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Integrin alphaV

Integrin alphav is a cell surface receptor that plays a crucial role in cell-cell and cell-extracellular matrix interactions.
It is involved in a variety of biological processes, such as cell adhesion, migration, proliferation, and differentiation.
Integrin alphav can bind to several ligands, including fibronectin, vitronectin, and osteopontin, and is implicated in the pathogenesis of diseases such as cancer, fibrosis, and inflammation.
Researchers can leverage PubCompare.ai's AI-driven platform to optimize their Integrin alphav research protocols, accessing a wealth of literature, pre-prints, and patents, and leveraging intelligent comparisons to identify the most effective protocols and products.
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Most cited protocols related to «Integrin alphaV»

1
Integrin Antibody Characterization
Cited 8 times
The antibodies used were the mouse anti-human integrin β1 antibodies TS2/16 (activating; a gift from Francisco Sanchez-Madrid, Universidad Autonoma de Madrid, Spain), 12G10 (activating) (Mould et al., 1995b (link)), and K20 (nonfunction-modulating, Immunotech); rat anti-human integrin β1 antibodies mAb13 (inhibitory) (Akiyama et al., 1989 (link)) and 9EG7 (activating, Pharmingen); rat anti-human integrin α5 mAb16 (inhibitory) (Akiyama et al., 1989 (link)) and mAb11 (nonfunction-modulating) (Miyamoto et al., 1995 (link)); mouse anti-human integrin α5 antibodies SNAKA52 (inhibitory) and JBS5 (inhibitory, Serotec); mouse anti-human integrin αV L230 (inhibitory, ATCC); and polyclonal rabbit anti-human fibronectin Rb745 (Cukierman et al., 2001 (link)).
Clark K., Pankov R., Travis M.A., Askari J.A., Mould A.P., Craig S.E., Newham P., Yamada K.M, & Humphries M.J. (2004). A Specific α5β1 Integrin Conformation Promotes Directional Integrin Translocation and Fibronectin Matrix Formation. Journal of cell science, 118(Pt 2), 291-300.
Publication 2004
Anti-Antibodies Antibodies FN1 protein, human Fungus, Filamentous Homo sapiens Integrin alphaV Integrins Mus Psychological Inhibition Rabbits
2
Immunohistochemical Analysis of Liver Fibrosis
Cited 6 times
Paraffin-embedded sections were processed for immunohistochemistry as described previously47 (link). The following primary antibodies were used for immunohistochemistry: αSMA A5228, 1:1000 (Sigma), GR1 MAB1037, 1:750 (R&D); F4/80 Ab6640, 1:100 (Abcam), CD31 sc1506, 1:80 (Santa Cruz Biotechnology), and αvβ6 mAb, 1:25 (human/mouse chimeric 2A1, a kind gift from Dr S. Violette, Biogen Idec, Cambridge, MA). 5 μM sections were stained with picrosirius red or antibody and results quantified using Nikon Elements software. Six random fields from each section were analyzed at a final magnification of 40×. For neutrophil counting, twenty random portal tracts per mouse liver were assessed. For immunofluoresence staining, liver tissue was fixed in 4% paraformaldehyde overnight at 4 °C, immersed in graded sucrose solutions, embedded in OCT (Tissue Tek) and stored at −80 °C. Frozen sections were incubated with the following antibodies: F4/80 MCA497R, 1:100; CD3 MCA500GT, 1:200 (Serotec), CD31 550274, 1:50 (BD Pharmingen), αSMA A5228, 1:200 (Sigma), PDGFRβ, 1:200 (a kind gift from Dr W. Stallcup, Sanford-Burnham Medical Research Institute, La Jolla), phospho-SMAD3 1880-1, 1:100 (Epitomics), cytokeratin WSS Z0622, 1:100 (Dako), αv integrin ab76609, 1:60; desmin ab8592, 1:250 (Abcam) and Alexa Fluor 488-conjugated and Alexa Fluor 555-conjugated secondary antibodies (Invitrogen). Confocal imaging was performed on a Zeiss LSM5 Pascal microscope. Digital morphometric measurements of P-SMAD3 were performed using Image J. Twelve random fields of areas of scar from each section were analyzed at a final magnification of 400×. Digital morphometric measurements of desmin and PDGFRβ immunostaining were performed using Image J. Eight random fields from each section were analyzed at a final magnification of 100×.
Henderson N.C., Arnold T.D., Katamura Y., Giacomini M.M., Rodriguez J.D., McCarty J.H., Pellicoro A., Raschperger E., Betsholtz C., Ruminski P.G., Griggs D.W., Prinsen M.J., Maher J.J., Iredale J.P., Lacy-Hulbert A., Adams R.H, & Sheppard D. (2013). Selective αv integrin depletion identifies a core, targetable molecular pathway that regulates fibrosis across solid organs. Nature medicine, 19(12), 10.1038/nm.3282.
Publication 2013
ACTA2 protein, human alexa fluor 488 Alexa Fluor 555 Antibodies Chimera Cicatrix Cytokeratin Desmin Fingers Frozen Sections Homo sapiens Immunoglobulins Immunohistochemistry Integrin alphaV Liver Mice, House Microscopy Neutrophil Paraffin paraform Platelet-Derived Growth Factor beta Receptor Portal System SMAD3 protein, human Sucrose Tissues
3
Immunohistochemical Analysis of Liver Fibrosis
Cited 6 times
