heart interneurons. ( A ) Initial application of monensin rapidly shortens the period towards a stable minimum value. The concentration of 10 µM monensin (vermilion line) shortens the period more rapidly than the lower concentration of 1 µM (blue line). The amount of time a period needs to reach its minimum value at the 200th cycle can be measured by summing up all the periods leading up to that 200th cycle. ( B ) A scatterplot of the amount of time that has passed before the period has reached its value at the 200th cycle in both 1 µM and 10 µM monensin treatments. ( C ) A scatterplot of the period at the 200th cycle in both 1 µM and 10 µM monensin treatments. The dashed green lines in the scatter plots represent means whereas the asterisk (*) represents significance from control (unpaired t-test, p=0.003). DOI: http://dx.doi.org/10.7554/eLife.19322.006
    Figure Legend Snippet: The cycle-to-cycle effects of monensin on the period of oscillator heart interneurons. ( A ) Initial application of monensin rapidly shortens the period towards a stable minimum value. The concentration of 10 µM monensin (vermilion line) shortens the period more rapidly than the lower concentration of 1 µM (blue line). The amount of time a period needs to reach its minimum value at the 200th cycle can be measured by summing up all the periods leading up to that 200th cycle. ( B ) A scatterplot of the amount of time that has passed before the period has reached its value at the 200th cycle in both 1 µM and 10 µM monensin treatments. ( C ) A scatterplot of the period at the 200th cycle in both 1 µM and 10 µM monensin treatments. The dashed green lines in the scatter plots represent means whereas the asterisk (*) represents significance from control (unpaired t-test, p=0.003). DOI: http://dx.doi.org/10.7554/eLife.19322.006

    Techniques Used: Concentration Assay

    Stimulating the pump with 10 µM monensin in pharmacologically isolated heart interneurons requires h -current to shorten the interburst interval but not to shorten the burst duration. Extracellular traces from left (blue) and right (vermilion) oscillator heart interneurons [HN(L) and HN(R) neurons] that were pharmacological isolated as bursters by being treated with ( A 1 ) saline that contained 500 µM bicuculline (Bic). ( A 2 ) The isolated oscillator heart interneurons were then treated with saline that contained 500 µM bicuculline plus 10 µM monensin. Corresponding scatter plots of ( A 3 ) burst duration and ( A 4 ) interburst interval. Extracellular traces from another pair of isolated oscillator heart interneurons that were treated with ( B 1 ) saline that contained 500 µM bicuculline plus 2 mM Cs + saline followed by followed by another treatment with ( B 2 ) saline that contained 500 µM bicuculline, 2 mM Cs + , plus 10 µM monensin saline. Corresponding scatter plots of ( B 3 ) burst duration and ( B 4 ) interburst interval. The dashed green lines represent means whereas asterisks (*) and hashtags (#) represent significance from control and bicuculline, respectively (Tukey’s test, p
    Figure Legend Snippet: Stimulating the pump with 10 µM monensin in pharmacologically isolated heart interneurons requires h -current to shorten the interburst interval but not to shorten the burst duration. Extracellular traces from left (blue) and right (vermilion) oscillator heart interneurons [HN(L) and HN(R) neurons] that were pharmacological isolated as bursters by being treated with ( A 1 ) saline that contained 500 µM bicuculline (Bic). ( A 2 ) The isolated oscillator heart interneurons were then treated with saline that contained 500 µM bicuculline plus 10 µM monensin. Corresponding scatter plots of ( A 3 ) burst duration and ( A 4 ) interburst interval. Extracellular traces from another pair of isolated oscillator heart interneurons that were treated with ( B 1 ) saline that contained 500 µM bicuculline plus 2 mM Cs + saline followed by followed by another treatment with ( B 2 ) saline that contained 500 µM bicuculline, 2 mM Cs + , plus 10 µM monensin saline. Corresponding scatter plots of ( B 3 ) burst duration and ( B 4 ) interburst interval. The dashed green lines represent means whereas asterisks (*) and hashtags (#) represent significance from control and bicuculline, respectively (Tukey’s test, p

    Techniques Used: Isolation

    3) Product Images from "Multiple phosphatidylinositol(3)phosphate roles in retinal pigment epithelium membrane recycling"

    Article Title: Multiple phosphatidylinositol(3)phosphate roles in retinal pigment epithelium membrane recycling

