Compounds were purchased from Chemdiv, San Diego CA: CK-0944636 (Catalog number 8012-5103), CK-0993548 (Catalog number K205-1650), CK-0944666 (Catalog number 8012-5153) and CK-0157869 (Catalog number K205-0942). We purified native Arp2/3 complex from human platelets12 (link), bovine thymus6 (link), Schizosaccharomyces pombe13 (link) and Saccharomyces cerevisiae (Supplemental methods ), actin from chicken skeletal muscle14 (link) and recombinant HsWASp, WASp105-502, WASp-VCA and Cdc4212 (link), N-WASp-VCA 428-505 (Supplemental methods ), GST-ActA 36-170 (Supplemental methods ) and S. pombe Cdc12p(FH2)-His 973-139015 (link) from E. coli. We used standard assays to measure polymerization of pyrenyl-actin16 (link) and to visualize actin filaments by fluorescence microscopy17 (link). Binding of etheno-ATP to Arp2/3 complex was performed as described previously with slight modifications18 (link). We crystallized BtArp2/3 complex7 (link) with either 0.5 mM CK-548 or 1 mM CK-636 in DMSO or soaked these compounds into crystals for 24 hours before freezing in liquid nitrogen. Diffraction data were collected at beamline X29A at Brookhaven National Laboratories. SKOV3 cells were infected with Listeria monocytogenes and fixed with 2% formaldehyde, permeabilized with 0.1% Triton-X in PBS, stained with Listeria antibody (US Biologics, Cleveland, Ohio) and Alexa Fluor 568 phalloidin (Molecular Probes, Eugene, OR), and imaged by fluorescence microscopy. We used an Isodata threshold on background-subtracted images of Listeria to isolate individual bacterium and measure the ratio of colocalized actin to Listeria fluorescence. Monocyte THP-1 cells were differentiated in 50 nM phorbol myristate acetate (Sigma-Aldrich-Fluka) to form podosomes before treatment with compounds. Black molly keratocytes19 (link) were observed by time-lapse phase contrast microscopy.
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Anatomy
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Cell Component
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Microfilaments
Microfilaments
Microfilaments are thin, thread-like structures found within the cytoplasm of cells.
These filaments are composed of actin proteins and play a crucial role in cell motility, cell division, and the maintenance of cell shape.
Microfilaments are dynamic structures that can polymerize and depolymerize in response to various cellular signals, allowing cells to undergo rapid changes in their morphology and movement.
They are involved in a wide range of cellular processes, including muscle contraction, vesicle trafficking, and the formation of specialized structures such as filopodia and lamellipodia.
Understanding the regulation and function of microfilaments is essential for research in areas such as cell biology, developmental biology, and neuroscience.
The PubCompare.ai platform can help researchers streamline their microfilament research by identifying the best protocols from literature, preprints, and patents, and providing intelligent comparisons to optimize experimental outcomes.
These filaments are composed of actin proteins and play a crucial role in cell motility, cell division, and the maintenance of cell shape.
Microfilaments are dynamic structures that can polymerize and depolymerize in response to various cellular signals, allowing cells to undergo rapid changes in their morphology and movement.
They are involved in a wide range of cellular processes, including muscle contraction, vesicle trafficking, and the formation of specialized structures such as filopodia and lamellipodia.
Understanding the regulation and function of microfilaments is essential for research in areas such as cell biology, developmental biology, and neuroscience.
The PubCompare.ai platform can help researchers streamline their microfilament research by identifying the best protocols from literature, preprints, and patents, and providing intelligent comparisons to optimize experimental outcomes.
