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VIL2 protein, human

The VIL2 protein, also known as ezrin, is a member of the ezrin-radixin-moesin (ERM) family of proteins.
It plays a key role in the regulation of cell shape, motility, and adhesion by linking the actin cytoskeleton to the plasma membrane.
VIL2 is involved in various cellular processes, such as cell signaling, membrane transport, and the organization of specialized membrane domains.
Researchers can explore a wealth of literature, pre-prints, and patents related to the VIL2 protein using the PubCompare.ai platform, which provides AI-driven insights to optimize research protocols and accelerate discoveries.
PubCompare.ai's powerful comparisons can guide researchers to the best protocols and products for their VIL2 protein research, streamlining their workflow and helping them make breakthroughs more efficiently.

Most cited protocols related to «VIL2 protein, human»

Antibody Characterization for Cellular Localization

Cited 5 times

Other antibodies used in this study were: a mouse monoclonal antibody (mAb) to TGN38 (gift from Dr. G. Banting, University of Bristol, Bristol, UK), mouse mAbs to mannosidase II and GM130 (gifts from Dr. G. Warren, ICRF, London, UK), an mAb to galactosyl transferase (provided by Dr. T. Suganuma, Miyazaki Medical College, Miyazaki, Japan) and rabbit polyclonal antibodies to ezrin (gift from Dr. A. Bretscher, Cornell University, Ithaca, NY).
Affinity-purified antibodies to myr 2 (myosin I from rat brain; Ruppert et al., 1995 (link)) were prepared against expressed GST-fusion protein of the tail domain (cDNA for myr2, provided by Dr. M. Bähler, Ludwig-Maximilians-Universität, Munich, Germany).

Buss F., Kendrick-Jones J., Lionne C., Knight A.E., Côté G.P, & Paul Luzio J. (1998). The Localization of Myosin VI at the Golgi Complex and Leading Edge of Fibroblasts and Its Phosphorylation and Recruitment into Membrane Ruffles of A431 Cells after Growth Factor Stimulation. The Journal of Cell Biology, 143(6), 1535-1545.

Publication 1998

alpha-D-mannosidase II Antibodies Brain DNA, Complementary Galactosyltransferases Gifts Mice, House Monoclonal Antibodies Myosin Type I Protein Domain Rabbits REG1A protein, human Tail VIL2 protein, human

Immunostaining of Retinal Cell Types

Cited 4 times

Wild type (WT) CD1, C57BL/6J, and CX3CR1+/GFP ^{2 (link)} mice were used. All studies adhered to the ARVO Statement for the Use of Animals in Ophthalmic and Vision Research and were approved by the Animal Care and Use Committee of the National Eye Institute. For whole mount pigment bleaching and immunostaining, mouse eyes were enucleated, fixed in 4% paraformaldehyde PBS for 30 minutes to 4 hours, and the anterior segments were removed before or after melanin bleaching. For whole mount staining, primary and secondary antibodies were treated at 4°C for 3 and 2 days, respectively. For 10 μm cryosectioned retina tissues, primary and secondary antibodies were treated at room temperature for 1.5 hours and 30 minutes, respectively. The primary antibodies used were rabbit anti-cone arrestin (CAR; Millipore, Billerica, MA), calbindin (Calbiochem, La Jolla, CA), protein kinase C alpha (PKCα; Sigma-Aldrich, St. Louis, MO), and ionized calcium-binding adapter molecule 1 (Iba-1; Wako, Richmond, VA), chicken anti-S-opsin, and green fluorescent protein (GFP; Millipore), rat anti-CD11b (Serotec, Oxford, England, UK), mouse anti-glutamine synthase (GS; Millipore), and ezrin (Thermo Scientific, Rockford, IL). The relevant secondary antibodies conjugated with Alexa Fluor 488 or 555 (Life Technologies, Carlsbad, CA) were used at a dilution of 1:1000. Bovine serum albumin (1%) and 0.2% or 0.5% Triton X-100 in PBS was used for blocking and antibody treatment. All experiments were repeated separately, at least twice, using multiple retinas.