Paraffin-embedded sections were processed for immunohistochemistry as described previously47 (link). The following primary antibodies were used for immunohistochemistry: αSMA A5228, 1:1000 (Sigma), GR1 MAB1037, 1:750 (R&D); F4/80 Ab6640, 1:100 (Abcam), CD31 sc1506, 1:80 (Santa Cruz Biotechnology), and αvβ6 mAb, 1:25 (human/mouse chimeric 2A1, a kind gift from Dr S. Violette, Biogen Idec, Cambridge, MA). 5 μM sections were stained with picrosirius red or antibody and results quantified using Nikon Elements software. Six random fields from each section were analyzed at a final magnification of 40×. For neutrophil counting, twenty random portal tracts per mouse liver were assessed. For immunofluoresence staining, liver tissue was fixed in 4% paraformaldehyde overnight at 4 °C, immersed in graded sucrose solutions, embedded in OCT (Tissue Tek) and stored at −80 °C. Frozen sections were incubated with the following antibodies: F4/80 MCA497R, 1:100; CD3 MCA500GT, 1:200 (Serotec), CD31 550274, 1:50 (BD Pharmingen), αSMA A5228, 1:200 (Sigma), PDGFRβ, 1:200 (a kind gift from Dr W. Stallcup, Sanford-Burnham Medical Research Institute, La Jolla), phospho-SMAD3 1880-1, 1:100 (Epitomics), cytokeratin WSS Z0622, 1:100 (Dako), αv integrin ab76609, 1:60; desmin ab8592, 1:250 (Abcam) and Alexa Fluor 488-conjugated and Alexa Fluor 555-conjugated secondary antibodies (Invitrogen). Confocal imaging was performed on a Zeiss LSM5 Pascal microscope. Digital morphometric measurements of P-SMAD3 were performed using Image J. Twelve random fields of areas of scar from each section were analyzed at a final magnification of 400×. Digital morphometric measurements of desmin and PDGFRβ immunostaining were performed using Image J. Eight random fields from each section were analyzed at a final magnification of 100×.
Henderson N.C., Arnold T.D., Katamura Y., Giacomini M.M., Rodriguez J.D., McCarty J.H., Pellicoro A., Raschperger E., Betsholtz C., Ruminski P.G., Griggs D.W., Prinsen M.J., Maher J.J., Iredale J.P., Lacy-Hulbert A., Adams R.H, & Sheppard D. (2013). Selective αv integrin depletion identifies a core, targetable molecular pathway that regulates fibrosis across solid organs. Nature medicine, 19(12), 10.1038/nm.3282.
Publication 2013
ACTA2 protein, human alexa fluor 488 Alexa Fluor 555 Antibodies Chimera Cicatrix Cytokeratin Desmin Fingers Frozen Sections Homo sapiens Immunoglobulins Immunohistochemistry Integrin alphaV Liver Mice, House Microscopy Neutrophil Paraffin paraform Platelet-Derived Growth Factor beta Receptor Portal System SMAD3 protein, human Sucrose Tissues
4
Isolation and Characterization of Skeletal Progenitors
Cited 5 times
C57/BL6 CD45.1/2 congenic mouse strains were derived and maintained in our laboratory. Timed embryos from GFP transgenic HZ mice were used in the majority of the fetal bone (fb) transplantation studies. Sl/+ mice were purchased from Jackson laboratory.
Skeletal progenitors were isolated from fb (humerus, radius, tibia, femur, and pelvis, mandible without the condyle, and the individual frontal and parietal bones by collagenase digestion. They were next stained with antibodies against CD45, Tie2, αV integrin, CD105 and Thy1.1 for fractionation by FACS. Sorted and unsorted skeletal progenitors were then injected underneath the renal capsule of 8-12 week old anesthetized mice.
SLF and osterix specific shRNA knockdown constructs, active lentiviral stock, and non-silencing shRNA constructs were generated as previously described (ref 29 ; supplementary table 1). Fb cell suspensions were transduced for 48hrs with specific shRNA vectors or control, sorted for GFP expression and transplanted as described.
To assess HSC engraftment in ectopic niches, grafted regions were dissected from kidney and crushed by mortar and pestle. Dissociated cells were stained with fluorochrome-conjugated antibodies against CD45, lineage (CD3, CD4, CD5, CD8, B220, Gr-1, Mac-1 and Ter119), c-Kit, Sca-1, and CD150 for FACS analysis. Sorted KLS, CD150+ LT-HSC were transplanted into lethally irradiated (800 rads delivered in split dose) by intravenous injection for functional analysis. Peripheral blood was obtained from the tail vein at 4 and 23 weeks after LT-HSC transplantation to assess donor-derived contributions by FACS.
Histological analyses of endochondral ossification were performed on sections that were obtained from either fresh frozen, OCT-embedded or formaldehye-fixed, paraffin-embedded specimens. Representative sections were stained with either Hematoxylin-and-Eosin, Movat's modified pentachrome35, Safranin-O or Alizarin Red stains depending on the experiments.
RNA was extracted from sorted cells using Trizol (Invitrogen) or RNeasy RNA isolation kits (Qiagen) and was reverse-transcribed into cDNA with SuperscriptRT III (Invitrogen). SYBR Green Universal Master Mix and a GeneAmp 7000 or 7500 fast sequence detection system (Applied Biosystems) were used for real-time PCR with primers listed in supplementary table 2. Relative expression was calculated for each gene by the 2-ΔΔ CT method with β-actin for normalization.
Chan C.K., Chen C.C., Luppen C.A., Kraft D.L., Kim J.B., DeBoer A., Wei K, & Weissman I.L. (2008). Endochondral ossification is required for hematopoietic stem cell niche formation. Nature, 457(7228), 490-494.
Publication 2008
Actins Antibodies BLOOD Bones Bone Transplantation Capsule CASP3 protein, human Cells Cloning Vectors Collagenase Digestion DNA, Complementary Embryo Endochondral Ossification Eosin Femur Fetus Fluorescent Dyes Fractionation, Chemical Freezing Genes Humerus Integrin alphaV isolation Kidney Macrophage-1 Antigen Mandibular Condyle Mice, Transgenic Mus Oligonucleotide Primers Paraffin Parietal Bone Pelvis Proto-Oncogene Protein c-kit Radius Real-Time Polymerase Chain Reaction RRAD protein, human safranine T Short Hairpin RNA signaling lymphocytic activation molecule, human Skeleton Staining Strains SYBR Green I Tail Tibia Tissue Donors Transplantation trizol Veins
5
Phage Binding Assay for Cell Adhesion
Cited 4 times