Most cited protocols related to «Microfilaments»
Actin-Related Protein 2-3 Complex
Actins
alexa 568
Bacteria
Biological Assay
Biological Factors
Cattle
Cells
Chickens
CK-0944636
CK-0944666
CK-0993548
Escherichia coli
Fluorescence
Formaldehyde
Homo sapiens
Immunoglobulins
Isoenzyme CPK MB
Listeria
Listeria monocytogenes
Microfilaments
Microscopy, Fluorescence
Microscopy, Phase-Contrast
Molecular Probes
Molly
Monocytes
Nitrogen
Phalloidine
Podosomes
Polymerization
Saccharomyces cerevisiae
Schizosaccharomyces
Schizosaccharomyces pombe
Skeleton
Sulfoxide, Dimethyl
Tetradecanoylphorbol Acetate
THP-1 Cells
WASL protein, human
WAS protein, human
Compounds were purchased from Chemdiv, San Diego CA: CK-0944636 (Catalog number 8012-5103), CK-0993548 (Catalog number K205-1650), CK-0944666 (Catalog number 8012-5153) and CK-0157869 (Catalog number K205-0942). We purified native Arp2/3 complex from human platelets12 (link), bovine thymus6 (link), Schizosaccharomyces pombe13 (link) and Saccharomyces cerevisiae (Supplemental methods ), actin from chicken skeletal muscle14 (link) and recombinant HsWASp, WASp105-502, WASp-VCA and Cdc4212 (link), N-WASp-VCA 428-505 (Supplemental methods ), GST-ActA 36-170 (Supplemental methods ) and S. pombe Cdc12p(FH2)-His 973-139015 (link) from E. coli. We used standard assays to measure polymerization of pyrenyl-actin16 (link) and to visualize actin filaments by fluorescence microscopy17 (link). Binding of etheno-ATP to Arp2/3 complex was performed as described previously with slight modifications18 (link). We crystallized BtArp2/3 complex7 (link) with either 0.5 mM CK-548 or 1 mM CK-636 in DMSO or soaked these compounds into crystals for 24 hours before freezing in liquid nitrogen. Diffraction data were collected at beamline X29A at Brookhaven National Laboratories. SKOV3 cells were infected with Listeria monocytogenes and fixed with 2% formaldehyde, permeabilized with 0.1% Triton-X in PBS, stained with Listeria antibody (US Biologics, Cleveland, Ohio) and Alexa Fluor 568 phalloidin (Molecular Probes, Eugene, OR), and imaged by fluorescence microscopy. We used an Isodata threshold on background-subtracted images of Listeria to isolate individual bacterium and measure the ratio of colocalized actin to Listeria fluorescence. Monocyte THP-1 cells were differentiated in 50 nM phorbol myristate acetate (Sigma-Aldrich-Fluka) to form podosomes before treatment with compounds. Black molly keratocytes19 (link) were observed by time-lapse phase contrast microscopy.
Actin-Related Protein 2-3 Complex
Actins
alexa 568
Bacteria
Biological Assay
Biological Factors
Cattle
Cells
Chickens
CK-0944636
CK-0944666
CK-0993548
Escherichia coli
Fluorescence
Formaldehyde
Homo sapiens
Immunoglobulins
Isoenzyme CPK MB
Listeria
Listeria monocytogenes
Microfilaments
Microscopy, Fluorescence
Microscopy, Phase-Contrast
Molecular Probes
Molly
Monocytes
Nitrogen
Phalloidine
Podosomes
Polymerization
Saccharomyces cerevisiae
Schizosaccharomyces
Schizosaccharomyces pombe
Skeleton
Sulfoxide, Dimethyl
Tetradecanoylphorbol Acetate
THP-1 Cells
WASL protein, human
WAS protein, human
Adenovirus Vaccine
blebbistatin
Cells
Flavoproteins
Fluorescence
Heart
Heart Ventricle
Langendorff Perfused Heart
Mice, Transgenic
Microfilaments
Microscopy, Confocal
Mitochondria
Muscle Cells
Myocardium
NADH
Neurons
Open Reading Frames
Pulse Rate
Reading Frames
Retention (Psychology)
rhod-2
Submersion
Superoxides
MEFs were derived from e10.5 embryos. Embryos were mechanically dispersed by repeated passage through a P1000 pipette tip and plated with MEF media (DME, 10% FCS, 1× nonessential amino acids, 1 mM l -glutamine, penicillin/streptomycin [Life Technologies/GIBCO BRL]).
For visualization of mitochondria, the MEFs were either stained with 150 nM MitoTracker Red CMXRos (Molecular Probes) or infected with a retrovirus expressing EYFP fused to the presequence from subunit VIII of human cytochrome c oxidase, which directs EYFP to the mitochondrial matrix (a gift from R. Lansford, California Institute of Technology, Pasadena, CA) (Okada et al., 1999 (link)). To facilitate immortalization, the MEFs were later infected with a retrovirus expressing SV40 large T antigen (a gift from L. Jackson-Grusby, Massachusetts Institute of Technology) (Jat et al., 1986 (link)). Neither retroviral infection nor immortalization affected mitochondrial morphology. To label actin filaments, cells were fixed in 4% PFA and stained with 2.5 U/ml rhodamine-phalloidin (Molecular Probes). The stained cells were postfixed in 4% PFA.