Kim S.Y, & Assawachananont J. (2016). A New Method to Visualize the Intact Subretina From Retinal Pigment Epithelium to Retinal Tissue in Whole Mount of Pigmented Mouse Eyes. Translational Vision Science & Technology, 5(1), 6.

Publication 2016

alexa fluor 488 Animals Antibodies Arrestin Calbindins Calcium Chickens Eye Glutamate-Ammonia Ligase Immunoglobulins ITGAM protein, human Melanins Mus paraform Pigmentation PRKCA protein, human Protein Kinase C alpha Rabbits Retina Retinal Cone Rod Opsins Serum Albumin, Bovine Technique, Dilution Tissues Triton X-100 VIL2 protein, human Vision

Recombinant Ezrin Fragment Biotinylation

Cited 4 times

LLC-PK1 cells (CCL 101; American Type Culture Collection) were cultured in DME containing 10% FCS and maintained at 37°C in 10% CO₂. Recombinant NH₂-terminal fragment 1–309 of ezrin was produced and purified as a GST fusion as previously described (Gautreau et al. 1999). GST moiety was cleaved off by thrombin digestion. Recombinant NH₂-terminal fragment was biotinylated with NHS-LC-biotin (Pierce Chemical Co.) according to the manufacturer's instructions.

Gautreau A., Louvard D, & Arpin M. (2000). Morphogenic Effects of Ezrin Require a Phosphorylation-Induced Transition from Oligomers to Monomers at the Plasma Membrane. The Journal of Cell Biology, 150(1), 193-204.

Publication 2000

Digestion LLC-PK1 Cells sulfosuccinimidyl 6-(biotinamido)hexanoate Thrombin VIL2 protein, human

