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> Chemicals & Drugs > Amino Acid > Fascin

Fascin

Fascins are a family of actin-bundling proteins that play crucial roles in organizing cytoskeletal structures and cell motility.
They are involved in the formation of filopodia, microspikes, and other cellular protrusions.
Fascins crosslink actin filaments into parralel bundles, contributing to the stability and dynamics of these structures.
Upregulation of fascin expression has been linked to increased tumor cell invasion and metastasis in various cancers.
Understanding the functional mechanisms of fascins is an active area of research, with potential implications for cancer diagnostics and therapeutuics.
The PubCompare.ai platform can help researchers identify the most reliable and effective methods for studying fascin and its role in cellular processes and disease.

Most cited protocols related to «Fascin»

1
Constructing mNeonGreen Fusion Protein Vectors
Cited 67 times
mNeonGreen fluorescent protein expression vectors were constructed using C1 and N1 (Clontech-style) cloning vectors. The mNeonGreen cDNA was amplified with a 5′ primer encoding an AgeI site and a 3′ primer encoding either a BspEI (C1) or NotI (N1) site for generating cloning vectors to create C-terminal and N-terminal fusions (with regards to the FP), respectively. Purified and digested PCR products were ligated into similarly digested EGFP-C1 and EGFP-N1 cloning vector backbones. To obtain targeting fusion vectors, the appropriate cloning vector and a previously assembled EGFP or mEmerald fusion vector were digested, either sequentially or doubly, with the appropriate enzymes and ligated together after gel purification.
Thus, to prepare mNeonGreen C-terminal fusions (number of linker amino acids in parenthesis), the following digests were performed: annexin A4 (12), NheI and BspEI (Alen Piljic, EMBL, Heidelberg, Germany; NM_001153.3); β-actin (7), NheI and BglII (human β-actin cDNA source: Clontech; NM_001101.3); β-catenin (20), XhoI and BamHI (mouse β-catenin cDNA source: Origene, Rockville, MD; NM_001165902.1); 20 amino acid farnesylation signal from c-Ha-Ras (CAAX; 5), AgeI and BspEI (c-Ha-Ras cDNA source: Clontech; NM_001130442.1); CAF1 (10), AgeI and BspEI (mouse chromatin assembly factor cDNA source: Akash Gunjan, Florida State University; NM_013733.3); caveolin 1 (10), NheI and BglII (human caveolin 1 cDNA source: Origene; NM_001753); endosomes (14), NheI and BspEI (endosomes cDNA source: Clontech; NM_004040.2); fascin (10), BspEI and BamHI (human fascin cDNA source: Origene; NM_003088.2); fibrillarin (7), AgeI and BspEI (fibrillarin cDNA source: Evrogen, Moscow, Russia; NM_001436.3); filamin A (14), BspEI and HindIII (human filamin cDNA source: David Calderwood, Yale University; NM_001456.3); human lysosomal membrane glycoprotein 1 (20), BamHI and NotI (LAMP1; George Patterson, NIH, Bethesda MD, U.S.A.; NM_012857.1); human light chain clathrin (15), NheI and BglII (human clathrin light chain cDNA source: George Patterson, NIH; NM_001834.2); human myotilin, AgeI and BspEI (MYOT; Origene; NM_006790.1); PCNA (19), AgeI and BspEI (proliferating cell nuclear antigen cDNA source: David Gilbert, FSU; NM_002592.2); plastin (10), BspEI and XhoI (human plastin 1 (fimbrin) cDNA source: Origene; NM_002670.1); canine Rab4a, BglII and BamHI (Rab4a cDNA source: Viki Allen, U. Manchester, UK; NM_004578.2); LC3B (7), AgeI and BspEI (rat LC3B cDNA source: Jenny M. Tam, Harvard University; U05784.1); talin (22) AgeI and BspEI (mouse talin 1 cDNA source: Clare Waterman, NIH; NM_011602.5); α-tubulin (18), NheI and BglII (human α-tubulin cDNA source: Clontech; NM_006082).