    Journal: bioRxiv

    doi: 10.1101/2020.01.09.899815

    Effects of WIPI2 knockdown on LC3 puncta and on lysosome colocalization. hRPE1 ( A ) ARPE-19 ( B ) or HEK ( C ) cells were transfected with WIPI2 shRNA (marked by DsRed expression) and immunostained for WIPI2 and LC3. ( B ) Results showing LC3 puncta in WIPI2 knockdown ARPE-19 cells were reproduced with a second shRNA targeting a different sequence in WIPI2 than the one used in Fig. 10 . (D-G) ARPE-19 cells were transfected with WIPI2 shRNA (marked by DsRed expression), and treated with starvation ( D ), bafilomycin A ( E ), or monensin ( F ), then immunostained for LC3 and LAMP2. LC3 puncta and LAMP1-positive lysosomes accumulate in each case, but lysosome co-localization with LC3 is much more pronounced in response to starvation or bafilomycin treatment than in response to monensin treatment. ( G ) ARPE-19 cells were transfected with WIPI2 shRNA, and treated overnight with CQ or CQ and wortmannin together.
    Figure Legend Snippet: Effects of WIPI2 knockdown on LC3 puncta and on lysosome colocalization. hRPE1 ( A ) ARPE-19 ( B ) or HEK ( C ) cells were transfected with WIPI2 shRNA (marked by DsRed expression) and immunostained for WIPI2 and LC3. ( B ) Results showing LC3 puncta in WIPI2 knockdown ARPE-19 cells were reproduced with a second shRNA targeting a different sequence in WIPI2 than the one used in Fig. 10 . (D-G) ARPE-19 cells were transfected with WIPI2 shRNA (marked by DsRed expression), and treated with starvation ( D ), bafilomycin A ( E ), or monensin ( F ), then immunostained for LC3 and LAMP2. LC3 puncta and LAMP1-positive lysosomes accumulate in each case, but lysosome co-localization with LC3 is much more pronounced in response to starvation or bafilomycin treatment than in response to monensin treatment. ( G ) ARPE-19 cells were transfected with WIPI2 shRNA, and treated overnight with CQ or CQ and wortmannin together.

    Techniques Used: Transfection, shRNA, Expressing, Sequencing

    4) Product Images from "Distinct functions of ATG16L1 isoforms in membrane binding and LC3B lipidation in autophagy-related processes"

    Article Title: Distinct functions of ATG16L1 isoforms in membrane binding and LC3B lipidation in autophagy-related processes

    Journal: Nature cell biology

    doi: 10.1038/s41556-019-0274-9

    Membrane binding of ATG16L1 in autophagy and during lipidation on perturbed endosomes reveals isoform specific functions a , LC3B/GABARAP lipidation in WT and ATG16L1 KO HEK293 cells rescued or not with ATG16L1β, ATG16L1β F32A/I35A/I36A (β FII) or ATG16L1 (aa 1–249), treated for 2 h as indicated. Cell lysates were immunoblotted against the indicated proteins. b, Levels of LC3B-II/GAPDH quantified from immunoblots in (a) and normalized to fed WT cells. c , Degradation of long-lived proteins in HEK293 WT and in ATG16L1 KO cells rescued or not with ATG16L1β, ATG16L1β F32A/I35A/I36A (β FII) or ATG16L1 (aa 1–249) was quantified based on the Baf.A1 sensitive release of 14 C-valine after 4 h in indicated conditions. d, Confocal images of Zymosan-Alexa594-containing phagosomes counter-stained for LC3B in ATG16L1 KO RAW264.7 cells rescued or not with ATG16L1β, ATG16L1β F32A/I35A/I36A (β FII) or ATG16L1α V308A/R309A/V310A (α VRV). Scale bars: 10μm. The images are representative of n=2 independent experiments. e , LC3B lipidation in ATG16L1 KO HEK293 cells rescued or not with ATG16L1β, ATG16L1α V308A/R309A/V310A (α VRV) or ATG16L1 (aa 1–249). Cells were treated or not with monensin for 1 h or EBSS for 2 h in the presence or absence of Baf.A1. Co-treatment with VPS34 inhibitor VPS34IN1 and ULK1/2 inhibitor MRT68921 was performed where indicated. Cell lysates were immunoblotted against the indicated proteins. f , The levels of LC3B-II/GAPDH were quantified from immunoblots in (e) and normalized to cells rescued with ATG16L1β in the starved condition. g , LC3B lipidation in ATG16L1 KO HEK293 cells rescued or not with ATG16L1β, ATG16L1α, ATG16L1β V308A/R309A/V310A (β VRV), ATG16L1α V308A/R309A/V310A (α VRV) or ATG16L1 (aa 1–249), treated as indicated for 2h. Cell lysates were immunoblotted against the indicated proteins. h .
    Figure Legend Snippet: Membrane binding of ATG16L1 in autophagy and during lipidation on perturbed endosomes reveals isoform specific functions a , LC3B/GABARAP lipidation in WT and ATG16L1 KO HEK293 cells rescued or not with ATG16L1β, ATG16L1β F32A/I35A/I36A (β FII) or ATG16L1 (aa 1–249), treated for 2 h as indicated. Cell lysates were immunoblotted against the indicated proteins. b, Levels of LC3B-II/GAPDH quantified from immunoblots in (a) and normalized to fed WT cells. c , Degradation of long-lived proteins in HEK293 WT and in ATG16L1 KO cells rescued or not with ATG16L1β, ATG16L1β F32A/I35A/I36A (β FII) or ATG16L1 (aa 1–249) was quantified based on the Baf.A1 sensitive release of 14 C-valine after 4 h in indicated conditions. d, Confocal images of Zymosan-Alexa594-containing phagosomes counter-stained for LC3B in ATG16L1 KO RAW264.7 cells rescued or not with ATG16L1β, ATG16L1β F32A/I35A/I36A (β FII) or ATG16L1α V308A/R309A/V310A (α VRV). Scale bars: 10μm. The images are representative of n=2 independent experiments. e , LC3B lipidation in ATG16L1 KO HEK293 cells rescued or not with ATG16L1β, ATG16L1α V308A/R309A/V310A (α VRV) or ATG16L1 (aa 1–249). Cells were treated or not with monensin for 1 h or EBSS for 2 h in the presence or absence of Baf.A1. Co-treatment with VPS34 inhibitor VPS34IN1 and ULK1/2 inhibitor MRT68921 was performed where indicated. Cell lysates were immunoblotted against the indicated proteins. f , The levels of LC3B-II/GAPDH were quantified from immunoblots in (e) and normalized to cells rescued with ATG16L1β in the starved condition. g , LC3B lipidation in ATG16L1 KO HEK293 cells rescued or not with ATG16L1β, ATG16L1α, ATG16L1β V308A/R309A/V310A (β VRV), ATG16L1α V308A/R309A/V310A (α VRV) or ATG16L1 (aa 1–249), treated as indicated for 2h. Cell lysates were immunoblotted against the indicated proteins. h .