Bioluminescent Biosensors for GPCR Signaling

Cited 3 times

Only human GPCRs and human Gα subunits were used in this study. An open reading frame of each full-length GPCR was cloned into pcDNA3.1(+) expression plasmid. Except when otherwise specified, GPCRs sequences were devoid of epitope tags.
Gα_s-67-RlucII (Carr et al., 2014 (link)), Gα_i1-loop-RlucII and GFP10-Gγ₁ (Armando et al., 2014 (link)), Gα_i2-loop-RlucII and βarrestin2-RlucII (Quoyer et al., 2013 (link)), Gα_oB-99-RlucII (Mende et al., 2018 (link)), Gα_q-118-RlucII (Breton et al., 2010 (link)), Gα₁₂-136-RlucII and PKN-RBD-RlucII (Namkung et al., 2018 (link)), Gα₁₃-130-RlucII (Avet et al., 2020 (link)), GFP10-Gγ₂ (Galés et al., 2006 (link)), βarrestin1-RlucII (Zimmerman et al., 2012 (link)), rGFP-CAAX (Namkung et al., 2016 (link)), EPAC (Leduc et al., 2009 (link)), MyrPB-Ezrin-RlucII (Leguay et al., 2021 (link)), HA-β₂AR (Lavoie et al., 2002 (link)), signal peptide-Flag-AT₁ (Goupil et al., 2015 (link)), and EAAC-1 (Brabet et al., 1998 (link)) were previously described. Full-length, untagged Gα subunits, Gβ₁ and Gγ₉ were purchased from cDNA Resource Center. GRK2 was generously provided by Dr. Antonio De Blasi (Istituto Neurologico Mediterraneo Neuromed, Pozzilli, Italy).
To selectively detect G_i/o activation, a construct coding for aa 1–442 of Rap1 GTPase-activating protein (comprising a G_i/o binding domain) fused to Rluc8, was sequence-optimized, synthetized and subcloned at TopGenetech (St-Laurent, QC, Canada). From this construct, a RlucII-tagged version of Rap1GAP (1-442) with a linker sequence (GSAGTGGRAIDIKLPAT) between Rap1GAP and RlucII was created by Gibson assembly in pCDNA3.1_Hygro (+) GFP10-RlucII, replacing GFP10. Three substitutions (i.e. S437A/S439A/S441A) were introduced into the Rap1GAP sequence by PCR-mediated mutagenesis. These putative (S437 and S439) and documented (S441) (McAvoy et al., 2009 (link)) protein kinase A phosphorylation sites were removed in order to eliminate any G_s-mediated Rap1GAP recruitment to the plasma-membrane.
To selectively detect G_q/11 activation, a construct encoding the G_q binding domain of the human p63 Rho guanine nucleotide exchange factor (p63RhoGEF; residues: 295–502) tagged with RlucII was done from IMAGE clones (OpenBiosystems; Burlington, ON, Canada) and subcloned by Gibson assembly in pCDNA3.1_Hygro (+) GFP10-RlucII, replacing GFP10. The G_q binding domain of p63RhoGEF and RlucII were separated by the peptidic linker ASGSAGTGGRAIDIKLPAT. N-term part containing palmitoylation sites maintaining p63 to plasma membrane and part of its DH domain involved in RhoA binding/activation (Aittaleb et al., 2010 (link); Aittaleb et al., 2011 (link)) are absent of the sensor.
To selectively detect G_12/13 activation, a construct encoding the G_12/13 binding domain of the human PDZ-RhoGEF (residues: 281–483) tagged with RlucII was done by PCR amplification from IMAGE clones (OpenBiosystems) and subcloned by Gibson assembly in pCDNA3.1_Hygro (+) GFP10-RlucII, replacing GFP10. The peptidic linker GIRLREALKLPAT is present between RlucII and the G_12/13 binding domain of PDZ-RhoGEF. The sensor is lacking the PDZ domain of PDZ-RhoGEF involved in protein-protein interaction, as well as actin-binding domain and DH/PH domains involved in GEF activity and RhoA activation (Aittaleb et al., 2010 (link)).
The sequence of each EMTA biosensors is provided in the Supplementary file 5.

Avet C., Mancini A., Breton B., Le Gouill C., Hauser A.S., Normand C., Kobayashi H., Gross F., Hogue M., Lukasheva V., St-Onge S., Carrier M., Héroux M., Morissette S., Fauman E.B., Fortin J.P., Schann S., Leroy X., Gloriam D.E, & Bouvier M. (2022). Effector membrane translocation biosensors reveal G protein and βarrestin coupling profiles of 100 therapeutically relevant GPCRs. eLife, 11, e74101.

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Publication 2022

Actins beta-Arrestin 1 beta-Arrestin 2 Biosensors Clone Cells DNA, Complementary Epitopes erythromycin propionate-N-acetylcysteinate GRK2 protein, human GTPase-Activating Proteins Homo sapiens link protein Mutagenesis Palmitoylation Peptides Phosphorylation Phosphotransferases Plasma Membrane Plasmids Pleckstrin Homology Domains Protein Kinases Proteins Protein Subunits RGNEF protein, human RHOA protein, human Rho Guanine Nucleotide Exchange Factor p115 Signal Peptides VIL2 protein, human

Generating Ezrin Fusion Proteins

Cited 3 times

Ezrin-pIRES2-EGFP was constructed by subcloning full-length ezrin (1-586) into the Xho I and EcoR I sites of pIRES2-EGFP vector (Clonetech). The threonine 567 residue in ezrin was mutated to aspartic acid (T567D) using the QuikChange® II Site-Directed mutagenesis kit (Stratagene). In order to generate YFP fusions of Ezrin, the stop codon TAA in Ezrin-pIRES2-EGFP was mutated to GGA (Glycine), and the stop codon-mutated wild type ezrin was subcloned into the Xho I and EcoR I sites of the vector pEYFP-N1 (Clonetech). The T567 site in the resulting fusion construct (Ez-YFP) was mutated to aspartic acid to generate a T567D-YFP fusion protein (TD-YFP). 2PK3 cells were transfected with 3-6 μg of the appropriate plasmids using Amaxa Nucleofector II (Lonza). Stable transfectants were generated by selecting for G418-resistance and sorting for high GFP expression using the Aria I cell sorter (Becton Dickinson).