To prepare mNeonGreen N-terminal fusions (number of linker amino acids in parenthesis), the following digests were performed: human non-muscle α-actinin, EcoRI and NotI (cDNA source, Tom Keller, Florida State University (FSU), Tallahassee, FL, U.S.A.; NM_001130005.1); human calnexin, AgeI and NotI (Origene; NM_001746.3); c-src (7), BamHI and EcoRI (chicken c-src cDNA source: Marilyn Resh, Sloan-Kettering, New York; XM_001232484.1); connexin-43 (7), BamHI and NotI (rat C×43 cDNA source: Matthias Falk, Lehigh U; NM_001004099.1); EB3 (7), BglII and BamHI (EB3 cDNA source: Lynne Cassimeris, Lehigh University; NM_012326.2); human keratin 18, EcoRI and NotI (Open Biosystems; NM_199187.1); lamin B1 (10), EcoRI and BamHI (human lamin B1 cDNA source: George Patterson, NIH; NM_005573.2); Lifeact (7), BamHI and NotI (Lifeact cDNA source: IDT); mouse mannosidase 2 (112 N-terminal amino acids, MANNII; 10), NheI and BamHI (cDNA source: Jennifer Lippincott-Schwartz, NIH; NM_008549.2); myosin IIA (14) NheI and BglII (mouse myosin IIA cDNA source: Origene; NM_022410.2); human nucleoporin 50kDa, BamHI and NotI (NUP50 cDNA source: Origene; NM_007172.2); human pyruvate dehydrogenase, AgeI and NotI (human PDHA1 cDNA source: Origene; NM_000284); human peroxisomal membrane protein, NotI and AgeI (PMP cDNA source: Origene; NM_018663.1); human MAP Tau (10), AgeI and NotI (MAP Tau cDNA source: Origene; NM_016841); human TfR (20), BamHI and NotI (transferrin receptor cDNA source: George Patterson, NIH; NM_NM_003234); human TPX2 (10), AgeI and NotI (TPX2 cDNA source: Patricia Wadsworth, University of Massachusetts, Amherst; NM_012112.4); mouse VASP (10), NheI and BamHI (cDNA source: Clare Waterman, NIH; NM_009499); vascular epithelial cadherin (10), AgeI and NotI (human VE cadherin cDNA source: Origene; NM_001795.3), vimentin (7), BamHI and NotI (human vimentin cDNA source: Robert Goldman, Northwestern University; NM_003380.3), zyxin (6), BamHI and NotI (human zyxin cDNA source: Origene; NM_003461). All DNA for transfection was prepared using the Plasmid Maxi kit (QIAGEN). To ensure proper localization, mNeonGreen fusion proteins were characterized by transfection in HeLa (S3 or CCL2 line) or MDCK cells (ATCC) using Effectene (QIAGEN) and ∼1 μg vector. Transfected cells were grown on coverslips in DMEM/F12, fixed after 48 hours, and mounted with Gelvatol. Epifluorescence images were captured with a Nikon 80i microscope using widefield illumination and a Chroma FITC filter set to confirm proper localization.
Shaner N.C., Lambert G.G., Chammas A., Ni Y., Cranfill P.J., Baird M.A., Sell B.R., Allen J.R., Day R.N., Israelsson M., Davidson M.W, & Wang J. (2013). A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum. Nature methods, 10(5), 407-409.
Publication 2013
2
Mical Regulates Actin and Microtubule Dynamics
Cited 34 times
We performed complementation analysis, genetics, molecular biology, western blotting, immunostaining and generation of transgenic animals using standard techniques4 (link). Multiple new lines of the full-length ‘short’ isoform of Mical, the MicalΔredox mutation (MicalG→W; ref. 4 (link)) and the other transgenic animals were generated and used for all experiments. Adult bristles were examined and quantified by crossing adults at 25 °C: adult offspring from these crosses were first sorted according to genotype and then examined under a dissecting microscope. We genotyped pupae using a Zeiss Discovery M2 Bio fluorescence stereomicroscope, and all preparation, staging and dissection of pupae were done using standard approaches. We imaged, drew and quantified the adult bristles with the aid of the Discovery M2 Bio stereomicroscope, a motorized focus and zoom, a Zeiss AxioCam HR camera and three-dimensional-reconstruction software (Zeiss AxioVision, version 4.6.3, and Extended Focus software). All other bright-field, dark-field, differential interference contrast and fluorescence visualization, and imaging of bristles, embryos and growth cones, was done using a Zeiss Axio Imager upright microscope with motorized focus and zoom and an ApoTome module, and images were captured and quantified using the AxioCam HR camera and AxioVision software. All electron microscopy of pupae and negative staining of purified proteins was done using a FEI Tecnai G2 Spirit BioTWIN transmission electron microscope. We purified recombinant Mical proteins10 and recombinant p-hydroxybenzoate hydroxylase using our previously developed approaches. Drosophila fascin (also known as singed) complementary DNA was inserted in a bacterial expression vector, and recombinant Drosophila fascin protein was purified. All F-actin and Mical co-sedimentation assays and G-actin/F-actin ratio experiments were performed using standard approaches, as were all pyrene-labelled actin polymerization and depolymerization assays, actin bundling assays, tubulin polymerization assays and microtubule co-sedimentation assays.