    Techniques Used: Binding Assay, Western Blot, Staining

    5) Product Images from "pH regulation in early endosomes and interferon-inducible transmembrane proteins control avian retrovirus fusion"

    Article Title: pH regulation in early endosomes and interferon-inducible transmembrane proteins control avian retrovirus fusion

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M117.783878

    Kinetics of ASLV fusion and measurement of endosomal pH. A, illustration of the virus labeling strategy with Gag-mCherry ( red ) and EcpH-ICAM ( green ) to assess the pH drop in virus-carrying endosomes ( top ) and images of CV-1 cells before (0 h) and after (1 h) internalization of labeled viruses ( bottom ). Virus entry into acidic endosomes is manifested in disappearance of the EcpH signal and accumulation of Gag-mCherry in the perinuclear areas. B , kinetics of ASLV fusion with A549/TVA950 cells in DMEM measured by the BlaM assay and EcpH quenching measured in parallel imaging experiments. C, images of Gag-mCherry/EcpH-ICAM co-labeled ASLV particles internalized by A549/TVA950 cells at different pH. Viruses were pre-bound to cells in the cold and allowed to enter by incubation at 37 °C for 15 min. Cells were then placed in buffers of the indicated acidity supplemented with monensin and nigericin to equilibrate the external and endosomal pH (see “Experimental procedures” for details). The EcpH signal is virtually lost in the background cell fluorescence at pH ≤ 6.2. A triangle shows the expected fluorescence ratio in DMEM equilibrated with air (pH ∼ 7.9). D, calibration of the mean ratio of EcpH and mCherry signals from intracellular compartments as a function of endosomal pH (as illustrated in panel C ). Data are mean ratios ± S.E. from at least 4 image fields acquired for each pH value. The light pink and blue colored regions represent the pH range conducive for ASLV fusion and the background EcpH/mCherry ratio, respectively. E and F, kinetics of ASLV fusion with A549/TVA950 cells in LIB ( E ) or DMEM buffered with HEPES at pH 7.4 ( F ), as measured by the BlaM assay. EcpH quenching in panel E was measured in parallel imaging experiments. Data are mean ± S.E. from 3 ( panels B and E ) and 2 ( panel F ) independent triplicate experiments.
    Figure Legend Snippet: Kinetics of ASLV fusion and measurement of endosomal pH. A, illustration of the virus labeling strategy with Gag-mCherry ( red ) and EcpH-ICAM ( green ) to assess the pH drop in virus-carrying endosomes ( top ) and images of CV-1 cells before (0 h) and after (1 h) internalization of labeled viruses ( bottom ). Virus entry into acidic endosomes is manifested in disappearance of the EcpH signal and accumulation of Gag-mCherry in the perinuclear areas. B , kinetics of ASLV fusion with A549/TVA950 cells in DMEM measured by the BlaM assay and EcpH quenching measured in parallel imaging experiments. C, images of Gag-mCherry/EcpH-ICAM co-labeled ASLV particles internalized by A549/TVA950 cells at different pH. Viruses were pre-bound to cells in the cold and allowed to enter by incubation at 37 °C for 15 min. Cells were then placed in buffers of the indicated acidity supplemented with monensin and nigericin to equilibrate the external and endosomal pH (see “Experimental procedures” for details). The EcpH signal is virtually lost in the background cell fluorescence at pH ≤ 6.2. A triangle shows the expected fluorescence ratio in DMEM equilibrated with air (pH ∼ 7.9). D, calibration of the mean ratio of EcpH and mCherry signals from intracellular compartments as a function of endosomal pH (as illustrated in panel C ). Data are mean ratios ± S.E. from at least 4 image fields acquired for each pH value. The light pink and blue colored regions represent the pH range conducive for ASLV fusion and the background EcpH/mCherry ratio, respectively. E and F, kinetics of ASLV fusion with A549/TVA950 cells in LIB ( E ) or DMEM buffered with HEPES at pH 7.4 ( F ), as measured by the BlaM assay. EcpH quenching in panel E was measured in parallel imaging experiments. Data are mean ± S.E. from 3 ( panels B and E ) and 2 ( panel F ) independent triplicate experiments.