For time-lapse confocal microscopy, cells were plated at low density onto chambered glass coverslips. Cells with culture medium were overlaid with light mineral oil and imaged in a 37°C chamber. EYFP-optimized filters and dichroics (q497lp, HQ500lp; Chroma) were used on a Zeiss 410 laser scanning confocal microscope (Carl Zeiss MicroImaging, Inc.)
TS cells from e3.5 blastocysts were derived using established protocols (Tanaka et al., 1998a (link)). Live cells were stained with MitoTracker Red (150 nM) and Syto16 (100 nM; Molecular Probes).
For visualization of mitochondria, the MEFs were either stained with 150 nM MitoTracker Red CMXRos (Molecular Probes) or infected with a retrovirus expressing EYFP fused to the presequence from subunit VIII of human cytochrome c oxidase, which directs EYFP to the mitochondrial matrix (a gift from R. Lansford, California Institute of Technology, Pasadena, CA) (Okada et al., 1999 (link)). To facilitate immortalization, the MEFs were later infected with a retrovirus expressing SV40 large T antigen (a gift from L. Jackson-Grusby, Massachusetts Institute of Technology) (Jat et al., 1986 (link)). Neither retroviral infection nor immortalization affected mitochondrial morphology. To label actin filaments, cells were fixed in 4% PFA and stained with 2.5 U/ml rhodamine-phalloidin (Molecular Probes). The stained cells were postfixed in 4% PFA.
For time-lapse confocal microscopy, cells were plated at low density onto chambered glass coverslips. Cells with culture medium were overlaid with light mineral oil and imaged in a 37°C chamber. EYFP-optimized filters and dichroics (q497lp, HQ500lp; Chroma) were used on a Zeiss 410 laser scanning confocal microscope (Carl Zeiss MicroImaging, Inc.)
TS cells from e3.5 blastocysts were derived using established protocols (Tanaka et al., 1998a (link)). Live cells were stained with MitoTracker Red (150 nM) and Syto16 (100 nM; Molecular Probes).
Amino Acids
Blastocyst
Cell Culture Techniques
Cells
COX8C protein, human
Culture Media
Embryo
Glutamine
Large T-Antigen
Light
Microfilaments
Microscopy, Confocal
Mitochondria
Mitochondrial Inheritance
MitoTracker red CMXRos
Molecular Probes
Oil, Mineral
Penicillins
Retroviridae
Retroviridae Infections
rhodamine-phalloidin
Simian virus 40
Streptomycin
First, a model of actin filament we built on our 3.6 Å resolution map (PDB ID: 5JLF)23 (link) was fitted into the 3D map of the thin filament as a rigid body. For modeling Tm structure, a homology model of Tm was constructed with the full length Tm crystal structure determined at 7 Å resolution (PDB: 1C1G)12 (link) as a template and fitted it into the 3D map. The Tn core domain was fitted by one of the crystal structures of human cardiac Tn in the Ca2+ bound state (PDB: 4Y99)13 (link). Since the resolution of the density of TnCN was not high enough to perform flexible fitting, we divided the Tn core into three domains, TnCN, TnCC, and IT arm, and treated them as rigid bodies. Since the Tm-Tm junction was clearly resolved in the 3D map, it was possible to place the N- and C-termini of four TM chains into the junction to build a model of Tm for its entire length. We then subtracted the model densities of actin filament and Tm from the 3D map of the thin filament to produce a difference map, which revealed the densities for the remaining chains of an N-terminal region of TnT (TnTN) and the C-terminal region of TnI (TnIC). For modeling TnTN, an α-helix model of TnTN residues 87–150 was built by MODELLER36 , and the interactions between the C-terminal end of rabbit skeletal Tm and a short fragment of chicken skeletal TnT revealed in the crystal structure (PDB: 2Z5H)21 (link) was used to build a model of Tm–TnTN complex. For TnIC, the difference map showed an elongated density along actin filament and Tm coiled coil above the Tn core only in the Ca2+ free state. We used the long C-terminal α-helix visualized in one of the crystal structure of human cardiac Tn (PDB: 1J1E)13 (link) to fit into the difference map and modeled the remaining C-terminal region as an extended chain. We used RosettaCM19 (link) for all the modeling and refinement to remove clashes between actin, Tm and Tn and keeping their stereochemistry and used UCSF Chimera for the preparation of all the figures37 (link).