Hung R.J., Yazdani U., Yoon J., Wu H., Yang T., Gupta N., Huang Z., van Berkel W.J, & Terman J.R. (2010). Mical links semaphorins to F-actin disassembly. Nature, 463(7282), 823-827.
Publication 2010
Actins Adult Animals, Transgenic Bacteria Biological Assay Cloning Vectors Dissection DNA, Complementary Drosophila Electron Microscopy Embryo F-Actin fascin Fluorescence G-Actin Growth Cones Hydroxybenzoates Microscopy Microtubules Mixed Function Oxygenases Mutation Polymerization Protein Isoforms Proteins Pupa Pyrenes Reconstructive Surgical Procedures Sn protein, Drosophila Transmission Electron Microscopy Tubulin
3
Drosophila Fertility Rescue Assay
Cited 11 times
We used the following lines obtained from the Bloomington Drosophila Stock Center and the community: sn28, DfsnC128, upstream activation sequence (UAS)-GFP-Moesin (Dutta et al., 2002 (link)), UAS-mCherry-Moesin (Millard and Martin, 2008 (link)), UAS-GFP-fascin (Zanet et al., 2009 (link)), and nanos-Gal4VP16. The percentage of the rescue of fertility was calculated by counting the number of pupae generated by one female sn28/sn28 expressing the different GFP-fascin transgenes in nurse cells under the nanos-Gal4 driver in comparison with a wild-type fly.
Zanet J., Jayo A., Plaza S., Millard T., Parsons M, & Stramer B. (2012). Fascin promotes filopodia formation independent of its role in actin bundling. The Journal of Cell Biology, 197(4), 477-486.
Publication 2012
Cells Drosophila fascin Females Fertility MSN protein, human Nurses Pupa Transgenes
4
Immunohistochemical Staining of Paraffin Sections
Cited 10 times
Immunohistochemical analysis staining of paraffin‐embedded tissue sections was carried out using the Dako Envision System (Dako, Glostrup, Denmark) following the manufacturer's protocols. Briefly, the sections were submerged in boiling 10 mmol/L sodium citrate (pH, 6.0) for 2 min in a pressure cooker. After being treated with 0.3% hydrogen peroxide for 10 min to block endogenous peroxidase, the sections were incubated with primary antibody for 1 h at room temperature. After washing, the sections were incubated with biotin‐labeled secondary immunoglobulin (Dako) for 40 min at room temperature, followed by incubation with 3,3′‐diaminobenzidine (Dako), also at room temperature. The primary antibodies used were anti‐fascin‐1 mouse monoclonal antibody (clone 55k‐2; diluted at 1:100; Santa Cruz Biotechnology, Santa Cruz, CA), ready‐to‐use anti‐ER rabbit monoclonal antibody (clone SP1, Dako), ready‐to‐use anti‐PR mouse monoclonal antibody (clone PgR636, Dako), HercepTest (Dako), and ready‐to‐use anti‐Ki‐67 mouse monoclonal antibody (clone MIB‐1, Dako).
Wang C., Tang C., Chang H., Li X., Zhao Y., Su C., Hu G., Zhang T., Sun X., Zeng Y., Du Z., Wang Y, & Huang B. (2016). Fascin‐1 as a novel diagnostic marker of triple‐negative breast cancer. Cancer Medicine, 5(8), 1983-1988.
Publication 2016
Antibodies Antibodies, Anti-Idiotypic Biotin Cardiac Arrest Clone Cells fascin Immunoglobulins Ki-67 Antigen Monoclonal Antibodies Mus Paraffin Embedding Peroxidase Peroxide, Hydrogen Pressure Rabbits Sodium Citrate Tissues
5
Affinity Purification of Biotinylated Proteins
Cited 9 times
4T1 tumor cells were lysed and the cell extract was then mixed with biotin-labeled macroketone or free biotin for 2 hours at 4°C with gentle rotation. Recombinant streptavidin-agarose beads (Pierce, IL) were added to the cell extract and the incubation was continued for another 2 hours with gentle rotation. The mixtures were then loaded onto the Poly-Prep chromatography column. After extensive wash with cell lysis buffer, samples were eluted by elution buffer. The elute was further concentrated by Centricon P-20 (Millipore, MA) and separated by SDS-PAGE. The gel was stained by Coomassie Blue and the indicated band was cut out for mass spectrometry and peptide sequencing analyses.
Chen L., Yang S., Jakoncic J., Zhang J.J, & Huang X.Y. (2010). Migrastatin Analogues Target Fascin to Block Tumor Metastasis. Nature, 464(7291), 1062-1066.
Publication 2010
Biotin biotin 2 Buffers Cell Extracts Cells Chromatography Coomassie blue Mass Spectrometry Neoplasms Poly A SDS-PAGE Sequence Analysis, Protein streptavidin-agarose