    Techniques Used: Labeling, Imaging, Incubation, Fluorescence

    6) Product Images from "In Vitro Assessment of Uptake and Lysosomal Sequestration of Respiratory Drugs in Alveolar Macrophage Cell Line NR8383"

    Article Title: In Vitro Assessment of Uptake and Lysosomal Sequestration of Respiratory Drugs in Alveolar Macrophage Cell Line NR8383

    Journal: Pharmaceutical Research

    doi: 10.1007/s11095-015-1753-8

    Qualitative assessment of lysosomal sequestration of LysoTracker Red (LTR) and three drugs studied in NR8383 by confocal microscopy: ( a ) differential interference contrast image of a single NR8383 cell treated with 200 nM LTR; ( b ) the same cell being excited to detect LTR localised in lysosomes under control conditions; the localisation of LTR in the lysosomes of NR8383 was reduced in presence of 20 mM NH4Cl ( c ), 5 μM monensin ( d ), 10 μM nigericin ( e ), 5 μM clarithromycin ( f ) and 5 μM imipramine ( g ), and showed minor changes in presence of 5 μM formoterol ( h ).
    Figure Legend Snippet: Qualitative assessment of lysosomal sequestration of LysoTracker Red (LTR) and three drugs studied in NR8383 by confocal microscopy: ( a ) differential interference contrast image of a single NR8383 cell treated with 200 nM LTR; ( b ) the same cell being excited to detect LTR localised in lysosomes under control conditions; the localisation of LTR in the lysosomes of NR8383 was reduced in presence of 20 mM NH4Cl ( c ), 5 μM monensin ( d ), 10 μM nigericin ( e ), 5 μM clarithromycin ( f ) and 5 μM imipramine ( g ), and showed minor changes in presence of 5 μM formoterol ( h ).

    Techniques Used: Confocal Microscopy

    K p (C cell /C medium ) estimated in NR8383 in the absence ( ) (control) and presence of ( a ) 10 μM nigericin ( ) ( b ) 5 μM monensin ( ) at 5 μM concentration of imipramine, clarithromycin, formoterol and fenoterol. Data represent mean ± SD of at least 3 experiments (**, p
    Figure Legend Snippet: K p (C cell /C medium ) estimated in NR8383 in the absence ( ) (control) and presence of ( a ) 10 μM nigericin ( ) ( b ) 5 μM monensin ( ) at 5 μM concentration of imipramine, clarithromycin, formoterol and fenoterol. Data represent mean ± SD of at least 3 experiments (**, p

    Techniques Used: Concentration Assay

    Related Articles

    other:

    Article Title: Wnt Modulating Agents Inhibit Human Cytomegalovirus Replication
    Article Snippet: Monensin, nigericin, salinomycin, and ganciclovir (GCV) were purchased from Sigma Chemicals (St. Louis, MO).

    Staining:

    Article Title: House dust mite induced allergic airway disease is attenuated in CD11ccreIL-4Rα−/l°x mice
    Article Snippet: .. For intracellular cytokine staining, lung cells were seeded at 2 × 106 cells/well and stimulated at 37 o C for 4 hours with phorbal myristate acetate (Sigma-Aldrich) (50ng/ml), ionomycin (Sigma-Aldrich) (250ng/ml) and monensin (Sigma-Aldrich) (200 μM) in DMEM/10% FCS. .. CD4+ T cells were stained with CD3-biotin with APC labeled streptavidin and CD4 PerCP, fixed and permeabilized, and intracellular cytokines were stained with PE anti-cytokine antibodies and isotype controls (BD Bioscience).