Parameswaran N., Matsui K, & Gupta N. (2011). Conformational switching in ezrin regulates morphological and cytoskeletal changes required for B cell chemotaxis. Journal of immunology (Baltimore, Md. : 1950), 186(7), 4088-4097.

Publication 2011

antibiotic G 418 Aspartic Acid Cells Cloning Vectors Codon, Terminator Glycine Mutagenesis, Site-Directed NRG1 protein, human Ochre Stop Codon Plasmids Proteins Threonine VIL2 protein, human

Most recents protocols related to «VIL2 protein, human»

Ezrin-Actin Cytoskeleton Reconstitution

Ezrin
T567D was bound to the SLBs at a concentration of 1 μm overnight at 4 °C. Excess protein was removed by a 10-fold
buffer exchange with ezrin buffer and F-actin buffer (50 mM KCl, 20
mM Tris, 2 mM MgCl₂, 0.1 mM NaN₃, pH 7.4). For
F-actin pre-polymerization, ATTO 594-NHS ester (ATTO-TEC, Siegen,
Germany) labeled nonmuscle G-actin and unlabeled monomers (Cytoskeleton,
Denver, CO, USA) were solved in a 1:10 ratio and a final concentration
of 0.44 mg/mL in G-buffer (5 mM Tris, 0.2 mM CaCl₂, 0.1
mM NaN₃, pH 8.0). Actin oligomers were depolymerized by
the addition of dithiothreitol (DTT, 0.5 mM) and adenosine 5′-triphosphate
(ATP, 0.2 mM) for 1 h on ice. Remaining actin aggregates were centrifuged
(17,000 × g, 20 min, 4 °C) and polymerization
was induced by the addition of 10% of the total volume of polymerization
solution (500 mM KCl, 20 mm MgCl₂, 20 mM ATP,
50 mM guanidine carbonate, pH 7.4). After a polymerization time of
20 min at 20 °C, the F-actin solution was mixed with unlabeled
phalloidin in a 1.5% (n/n) ratio
and incubated for another 20 min. Minimal actin networks were formed
at 20 °C by incubating the ezrin T567D-decorated SLBs with polymerized
F-actin at a concentration of 4.6 μM for at least 2 h. Unbound
filaments were washed off by a 10-fold buffer exchange with F-actin
buffer.

Liebe N.L., Mey I., Vuong L., Shikho F., Geil B., Janshoff A, & Steinem C. (2023). Bioinspired Membrane Interfaces: Controlling Actomyosin Architecture and Contractility. ACS Applied Materials & Interfaces, 15(9), 11586-11598.

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Publication 2023

Actins Adenosine Triphosphate Buffers Carbonates Cytoskeleton Dithiothreitol Esters F-Actin G-Actin Guanidine Magnesium Chloride Polymerization Proteins Sodium Azide Tromethamine VIL2 protein, human