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Actins
Chickens
Chimera
Cytoskeletal Filaments
Heart
Helix (Snails)
Homo sapiens
Human Body
Microfilaments
Muscle Rigidity
Rabbits
Skeleton
Most recents protocols related to «Microfilaments»
Example 8
Cell adhesion was also evaluated by means of in vitro scratch wound-healing assay. HDPSCs cells were analyzed by difference in staining with phalloidin (cell nucleus) and DAPI to visualize actin cytoskeleton.
Cell adhesion results showed excellent interaction and adhesion between neighboring cells in the presence of bioceramic composition. The Bioceramic composition sealer (CB5) and Bioceramic composition repair (CB6), showed a gradual increase in growth over time, an extended morphology and a high content of F-Actin (cell microfilamen), reaching confluence after 72 hours of culture.
The analysis of cell proliferation (via cell viability study), apoptosis, cell adhesion and morphology (via cell adhesion study) and migration (via cell migration study) showed very positive results, indicating that the proposed bioceramic composition induces the odonto/osteogenic mineralization and differentiation process in the presence of tooth-specific human stem cells (hDPSCs pulp). While a market resin sealer was also used in the comparative studies, however, all results were not satisfactory for this product.
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Apoptosis
Biological Assay
Cell Adhesion
Cell Nucleus
Cell Proliferation
Cell Survival
DAPI
Dental Pulp
Differentiations, Cell
F-Actin
Homo sapiens
Microfilaments
Migration, Cell
Osteogenesis
Phalloidine
Physiologic Calcification
Resins, Plant
Stem, Plant
Stem Cells
Tooth
To analyze
cellular cytoskeletal staining and to visualize overall cell morphology
on fibrinogen scaffolds with different topographies, cells were fixated
using 4% (v/v) solution of paraformaldehyde (PFA) in PBS (Biotrend,
Cologne, Germany) for 30 min at room temperature and were analyzed
via fluorescence microscopy as well as SEM imaging.
For cytoskeletal
staining, actin filaments of cells grown on fibrinogen scaffolds for
4 days were stained with phalloidin (ActinRed ReadyProbes Reagent,
Life Technologies Europe BV, Netherlands) and nuclei were stained
with Hoechst H33342 (NucBlue Live ReadyProbes Reagent, Life Technologies)
for 30 min at room temperature using 2 drops/500 μL of PBS.
After washing two times with PBS, stained samples were mounted onto
glass slides with Prolong Gold antifade mounting medium (ThermoFisher)
and cured overnight at room temperature. The specimens were imaged
at 40× magnification in an inverted fluorescence microscope (Ti-E
– V5.30, Nikon, Tokyo, Japan) and appropriate filter settings
(λex = 540 nm and λem = 565 nm for
Actin Red and λex = 330–380 nm and λem = 435–485 nm for H33342).
Fluorescence images
of phalloidin and H33342 stained cells were
analyzed using the open-source software ImageJ provided by the NIH,51 (link) from three independent experiments performed
in triplicate for each substrate type, amounting to nine images analyzed
per sample. Analysis of the cell orientation was performed using the
red and blue channel via the ImageJ plugin OrientationJ and the Origin
2021 software as described earlier.45 (link),47 (link)For
SEM analysis, cells grown on fibrinogen scaffolds for 10 days
were dried with ethanol exchange by gradually increasing the concentration
of pure ethanol on the samples. Samples were subsequently sputter-coated
with gold for 25 s using a sputter coater 108 auto system (Tescan
GmbH, Dortmund, Germany) before SEM imaging with a Zeiss Supra 40
device (Carl Zeiss, Oberkochen, Germany) at an acceleration voltage
of 3 kV.
cellular cytoskeletal staining and to visualize overall cell morphology
on fibrinogen scaffolds with different topographies, cells were fixated
using 4% (v/v) solution of paraformaldehyde (PFA) in PBS (Biotrend,
Cologne, Germany) for 30 min at room temperature and were analyzed
via fluorescence microscopy as well as SEM imaging.
For cytoskeletal
staining, actin filaments of cells grown on fibrinogen scaffolds for
4 days were stained with phalloidin (ActinRed ReadyProbes Reagent,
Life Technologies Europe BV, Netherlands) and nuclei were stained
with Hoechst H33342 (NucBlue Live ReadyProbes Reagent, Life Technologies)
for 30 min at room temperature using 2 drops/500 μL of PBS.