    Expressing:

    Article Title: TIM-4 Identifies IFN-γ–Expressing Proinflammatory B Effector 1 Cells That Promote Tumor and Allograft Rejection
    Article Snippet: The digested tissue was layered onto Lympholyte M and spun at 1500 × g for 20 min. Lymphocytes isolated from the buffy coat were enumerated. .. The cells were plated at 1 × 106 /ml and stimulated with PMA (50 ng/ml), ionomycin (500 ng/ml), and monensin (1:1000) for 4–5 h (Sigma Aldrich) for phenotypic assessment of infiltrating lymphocytes and their intracellular cytokine expression. .. μMT mice received 2 × 105 B16 cells (grown as above) by tail vein injection.

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    Millipore monensin
    Reduced Th2 cytokine production in CD11c cre IL-4Rα −/lox mice sensitized and challenged with HDM (day 14). ( A ) Cytokine production by lung CD4 + T cells after stimulation with <t>PMA/ionomycin/monensin.</t> ( B ) Cytokine production by mediastinal lymph node cells after restimulation with HDM extract, measured by ELISA. ( C ) HDM-specific antibodies measured in serum by ELISA. Graphs are representative of two experiments. Significant differences are shown between IL-4Rα −/lox PBS and the other groups unless otherwise indicated by brackets. *P
    Monensin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Reduced Th2 cytokine production in CD11c cre IL-4Rα −/lox mice sensitized and challenged with HDM (day 14). ( A ) Cytokine production by lung CD4 + T cells after stimulation with PMA/ionomycin/monensin. ( B ) Cytokine production by mediastinal lymph node cells after restimulation with HDM extract, measured by ELISA. ( C ) HDM-specific antibodies measured in serum by ELISA. Graphs are representative of two experiments. Significant differences are shown between IL-4Rα −/lox PBS and the other groups unless otherwise indicated by brackets. *P

    Journal: Scientific Reports

    Article Title: House dust mite induced allergic airway disease is attenuated in CD11ccreIL-4Rα−/l°x mice

    doi: 10.1038/s41598-017-19060-9

    Figure Lengend Snippet: Reduced Th2 cytokine production in CD11c cre IL-4Rα −/lox mice sensitized and challenged with HDM (day 14). ( A ) Cytokine production by lung CD4 + T cells after stimulation with PMA/ionomycin/monensin. ( B ) Cytokine production by mediastinal lymph node cells after restimulation with HDM extract, measured by ELISA. ( C ) HDM-specific antibodies measured in serum by ELISA. Graphs are representative of two experiments. Significant differences are shown between IL-4Rα −/lox PBS and the other groups unless otherwise indicated by brackets. *P

    Article Snippet: For intracellular cytokine staining, lung cells were seeded at 2 × 106 cells/well and stimulated at 37 o C for 4 hours with phorbal myristate acetate (Sigma-Aldrich) (50ng/ml), ionomycin (Sigma-Aldrich) (250ng/ml) and monensin (Sigma-Aldrich) (200 μM) in DMEM/10% FCS.

    Techniques: Mouse Assay, Enzyme-linked Immunosorbent Assay

    Enrichment of interleukin (IL)‐10 producing regulatory T cells (T reg ) cells in visceral leishmaniasis (VL) patients at disease site. (a) Enumeration of IL‐10‐producing T reg (CD4 + FoxP3 + IL‐10 + ) cells in bone marrow mononuclear cells (BM MNCs): isolated MNCs from bone marrow of VL patients were cultured for the assessment of IL‐10 production by antigen‐specific T reg cells in response to Leishmania donovani antigen (whole cell lysate; 10 μg/ml). Cells were cultured for 72 h in animal cell culture conditions (incubation at 37°C with 5% CO 2 ). Monensin (Golgi transport inhibitor; 1 mM) was added in the last 6 h of culture. On forward‐ versus side‐scatter gated lymphocytes, the dual population of CD4 + CD25 + was defined and divided further into CD4 + CD25 dim and CD4 + CD25 br T cells. Histogram plot of FoxP3 expressing CD4 + CD25 dim or CD4 + CD25 br (thin red dotted line) was overlaid on FoxP3 fluorescence minus one (FMO) (Fig. 2a, ii: inset). IL‐10 expression was then assessed on CD4 + CD25 br FoxP3 + T cells. For this, IL‐10 expressing CD4 + CD25 br FoxP3 + T cells were overlaid on IL‐10 FMO (Fig. 2, iii and iv). (b) Increased frequency of IL‐10‐producing T reg cells at disease site in VL patients with high parasitic load (HPL): CD4 + FoxP3 + pregated lymphocytes were used for illustration of the IL‐10‐producing T reg population (histogram). T reg ‐specific IL‐10 population was increased significantly in VL patients with HPL in response to whole cell lysate of L. donovani (10 μg/ml) [ n = 10: mean ± standard deviation (s.d.): 24·03 ± 6·31%] compared to the patients with low parasitic load (LPL) ( n = 12: mean ± s.d.: 3·87 ± 0·49%) ( P = 0·002: unpaired t ‐test). Horizontal lines in scatter‐plot depicted as mean value. (c) Significantly increased soluble level of IL‐10 in VL patients with HPL: enzyme‐linked immunosorbent assay (ELISA)‐based soluble level of IL‐10 in BM aspirate of HPL ( n = 11: mean ± s.d.: 208·5 ± 16·09 pg/ml) patients was significantly higher compared with LPL ( n = 13: mean ± s.d.: 106·3 ± 3·44 pg/ml) patients ( P = 0·0001: unpaired t ]