Supported Lipid Bilayer Formation

Supported lipid bilayers (SLBs) were
prepared on glass substrates (no. 1.5, Marienfeld-Superio, Lauda-Königshofen,
Germany), used for fluorescence microscopy imaging, and on silicon
wafers coated with 5 μm SiO₂ (Silicon Materials,
Kaufering, Germany), used for reflectometric interference spectroscopy
(RIfS). Both substrates were treated for 20 min with a H₂O/NH₃/H₂O₂ (5:1:1, v/v) solution
at 70 °C and subsequently activated for 30 s with O₂-plasma (Zepto LF PC, Diener electronic, Ebhausen, Germany). The
hydrophilized substrates were mounted in a measuring chamber and immediately
incubated with SUVs.
For the preparations on glass slides, SLBs
were formed by incubating the substrates for 1 h with SUVs (m = 0.2 mg, c = 0.53 mg/mL) at 20 °C
and excess lipid material was removed by a 10-fold buffer exchange
with spreading buffer followed by ezrin buffer (50 mM KCl, 20 mM Tris,
0.1 mM NaN₃, 0.1 mM EDTA, pH 7.4). For SLB formation on
silicon substrates, SUVs (m = 0.2 mg, c = 0.53 mg/mL) were spread while the optical thickness was read out.
After successful SLB formation, excess lipid material was removed
by rinsing 5 min with spreading buffer and 5 min with ezrin buffer.

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Publication 2023

Buffers Edetic Acid Lipid Bilayers Lipids Microscopy, Fluorescence Peroxide, Hydrogen Plasma Rifampin Silicon Sodium Azide Spectrum Analysis Tromethamine VIL2 protein, human Vision

Ezrin T567D Membrane Binding Assay

Ezrin T567D was recombinantly
expressed in E. coli (BL21(DE3)pLysS,
Novagen, Madison, WI, USA) and purified as described previously.^{33 (link)} RIfS was used to measure the formation of SLBs
on the silicon wafers and binding of the protein onto the membranes.
RIfS is a noninvasive label-free technique to determine optical layer
thicknesses (OT = nd). OT values were monitored using
a flame-S-UV/vis spectrometer (Ocean Optics, Dunedin, FL, USA), recording
a spectrum every 2 s and analyzed utilizing a custom MATLAB script
(R2021a, Mathworks). The experimental setup was described previously.^{37 (link)} After SLB formation, the membrane surface was
rinsed with ezrin buffer and a BSA solution (1 mg/mL in ezrin buffer)
for 5 min. After rinsing again with ezrin buffer for 5 min, ezrin
T567D was added (0.8 μM) for 10 min. Unbound protein was removed
by rinsing with ezrin buffer.

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Publication 2023

Binding Proteins Buffers Escherichia coli Eye Proteins Rifampin Silicon Tissue, Membrane VIL2 protein, human Vision

Modulating Periaxin and Ezrin in Peripheral Nerve Injury

Animal studies were performed according to the Guide for the Care and Use of Laboratory Animals published by the US National Institutes of Health and China. The Experimental Animal Centre of Hubei Medical University provided C57BL/6 mice (male, 3–5 months) that met the criteria. The Institutional Animal Care and Use Committee of Hubei Medical University approved the animal protocols (Cat: 2019–111).
For the transduction of adult muscles, C57BL/6 male mice were anesthetized by using an isoflurane vaporizer maintained at 2% isoflurane and 1 L/m oxygen. Gastrocnemius and soleus (SL) muscles were exposed and injected with Ad-Ezrin (1 × 10¹⁰ pfu, two points, 50 μm/each) [15 (link)]. Muscles were removed 7 days after transfection, frozen in isopentane cooled in liquid nitrogen, and stored at − 80 °C.
Mutation and deletion of L-periaxin was associated with Charcot-Marie-Tooth (CMT) characterized by progressive muscle weakness and atrophy of distal extremities with sensory impairment through destroying the myelin sheath formed by Schwann cells. Interestingly, Ezrin inhibits the self-association of L-periaxin and participates in myelin sheath maintenance [4 (link), 5 (link)]. To confirm whether L-periaxin/Ezrin independence and interaction participate in CMT and muscular atrophy, a peroneal nerve injury model was prepared. Briefly, C57BL/6 male mice were anesthetized by using an isoflurane vaporizer maintained at 2% isoflurane and 1 L/m oxygen. Peroneal nerves were exposed and clamped for 15 min; subsequently, the gastrocnemius muscle (GA) was injected with Ad-Ezrin, Ad-Periaxin or Ad-shPeriaxin alone (1 × 10¹⁰ pfu, three points, 50 μm/each), and combined treatment with Ad-Ezrin (1 × 10¹⁰ pfu, three points, 50 μm/each) injection into the GA with Ad-shPeriaxin injection into the GA or Ad-Periaxin incubation within the injured peroneal nerves was incubated with Ad-Periaxin (1 × 10¹⁰ pfu, 50 μm/each) [15 (link)]. The sham and PNI groups within the peroneal nerves and GA were treated with equal amounts of normal saline. Muscles were removed 14 days after transfection, frozen in isopentane cooled in liquid nitrogen, and stored at − 80 °C. The myofiber types were measured through double fluorescence immunostaining of MyHC-I (NOQ, ab234431) and MyHC-II (My32, ab51263). Masson and hematoxylin-eosin staining were performed according to the manufacturer’s instructions. The successful establishment of the peroneal nerve injury model is shown in Additional file 1: Figure S1.