Most recents protocols related to «Fascin»

1
Quantifying Fascin Expression in Cancer
Not available on PMC !

Example 3

The levels of fascin mRNA and protein can be determined by real-time PCR and Western blot, respectively. For quantitative real-time PCR, samples from cancer patients were used for RNA isolation. Oligonucleotide primers specific for fascin mRNA were used for PCR reactions. For Western blots, samples from cancer patients were assessed with anti-fascin antibody. The intensity of the bands representing fascin proteins was quantified by image documentation and quantification software.

US11866440B2. Methods for inhibiting fascin (2024-01-09). NOVITA PHARMACEUTICALS, INC. [US], CORNELL UNIVERSITY [US]. Inventors: Xin-Yun Huang [US], Christy Young Shue [US].
Patent 2024
Antibodies, Anti-Idiotypic fascin isolation Malignant Neoplasms Oligonucleotide Primers Patients Proteins Real-Time Polymerase Chain Reaction RNA, Messenger Western Blot Western Blotting
2
Quantifying Fascin mRNA and Protein
Not available on PMC !

Example 3

The levels of fascin mRNA and protein can be determined by real-time PCR and Western blot, respectively. For quantitative real-time PCR, samples from cancer patients were used for RNA isolation. Oligonucleotide primers specific for fascin mRNA were used for PCR reactions. For Western blots, samples from cancer patients were assessed with anti-fascin antibody. The intensity of the bands representing fascin proteins was quantified by image documentation and quantification software.

US11858929B2. Compounds and methods for inhibiting fascin (2024-01-02). NOVITA PHARMACEUTICALS, INC. [US], CORNELL UNIVERSITY [US]. Inventors: Xin-Yun Huang [US], Christy Young Shue [US].
Patent 2024
Antibodies, Anti-Idiotypic fascin isolation Malignant Neoplasms Oligonucleotide Primers Patients Proteins Real-Time Polymerase Chain Reaction RNA, Messenger Western Blot Western Blotting
3
High-Throughput Assay for Fascin Inhibitors
Not available on PMC !

Example 1

A high throughput assay was developed to screen for fascin specific inhibitors. Purified polymerized F-actin with or without fascin were mixed and incubated to allow actin bundle formation. F-actin polymers were then bound to the poly-D-lysine coated plates. After extensive washes, F-actin polymers were visualized by labeling them with Alexa Fluor 488 phalloidin. Four images were taken from each well and the average fiber length was analyzed for each tested compound. In the presence of fascin, actin fibers were longer and thicker as shown below. 30 μM of 2-chloro-N-(6-chlorobenzo[d]thiazol-2-yl)-5-nitrobenzenesulfonamide (Compound 3) inhibited fiber growth.

Average fiber lengthAverage fiber thickness
(arbitrary unit)(arbitrary unit)
Actin0.360.32
Actin + Fascin1.570.53
Actin + Fascin +0.390.35
Compound 3 (30 μM)

From the primary screens of ˜150,000 small molecule compounds, ˜700 compounds were identified that resulted in shorter and thinner actin bundles when compared with those without the small molecule compounds.