After washing two times with PBS, stained samples were mounted onto
glass slides with Prolong Gold antifade mounting medium (ThermoFisher)
and cured overnight at room temperature. The specimens were imaged
at 40× magnification in an inverted fluorescence microscope (Ti-E
– V5.30, Nikon, Tokyo, Japan) and appropriate filter settings
(λex = 540 nm and λem = 565 nm for
Actin Red and λex = 330–380 nm and λem = 435–485 nm for H33342).
Fluorescence images
of phalloidin and H33342 stained cells were
analyzed using the open-source software ImageJ provided by the NIH,51 (link) from three independent experiments performed
in triplicate for each substrate type, amounting to nine images analyzed
per sample. Analysis of the cell orientation was performed using the
red and blue channel via the ImageJ plugin OrientationJ and the Origin
2021 software as described earlier.45 (link),47 (link)For
SEM analysis, cells grown on fibrinogen scaffolds for 10 days
were dried with ethanol exchange by gradually increasing the concentration
of pure ethanol on the samples. Samples were subsequently sputter-coated
with gold for 25 s using a sputter coater 108 auto system (Tescan
GmbH, Dortmund, Germany) before SEM imaging with a Zeiss Supra 40
device (Carl Zeiss, Oberkochen, Germany) at an acceleration voltage
of 3 kV.
Acceleration
Cell Nucleus
Cells
Cytoskeleton
Ethanol
Fibrinogen
Fluorescence
Gold
HOE 33342
Microfilaments
Microscopy, Fluorescence
paraform
Phalloidine
For all cell assays, HepG2 at passages below 10 were seeded in the gel at a final concentration of 1 × 106 cells/ml and experiments carried out for n = 3. Proliferation of HepG2 in culture was assessed with a CellTiter Blue assay (Promega Corporation, Fitchburg, United States of America). 100 µl of medium with 20 µl CellTiter Blue were added to each well and incubated at 37°C for 3 h. Fluorescence intensity of the supernatant was read with an Infinite M Plex plate reader (Tecan Group AG, Männedorf, Switzerland). Cell viability was determined by staining for live cells with fluorescein diacetate (Sigma-Aldrich, St. Louis, United States of America) and dead cells with propidium iodide (Carl Roth GmbH + Co. KG, Karlsruhe, Germany) (1:60 diluted in Ringer’s solution). Quantification of viable and dead cells was done in ImageJ (see Supplementary Figure S3 ).
For the analysis of live cell morphology inside the gels, HepG2 were incubated with 2 µM CellTracker™ Green CMFDA Dye (Thermo Fisher Scientific Inc. Waltham, United States of America) per 10 × 106 cells for 30 min before seeding. Cells retained their fluorescence signal and passed it on to daughter cells for up to 7 days. Before immunofluorescence stains, cells were fixed in 4% paraformaldehyde (Carl Roth GmbH + Co. KG, Karlsruhe, Germany) for 15 min and permeabilized with 0.5% Triton X-100 in PBS (Carl Roth GmbH + Co. KG, Karlsruhe, Germany) for 10 min. Actin filaments were stained for 30 min with Alexa Fluor 488 Phalloidin (1:400 dilution in PBS) (Thermo Fisher Scientific Inc. Waltham, United States of America) and nuclei for 3 min with DAPI (1:800 dilution in PBS) (Sigma Aldrich, St. Louis, United States of America).
For the analysis of live cell morphology inside the gels, HepG2 were incubated with 2 µM CellTracker™ Green CMFDA Dye (Thermo Fisher Scientific Inc. Waltham, United States of America) per 10 × 106 cells for 30 min before seeding. Cells retained their fluorescence signal and passed it on to daughter cells for up to 7 days. Before immunofluorescence stains, cells were fixed in 4% paraformaldehyde (Carl Roth GmbH + Co. KG, Karlsruhe, Germany) for 15 min and permeabilized with 0.5% Triton X-100 in PBS (Carl Roth GmbH + Co. KG, Karlsruhe, Germany) for 10 min. Actin filaments were stained for 30 min with Alexa Fluor 488 Phalloidin (1:400 dilution in PBS) (Thermo Fisher Scientific Inc. Waltham, United States of America) and nuclei for 3 min with DAPI (1:800 dilution in PBS) (Sigma Aldrich, St. Louis, United States of America).