Zhang R.N., Bao X., Liu Y., Wang Y., Li X.Y., Tan G., Mbadhi M.N., Xu W., Yang Q., Yao L.Y., Chen L., Zhao X.Y., Hu C.Q., Zhang J.X., Zheng H.T., Wu Y., Li S., Chen S.J., Chen S.Y., Lv J., Shi L.L, & Tang J.M. (2023). The spatiotemporal matching pattern of Ezrin/Periaxin involved in myoblast differentiation and fusion and Charcot-Marie-Tooth disease-associated muscle atrophy. Journal of Translational Medicine, 21, 173.

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Publication 2023

Adult Animals Animals, Laboratory Atrophy Cardiac Arrest Charcot-Marie-Tooth Disease Combined Modality Therapy Deletion Mutation Eosin Fluorescence Freezing Injuries Institutional Animal Care and Use Committees Isoflurane isopentane Males Mice, Inbred C57BL Muscle, Gastrocnemius Muscle Tissue Muscle Weakness Muscular Atrophy Mutation Myelin Sheath Nitrogen Normal Saline Oxygen periaxin Peroneal Nerve Schwann Cells Soleus Muscle Transfection Vaporizers VIL2 protein, human

Adenoviral Vectors for Myoblast Regulation

Ezrin-, L-periaxin-, and NFATc1/c2-overexpressing adenoviral vectors were prepared as previously described [15 (link)]. The gene accession numbers of overexpressing-Ezrin, L-periaxin, and NFATc1/c2 are NM_172390 and NM_173091, respectively. The adenoviral vectors carrying short hairpin RNA (shRNA) for knockdown of Ezrin, L-periaxin and NFATc3/c4 were prepared as previously described (Hicks et al., 2014). These overexpression adenoviral vectors containing Ad-NFATc1, Ad-NFATc2, Ad-shNFATc3 and Ad-shNFATc4 were obtained from Vigenebio. To confirm the role of L-periaxin in myoblasts, Ad-Null, Ad-Periaxin, or Ad-shPeriaxin (1 × 10⁹ pfu) was added to the corresponding culture dishes one day before Ad-Ezrin or Ad-shEzrin was added. To confirm the role of NFATc3 or NFAtc4 in myoblasts, Ad-Null, Ad-shNFATc3, or Ad-shNFATc4 (1 × 10⁹ pfu) was added to the corresponding culture dish one day before Ad-Ezrin or Ad-shEzrin was added. Then, the proliferation medium was replaced with differentiation medium for further observation. The successful knockdown and overexpression of exogenous genes was measured by detecting the His-tag, Ezrin and L-periaxin (Additional file 1: Figure S2–S3).

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Publication 2023

Adenoviruses Cloning Vectors Genes Hyperostosis, Diffuse Idiopathic Skeletal Myoblasts periaxin Short Hairpin RNA STK35 protein, human transcription factor NF-AT c3 VIL2 protein, human

Top products related to «VIL2 protein, human»

Ezrin by Santa Cruz Biotechnology

Sourced in China, United States

Ezrin is a laboratory equipment product offered by Santa Cruz Biotechnology. Ezrin is a cytoskeletal protein that connects the cell membrane to the actin cytoskeleton. It is involved in the regulation of cell shape, motility, and organization.