The images from screens with these ˜700 compounds were individually examined to insure that they looked like those of actin alone controls. After 2nd and 3rd confirmative screens, in which both muscle and non-muscle actin proteins were tested, 145 small-molecule compounds were confirmed to inhibit the actin-bundling function of fascin. The dose-response curves of these 145 compounds were established.

US11866440B2. Methods for inhibiting fascin (2024-01-09). NOVITA PHARMACEUTICALS, INC. [US], CORNELL UNIVERSITY [US]. Inventors: Xin-Yun Huang [US], Christy Young Shue [US].
Patent 2024
4
Recombinant Fascin 1 Protein Expression
Not available on PMC !

Example 2

Recombinant human fascin 1 was expressed as a GST fusion protein in BL21 Escherichia coli. One liter of 2YT medium with ampicillin was inoculated overnight with 3 mL of BL21/DE3 culture transformed with pGEX4T-fascin 1 plasmid and grown at 37° C. until attenuance at 600 nm (D600) reached about 0.8. The culture was then transferred to 18° C. and induced by the addition of 0.1 mM isopropyl β-d-thiogalactoside (IPTG) for 12 h. Bacteria were harvested by centrifugation at 5,000 r.p.m. for 10 min. The pellets were suspended in 30 mL of PBS supplemented with 0.2 mM PMSF, 1 mM DTT, 1% (v/v) Triton X-100 and 1 mM EDTA. After sonication, the suspension was centrifuged at 15,000 r.p.m. for 30 min to remove the cell debris. The supernatant was then incubated for 2 h with 4 mL of glutathione beads (Sigma) at 4° C. After extensive washing with PBS, the beads were resuspended in 10 mL of thrombin cleavage buffer (20 mM Tris-HCl pH 8.0, 150 mM NaCl, 2 mM CaCl2, 1 mM DTT). Fascin was released from the beads by incubation overnight with 40-100 U of thrombin at 4° C. After centrifugation, 0.2 mM PMSF was added to the supernatant to inactivate the remnant thrombin activity. The fascin protein was further concentrated with a Centricon® (Boca Raton, FL) filter to about 50 mg/mL.

US11866440B2. Methods for inhibiting fascin (2024-01-09). NOVITA PHARMACEUTICALS, INC. [US], CORNELL UNIVERSITY [US]. Inventors: Xin-Yun Huang [US], Christy Young Shue [US].
Patent 2024
Ampicillin Bacteria Brown Oculocutaneous Albinism Buffers Cells Centrifugation Cytokinesis D-600 Edetic Acid Escherichia coli fascin Glutathione Homo sapiens Isopropyl Thiogalactoside Pellets, Drug Plasmids Proteins Sodium Chloride Staphylococcal Protein A Thrombin Triton X-100 Tromethamine
5
Recombinant Human Fascin 1 Purification
Not available on PMC !

Example 2

Recombinant human fascin 1 was expressed as a GST fusion protein in BL21 Escherichia coli. One liter of 2YT medium with ampicillin was inoculated overnight with 3 mL of BL21/DE3 culture transformed with pGEX4T-fascin 1 plasmid and grown at 37° C. until attenuance at 600 nm (D600) reached about 0.8. The culture was then transferred to 18° C. and induced by the addition of 0.1 mM isopropyl β-d-thiogalactoside (IPTG) for 12 h. Bacteria were harvested by centrifugation at 5,000 r.p.m. for 10 min. The pellets were suspended in 30 mL of PBS supplemented with 0.2 mM PMSF, 1 mM DTT, 1% (v/v) Triton X-100 and 1 mM EDTA. After sonication, the suspension was centrifuged at 15,000 r.p.m. for 30 min to remove the cell debris. The supernatant was then incubated for 2 h with 4 mL of glutathione beads (Sigma) at 4° C. After extensive washing with PBS, the beads were resuspended in 10 mL of thrombin cleavage buffer (20 mM Tris-HCl pH 8.0, 150 mM NaCl, 2 mM CaCl2), 1 mM DTT). Fascin was released from the beads by incubation overnight with 40-100 U of thrombin at 4° C. After centrifugation, 0.2 mM PMSF was added to the supernatant to inactivate the remnant thrombin activity. The fascin protein was further concentrated with a Centricon® (Boca Raton, FL) filter to about 50 mg/mL.