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2-(2-(2-chloro-3-(2-(3,3-dimethyl-5-sulfo-1-(4-sulfo-butyl)-3H-indol-2-yl)-vinyl)-cyclohex-2-enylidene)-ethylidene)-3,3-dimethyl-1-(4-sulfo-butyl)-2,3-dihydro-1H-indole-5-carboxylic acid
5-chloromethylfluorescein diacetate
alexa fluor 488
Biological Assay
Cell Nucleus
Cells
Cell Survival
DAPI
Daughter
diacetylfluorescein
Fluorescence
Gels
Immunofluorescence
Microfilaments
paraform
Phalloidine
Promega
Propidium Iodide
Ringer's Solution
Staining
Technique, Dilution
Triton X-100
After culturing the cells were fixed with 4% PFA in PBS for 10 min at RT. The actin cytoskeleton was stained with Alexa 488-conjugated phalloidin (200 U/ml stock diluted 1:100 in PBS; Invitrogen Europe, Paisley, UK) for 20 min at + 37 °C. Nuclei were stained with Hoechst 33258 (1 mg/ml stock diluted 1:800 in PBS; Sigma-Aldrich) for 10 min at room temperature (RT). Staining for osteoclast-specific enzyme TRACP was carried out with a commercial acid phosphatase leukocyte kit (Sigma-Aldrich) for 20 min at + 37 °C. The samples were mounted in 70% glycerol-PBS and viewed in a Zeiss Axio Scope.A1 fluorescence microscope (Oberkochen, Germany) and EC Plan Neofluar 20 × objective. Multinuclear cells with three or more nuclei were counted from each bone slice from five randomly chosen microscope fields, bone slice n = 4–6. The number of nuclei per cell were counted from 5 multinuclear cells from 5 randomly chosen areas. Images were taken with Nikon Eclipse E600 fluorescence microscope using Plan 20 ×/0.5 objective (Tokyo, Japan), QImaging MicroPublisher 5.0 RTV camera and QCapture 2.90.1 software (QImaging, Surrey, Canada). Confocal images were taken with Leica TCS SP8 confocal with a DMI8 microscope using LAS X 3.5.2 acquisition software. The objective used was an HC PL APO CS2 20 ×/0.75 DRY. Samples were imaged with 488 nm and 405 nm solid-state lasers; the pinhole was set to Airy 1 and scan speed to 600 Hz.
Full text: Click here
Acid Phosphatase
Bones
Cell Nucleus
Cells
E-600
Enzymes
GART protein, human
Glycerin
Hoechst 33258
Leukocytes
Microfilaments
Microscopy
Microscopy, Confocal
Microscopy, Fluorescence
Osteoclasts
Phalloidine
Radionuclide Imaging
Tartrate-Resistant Acid Phosphatase
To determined possible effects on myofilament organization by the stone heart development, trabecular preparations were isolated from fresh control hearts and from hearts with developed stone heart condition. The muscle strips were mounted horizontally using silk thread in a temperature controlled (37°C) cuvette in MOPS buffered physiological solution (NaCl 118, KCl 5, Na2HPO4 1.2, MgC2 1.2, CaCl2 1.6, glucose 10 mM, pH 7.4). The solution was gassed with air and exchanged every 5–10 min. The cuvette was equipped with Kapton windows and mounted on a stand in the CoSAXS beamline at the MAX IV synchrotron light facility, Lund, Sweden. The X-ray beam (wavelength 1 Å), had a size at the sample of about 50 × 60 μm. The sample detector distance was set to 3.5 m which gave a good resolution of the equatorial pattern using exposures of 0.5–1 s. The sample was moved between exposures to prevent beam damage. Scattering patterns were recorded using an EIGER 2 × 4 M detector (Dectris AG, Baden-Daettwil, Switzerland) and analyzed using a dedicated software. For each sample, recordings were made at different lengths (L) starting at slack length (Ls) and stretched to 1.0, 1.2, 1.3, and 1.4 L/Ls. At each length, the filament lattice spacing and intensity of the equatorial reflections were determined.
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Calculi
Cancellous Bone
Cytoskeletal Filaments
Glucose
Heart
Light
Microfilaments
morpholinopropane sulfonic acid
Muscle Tissue
physiology
Radiography
Reflex
Silk
Sodium Chloride
Top products related to «Microfilaments»
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Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
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DAPI is a fluorescent dye that binds strongly to adenine-thymine (A-T) rich regions in DNA. It is commonly used as a nuclear counterstain in fluorescence microscopy to visualize and locate cell nuclei.