Ezrin by Cell Signaling Technology

Sourced in United States

Ezrin is a recombinant protein produced by Cell Signaling Technology. It is a member of the ezrin-radixin-moesin (ERM) family of proteins, which function as linkers between the actin cytoskeleton and the plasma membrane. Ezrin plays a role in cellular processes such as cell adhesion, cell migration, and signal transduction.

Trizol reagent 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.

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Ezrin by Abcam

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Ezrin is a cytoskeletal protein that functions as a linker between the cell membrane and the actin cytoskeleton. It is involved in the regulation of cell shape, motility, and signal transduction.

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GAPDH is a protein that functions as an enzyme involved in the glycolysis process, catalyzing the conversion of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. It is a common reference or housekeeping protein used in various assays and analyses.

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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.

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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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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.

What is the VIL2 protein and what is its role in the human body?

The VIL2 protein, also known as ezrin, is a member of the ezrin-radixin-moesin (ERM) family of proteins. It plays a key role in regulating cell shape, motility, and adhesion by linking the actin cytoskeleton to the plasma membrane. VIL2 is involved in various cellular processes, such as cell signaling, membrane transport, and the organization of specialized membrane domains.

What are some common applications of the VIL2 protein in research?

VIL2 protein is widely studied in areas such as cell biology, cancer research, and immunology. Researchers may use VIL2 as a marker for cell migration and invasiveness, or investigate its role in signaling pathways and membrane dynamics. Understanding the function of VIL2 can provide insights into diseases where cell-cell interactions and cytoskeletal remodeling are disrupted, such as cancer and inflammatory disorders.

Are there different types or variants of the VIL2 protein?

Yes, there are several isoforms of the VIL2 protein that can be expressed in different cell types or under specific conditions. For example, ezrin, radixin, and moesin are the three main ERM family members that share similar structures and functions. Additionally, post-translational modifications, such as phosphorylation, can lead to different conformational states and regulatory mechanisms of the VIL2 protein.

How can PubCompare.ai help with VIL2 protein research?

PubComapre.ai can be a valuable tool for researchers working with the VIL2 protein. The platform allows you to screen protocol literature more efficiently and leverage AI to pinpoit critical insights. PubCompare.ai's AI-driven analysis can help you identify the most effective protocols related to VIL2 protein, human for your specific research goals, highlighting key differences in protocol effectiveness and enabling you to choose the best option for reproducibility and accuaracy. This can streamline your workflow and accelerate your discoveries.

More about "VIL2 protein, human"

The VIL2 protein, also known as ezrin, is a crucial member of the ezrin-radixin-moesin (ERM) family.
This versatile protein plays a pivotal role in regulating cell shape, motility, and adhesion by acting as a linker between the actin cytoskeleton and the plasma membrane.
VIL2/ezrin is involved in a myriad of cellular processes, including cell signaling, membrane transport, and the organization of specialized membrane domains.
Researchers can delve into a wealth of literature, pre-prints, and patents related to the VIL2 protein using the innovative PubCompare.ai platform.
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Leveraging the power of artificial intelligence, PubCompare.ai can help researchers navigate the vast landscape of VIL2 protein-related information, streamlining their workflow and guiding them to the best protocols and products for their specific research needs.
In addition to the VIL2 protein, researchers may encounter other important molecules and techniques in their studies, such as ezrin, TRIzol reagent, Lipofectamine 2000, Bovine serum albumin (BSA), GAPDH, RNeasy Mini Kit, and DAPI.
These tools and reagents can play crucial roles in various aspects of VIL2 protein research, from RNA extraction and cell culture to Western blotting and immunofluorescence.
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