    Journal: Clinical and Experimental Immunology

    Article Title: T cell suppression in the bone marrow of visceral leishmaniasis patients: impact of parasite load

    doi: 10.1111/cei.13074

    Figure Lengend Snippet: Enrichment of interleukin (IL)‐10 producing regulatory T cells (T reg ) cells in visceral leishmaniasis (VL) patients at disease site. (a) Enumeration of IL‐10‐producing T reg (CD4 + FoxP3 + IL‐10 + ) cells in bone marrow mononuclear cells (BM MNCs): isolated MNCs from bone marrow of VL patients were cultured for the assessment of IL‐10 production by antigen‐specific T reg cells in response to Leishmania donovani antigen (whole cell lysate; 10 μg/ml). Cells were cultured for 72 h in animal cell culture conditions (incubation at 37°C with 5% CO 2 ). Monensin (Golgi transport inhibitor; 1 mM) was added in the last 6 h of culture. On forward‐ versus side‐scatter gated lymphocytes, the dual population of CD4 + CD25 + was defined and divided further into CD4 + CD25 dim and CD4 + CD25 br T cells. Histogram plot of FoxP3 expressing CD4 + CD25 dim or CD4 + CD25 br (thin red dotted line) was overlaid on FoxP3 fluorescence minus one (FMO) (Fig. 2a, ii: inset). IL‐10 expression was then assessed on CD4 + CD25 br FoxP3 + T cells. For this, IL‐10 expressing CD4 + CD25 br FoxP3 + T cells were overlaid on IL‐10 FMO (Fig. 2, iii and iv). (b) Increased frequency of IL‐10‐producing T reg cells at disease site in VL patients with high parasitic load (HPL): CD4 + FoxP3 + pregated lymphocytes were used for illustration of the IL‐10‐producing T reg population (histogram). T reg ‐specific IL‐10 population was increased significantly in VL patients with HPL in response to whole cell lysate of L. donovani (10 μg/ml) [ n = 10: mean ± standard deviation (s.d.): 24·03 ± 6·31%] compared to the patients with low parasitic load (LPL) ( n = 12: mean ± s.d.: 3·87 ± 0·49%) ( P = 0·002: unpaired t ‐test). Horizontal lines in scatter‐plot depicted as mean value. (c) Significantly increased soluble level of IL‐10 in VL patients with HPL: enzyme‐linked immunosorbent assay (ELISA)‐based soluble level of IL‐10 in BM aspirate of HPL ( n = 11: mean ± s.d.: 208·5 ± 16·09 pg/ml) patients was significantly higher compared with LPL ( n = 13: mean ± s.d.: 106·3 ± 3·44 pg/ml) patients ( P = 0·0001: unpaired t ]

    Article Snippet: Monensin (Golgi transport inhibitor; 1 mM; Sigma‐Aldrich) was added in the last 6 h of culture.

    Techniques: Isolation, Cell Culture, Incubation, Expressing, Fluorescence, Standard Deviation, Enzyme-linked Immunosorbent Assay

    Decreased frequency of interferon (IFN)‐γ‐ and interleukin (IL)‐17A‐producing cells in visceral leishmaniasis (VL) patients with high parasitic load (HPL). Enumeration of IFN‐γ‐ and IL‐17A‐producing cells in bone marrow mononuclear cells (BM MNCs): isolated MNCs ( n = 24) from bone marrow of VL patients were cultured for IFN‐γ and IL‐17A production: BM ‐MNCs were cultured for 24 h. At the 0 h time‐point, whole cell lysate of Leishmania donovani antigen (10 µg/ml) and at the 18 h time‐point, monensin was supplemented in culture. Finally, at the end of 24 h of culture, cells were harvested and used for intracellular staining of IFN‐γ‐ and IL‐17A‐producing cells using anti‐human IFN‐γ and IL‐17A monoclonal antibodies along with anti‐human CD4 antibodies. (a) Scatter‐plot of IFN‐γ‐producing cells on gated CD4 + T cells: significantly decreased percentage frequency of IFN‐γ‐producing cells in patients with HPL ( n = 11: mean ± s.d.: 0·87 ± 0·13%) in comparison with patients with LPL ( n = 13: mean ± s.d.: 2·72 ± 0·54%) ( P = 0·005). (b) Scatter‐plot of IL‐17A‐producing cells on gated CD4 + T cells: as of IFN‐γ; the percentage frequency of IL‐17A also follows the same trend between HPL ( n = 11: mean ± s.d.: 0·68 ± 0·12%) and low parasitic load (LPL) ( n = 13: mean ± s.d.: 1·83 ± 0·29%) ( P