US11858929B2. Compounds and methods for inhibiting fascin (2024-01-02). NOVITA PHARMACEUTICALS, INC. [US], CORNELL UNIVERSITY [US]. Inventors: Xin-Yun Huang [US], Christy Young Shue [US].
Patent 2024
Ampicillin Bacteria Brown Oculocutaneous Albinism Buffers Cells Centrifugation Cytokinesis D-600 Edetic Acid Escherichia coli fascin Glutathione Homo sapiens Isopropyl Thiogalactoside Pellets, Drug Plasmids Proteins Sodium Chloride Staphylococcal Protein A Thrombin Triton X-100 Tromethamine

Top products related to «Fascin»

1
Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
2
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
3
Trizol reagent by Thermo Fisher Scientific
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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
4
Fascin by Santa Cruz Biotechnology
Sourced in United States
Fascin is a cytoskeletal protein that plays a role in the organization and dynamics of actin filaments. It is involved in the formation of parallel actin bundles, which are important for cell migration, adhesion, and signaling. Fascin is expressed in various cell types, including neurons, dendritic cells, and cancer cells.
5
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Lipofectamine 3000 is a transfection reagent used for the efficient delivery of nucleic acids, such as plasmid DNA, siRNA, and mRNA, into a variety of mammalian cell types. It facilitates the entry of these molecules into the cells, enabling their expression or silencing.
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Glutathione beads by Merck Group
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Glutathione beads are a type of affinity chromatography resin used for the purification of glutathione-S-transferase (GST)-tagged proteins. They consist of glutathione, a tripeptide, immobilized on agarose or sepharose beads. Glutathione beads selectively bind to GST-tagged proteins, allowing their separation from other components in a sample.
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Matrigel is a solubilized basement membrane preparation extracted from the Engelbreth-Holm-Swarm (EHS) mouse sarcoma, a tumor rich in extracellular matrix proteins. It is widely used as a substrate for the in vitro cultivation of cells, particularly those that require a more physiologically relevant microenvironment for growth and differentiation.
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L glutamine by Thermo Fisher Scientific
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L-glutamine is an amino acid that is commonly used as a dietary supplement and in cell culture media. It serves as a source of nitrogen and supports cellular growth and metabolism.
9
Plenti cmv blasticidin vector by Addgene
The PLenti.CMV.blasticidin vector is a lentiviral expression vector that allows for the stable integration and expression of a gene of interest in target cells. It contains the Cytomegalovirus (CMV) promoter to drive expression and the blasticidin resistance gene for selection of transduced cells.
10
Penicillin streptomycin by Thermo Fisher Scientific
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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.

More about "Fascin"

Fascins are a family of actin-binding and actin-bundling proteins that play crucial roles in organizing cytoskeletal structures and cell motility.
These proteins are involved in the formation of cellular protrusions like filopodia and microspikes, which contribute to the stability and dynamics of these structures.
Fascins crosslink actin filaments into parallel bundles, enabling the reorganization of the cytoskeleton and facilitating processes like cell migration and invasion.
The upregulation of fascin expression has been linked to increased tumor cell invasion and metastasis in various cancers, making it an important area of research for cancer diagnostics and therapeutics.
Understanding the functional mechanisms of fascins is an active area of investigation, with researchers utilizing a variety of techniques and tools to study these proteins.
Commonly used methods in fascin research include transfection with Lipofectamine 2000 or Lipofectamine 3000 to modulate fascin expression, cell culture with FBS and L-glutamine supplementation, and RNA extraction using TRIzol reagent.
Downstream analyses may involve pulldown assays with Glutathione beads, Western blotting, and assays of cell migration and invasion using Matrigel-coated chambers.
The PubCompare.ai platform can enhance research on fascins by helping researchers identify the most reliable and effective methods from the literature, preprints, and patents.
By comparing protocols and identifying the best approaches, researchers can streamline their workflows, improve reproducibility, and gain greater confidence in their findings.
This can ultimately lead to a better understanding of the role of fascins in cellular processes and disease, with potential implications for developing novel diagnostic and therapeutic strategies.