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Alexa Fluor 488 phalloidin is a fluorescent dye that selectively binds to F-actin, a component of the cytoskeleton. It is used in microscopy and flow cytometry applications to visualize and study the distribution and organization of actin filaments within cells.
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DAPI is a fluorescent dye used in microscopy and flow cytometry to stain cell nuclei. It binds strongly to the minor groove of double-stranded DNA, emitting blue fluorescence when excited by ultraviolet light.
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Rhodamine phalloidin is a fluorescent dye used for staining and visualizing actin filaments in cells. It binds specifically to actin and can be used to label the cytoskeleton in fixed cells for microscopy analysis.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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Hoechst 33342 is a fluorescent dye that binds to DNA. It is commonly used in various applications, such as cell staining and flow cytometry, to identify and analyze cell populations.
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Paraformaldehyde is a white, crystalline solid compound that is a polymer of formaldehyde. It is commonly used as a fixative in histology and microscopy applications to preserve biological samples.
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Alexa Fluor 488 is a fluorescent dye used in various biotechnological applications. It has an excitation maximum at 495 nm and an emission maximum at 519 nm, producing a green fluorescent signal. Alexa Fluor 488 is known for its brightness, photostability, and pH-insensitivity, making it a popular choice for labeling biomolecules in biological research.
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Phalloidin-TRITC is a fluorescent dye used to label and visualize actin filaments in cells. It binds specifically to F-actin and emits a red fluorescent signal when excited by an appropriate light source. This product is commonly used in microscopy and cell biology applications.
More about "Microfilaments"
Microfilaments, also known as actin filaments, are thin, thread-like cytoskeletal structures found within the cytoplasm of cells.
These dynamic, polymerizing and depolymerizing filaments are composed of actin proteins and play a crucial role in various cellular processes, such as cell motility, cell division, and the maintenance of cell shape.
Microfilaments are involved in a wide range of activities, including muscle contraction, vesicle trafficking, and the formation of specialized structures like filopodia and lamellipodia.
Understanding the regulation and function of microfilaments is essential for research in fields like cell biology, developmental biology, and neuroscience.
Researchers can utilize tools like Triton X-100 (a detergent), DAPI (a nuclear stain), Alexa Fluor 488 phalloidin and Rhodamine phalloidin (actin-binding fluorescent probes), Bovine serum albumin (a blocking agent), Hoechst 33342 (another nuclear stain), and Paraformaldehyde (a fixative) to visualize and study microfilaments.
The PubCompare.ai platform can enhance microfilament research by helping researchers identify the best protocols from literature, preprints, and patents, and providing intelligent comparisons to optimize experimental outcomes.
By streamlining the research workflow and improving reproducibility, PubCompare.ai can support advancements in our understanding of these essential cytoskeletal structures and their roles in cellular processes.
Alexa Fluor 488, a fluorescent dye, can also be used to label and visualize microfilaments in various experimental setings.
These dynamic, polymerizing and depolymerizing filaments are composed of actin proteins and play a crucial role in various cellular processes, such as cell motility, cell division, and the maintenance of cell shape.
Microfilaments are involved in a wide range of activities, including muscle contraction, vesicle trafficking, and the formation of specialized structures like filopodia and lamellipodia.
Understanding the regulation and function of microfilaments is essential for research in fields like cell biology, developmental biology, and neuroscience.
Researchers can utilize tools like Triton X-100 (a detergent), DAPI (a nuclear stain), Alexa Fluor 488 phalloidin and Rhodamine phalloidin (actin-binding fluorescent probes), Bovine serum albumin (a blocking agent), Hoechst 33342 (another nuclear stain), and Paraformaldehyde (a fixative) to visualize and study microfilaments.
The PubCompare.ai platform can enhance microfilament research by helping researchers identify the best protocols from literature, preprints, and patents, and providing intelligent comparisons to optimize experimental outcomes.
By streamlining the research workflow and improving reproducibility, PubCompare.ai can support advancements in our understanding of these essential cytoskeletal structures and their roles in cellular processes.
Alexa Fluor 488, a fluorescent dye, can also be used to label and visualize microfilaments in various experimental setings.