    Journal: Clinical and Experimental Immunology

    Article Title: T cell suppression in the bone marrow of visceral leishmaniasis patients: impact of parasite load

    doi: 10.1111/cei.13074

    Figure Lengend Snippet: Decreased frequency of interferon (IFN)‐γ‐ and interleukin (IL)‐17A‐producing cells in visceral leishmaniasis (VL) patients with high parasitic load (HPL). Enumeration of IFN‐γ‐ and IL‐17A‐producing cells in bone marrow mononuclear cells (BM MNCs): isolated MNCs ( n = 24) from bone marrow of VL patients were cultured for IFN‐γ and IL‐17A production: BM ‐MNCs were cultured for 24 h. At the 0 h time‐point, whole cell lysate of Leishmania donovani antigen (10 µg/ml) and at the 18 h time‐point, monensin was supplemented in culture. Finally, at the end of 24 h of culture, cells were harvested and used for intracellular staining of IFN‐γ‐ and IL‐17A‐producing cells using anti‐human IFN‐γ and IL‐17A monoclonal antibodies along with anti‐human CD4 antibodies. (a) Scatter‐plot of IFN‐γ‐producing cells on gated CD4 + T cells: significantly decreased percentage frequency of IFN‐γ‐producing cells in patients with HPL ( n = 11: mean ± s.d.: 0·87 ± 0·13%) in comparison with patients with LPL ( n = 13: mean ± s.d.: 2·72 ± 0·54%) ( P = 0·005). (b) Scatter‐plot of IL‐17A‐producing cells on gated CD4 + T cells: as of IFN‐γ; the percentage frequency of IL‐17A also follows the same trend between HPL ( n = 11: mean ± s.d.: 0·68 ± 0·12%) and low parasitic load (LPL) ( n = 13: mean ± s.d.: 1·83 ± 0·29%) ( P

    Article Snippet: Monensin (Golgi transport inhibitor; 1 mM; Sigma‐Aldrich) was added in the last 6 h of culture.

    Techniques: Isolation, Cell Culture, Staining

    Anti–TIM-4 inhibits IFN-γ expression by TIM-4 + B cells and augments IL-10 expression by TIM-1 + B cells in vitro. Purified B cells from IL-10–GFP reporter mice (BALB/c) were treated in vitro with LPS (2 μg/ml) and RIgG2a or anti–TIM-4 for 48 h. PMA, ionomycin, and monensin were added for the final 5 h. IL-10 expression was detected by GFP expression, whereas IFN-γ was detected by intracellular staining. Representative flow cytometry plots showing IFN-γ expression ( A ) or IL-10 expression ( C ) on CD19 + , CD19 + TIM-1 − TIM-4 − (DN), CD19 + TIM-1 + , and CD19 + TIM-4 + B cells. Frequency (mean + SD) of IFN-γ ( B ) or IL-10 ( D ) on cells in (A) ( n = 3). * p

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

    Article Title: TIM-4 Identifies IFN-γ–Expressing Proinflammatory B Effector 1 Cells That Promote Tumor and Allograft Rejection

    doi: 10.4049/jimmunol.1602107

    Figure Lengend Snippet: Anti–TIM-4 inhibits IFN-γ expression by TIM-4 + B cells and augments IL-10 expression by TIM-1 + B cells in vitro. Purified B cells from IL-10–GFP reporter mice (BALB/c) were treated in vitro with LPS (2 μg/ml) and RIgG2a or anti–TIM-4 for 48 h. PMA, ionomycin, and monensin were added for the final 5 h. IL-10 expression was detected by GFP expression, whereas IFN-γ was detected by intracellular staining. Representative flow cytometry plots showing IFN-γ expression ( A ) or IL-10 expression ( C ) on CD19 + , CD19 + TIM-1 − TIM-4 − (DN), CD19 + TIM-1 + , and CD19 + TIM-4 + B cells. Frequency (mean + SD) of IFN-γ ( B ) or IL-10 ( D ) on cells in (A) ( n = 3). * p

    Article Snippet: The cells were plated at 1 × 106 /ml and stimulated with PMA (50 ng/ml), ionomycin (500 ng/ml), and monensin (1:1000) for 4–5 h (Sigma Aldrich) for phenotypic assessment of infiltrating lymphocytes and their intracellular cytokine expression.

    Techniques: Expressing, In Vitro, Purification, Mouse Assay, Staining, Flow Cytometry, Cytometry

    A Model Integrating Na V in Regeneration By 6 hpa, the H + pump V-ATPase is expressed in the regeneration bud where it regulates the membrane voltage of the bud. V-ATPase activation results in the up-regulation of Na V 1.2 by 18 hpa. Ablation of Na V 1.2 expression (RNAi) or Na V function (pharmacological treatment) inhibits regeneration. Na V activity enables sodium ions to enter regeneration bud cells and, potentially through SIK, to activate downstream pathways (such as BMP and Notch) by 24 hpa, driving regenerative outgrowth and patterning. By 7 days after injury, the rebuilding of the tail is largely complete. Importantly, monensin-mediated induction of a transient sodium flux into non-regenerative buds is sufficient to restore full tail regeneration, demonstrating that intracellular sodium signaling is a key regulator of regeneration able to initiate repair even after a non-regenerative wound epithelium has formed.

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Induction of Vertebrate Regeneration by a Transient Sodium Current

    doi: 10.1523/JNEUROSCI.3315-10.2010

    Figure Lengend Snippet: A Model Integrating Na V in Regeneration By 6 hpa, the H + pump V-ATPase is expressed in the regeneration bud where it regulates the membrane voltage of the bud. V-ATPase activation results in the up-regulation of Na V 1.2 by 18 hpa. Ablation of Na V 1.2 expression (RNAi) or Na V function (pharmacological treatment) inhibits regeneration. Na V activity enables sodium ions to enter regeneration bud cells and, potentially through SIK, to activate downstream pathways (such as BMP and Notch) by 24 hpa, driving regenerative outgrowth and patterning. By 7 days after injury, the rebuilding of the tail is largely complete. Importantly, monensin-mediated induction of a transient sodium flux into non-regenerative buds is sufficient to restore full tail regeneration, demonstrating that intracellular sodium signaling is a key regulator of regeneration able to initiate repair even after a non-regenerative wound epithelium has formed.

    Article Snippet: For refractory period analysis, tails were amputated at st. 46–47, and at 18 hpa animals were treated with or without 90mM sodium and 20µM monensin (Sigma) in 0.1X MMR with 90µM CoroNa Green for 45 min and washed twice in 0.1X MMR and 50µM BTS.

    Techniques: Activation Assay, Expressing, Activity Assay

    Transient Induction of Sodium Current Drives Regeneration ( A ) Regeneration rescue by human Na V 1.5. Control tail stumps (β-gal-injected) cut during the refractory period regenerate poorly, which is rescued by hNa V 1.5 expression. ( B ) Effects of regeneration rescue by hNa V 1.5 during refractory period block. ( C ) CoroNa Green analysis of Sodium current induction. ( C1 ) Control (vehicle only), non-induced refractory stage bud has little CoroNa Green signal. ( C2 ) Induction with 90mM sodium and 20µM monensin for 1 hour (18–19 hpa) significantly increases intracellular sodium (green). Images are merged brightfield and fluorescence of the same exposure time. white circle = refractory bud. ( C3 ) Most refractory stage amputations fail to regenerate. ( C4 ) Stimulation with sodium current restores full regeneration. ( D ) Transient sodium current rescues non-regenerative wound epidermis. Stimulation of sodium current increased regeneration > 2-fold and improved regeneration quality as compared to control siblings (treated with vehicle only: 0.01% ethanol). Treatment with either monensin or 90mM sodium alone showed no effect. Scale bars: ( A ) 1mm, ( C ) 500µm.

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Induction of Vertebrate Regeneration by a Transient Sodium Current

    doi: 10.1523/JNEUROSCI.3315-10.2010

    Figure Lengend Snippet: Transient Induction of Sodium Current Drives Regeneration ( A ) Regeneration rescue by human Na V 1.5. Control tail stumps (β-gal-injected) cut during the refractory period regenerate poorly, which is rescued by hNa V 1.5 expression. ( B ) Effects of regeneration rescue by hNa V 1.5 during refractory period block. ( C ) CoroNa Green analysis of Sodium current induction. ( C1 ) Control (vehicle only), non-induced refractory stage bud has little CoroNa Green signal. ( C2 ) Induction with 90mM sodium and 20µM monensin for 1 hour (18–19 hpa) significantly increases intracellular sodium (green). Images are merged brightfield and fluorescence of the same exposure time. white circle = refractory bud. ( C3 ) Most refractory stage amputations fail to regenerate. ( C4 ) Stimulation with sodium current restores full regeneration. ( D ) Transient sodium current rescues non-regenerative wound epidermis. Stimulation of sodium current increased regeneration > 2-fold and improved regeneration quality as compared to control siblings (treated with vehicle only: 0.01% ethanol). Treatment with either monensin or 90mM sodium alone showed no effect. Scale bars: ( A ) 1mm, ( C ) 500µm.

    Article Snippet: For refractory period analysis, tails were amputated at st. 46–47, and at 18 hpa animals were treated with or without 90mM sodium and 20µM monensin (Sigma) in 0.1X MMR with 90µM CoroNa Green for 45 min and washed twice in 0.1X MMR and 50µM BTS.

    Techniques: Injection, Expressing, Blocking Assay, Fluorescence