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Publication 2009
Alexa594 Antibodies Antibodies, Anti-Idiotypic Bacteriophage T7 Cells Collagen Type I DAPI Equus asinus Fluorescent Antibody Technique Goat Homo sapiens Integrin alphaV Microscopy, Confocal Molecular Probes Mus Neuropilin-1 paraform Rabbits Tissues

Most recents protocols related to «Integrin alphaV»

1
Collagen and Integrin Immunohistochemistry in Carotid Arteries
Histological studies were performed on carotid arteries fixed with 10% buffered formalin under pressure (100 mmHg) in vivo for 2 h. Fixed specimens were embedded in paraffin following regular procedures. Five micrometre sections were stained with Sirius Red and Picrosirius Red (PSR) for collagen. PSR sections were imaged under cross-polarized light (darkfield) to observe collagen birefringence. Images were acquired on an Olympus BX/51 microscope using an Olympus DP70 digital camera (cellSens Dimension) under a × 40 magnification objective. The area fraction of collagen was based on total fibrillar collagen. A custom MATLAB script was used to extract layer-specific (media or adventitia) wall percentages as well as the proportions of thick (red) and thin (orange–yellow–green) birefringent collagen fibres.16 (link),17 (link)For integrin αv subunit immunostaining, rabbit polyclonal antibodies against integrin αv subunit, biotinylated goat anti-rabbit immunoglobulins, HRP-conjugated streptavidin, and 3,3′-diaminobenzidine (DAB) substrate (see Supplementary material online, Tables S7 and S8) were used. Composition of the arterial wall and the media cross-sectional area (MCSA) were determined using a Nikon NIS-Elements Basic Research microscope imaging software as described previously.18 (link)Immunofluorescence staining on 8 µm cryo-sections fixed with 4% paraformaldehyde or cooled acetone for 5 min was performed with specific antibodies as described previously.14 (link) Briefly, sections were incubated with primary antibodies at 4°C overnight after permeabilization with 0.2% Triton X100 for 10 min and blocking with 5% bovine serum albumin (BSA) for 1 h. After washing in PBS-Tween 20, sections were incubated with fluorescent-conjugated secondary antibodies. A complete list of antibodies is provided in Supplementary material online, Table S8. Image acquisition was on a Leica TCS SP5 confocal microscope (Leica, Wetzlar, Germany) with the same depth of field and with identical settings for laser, gain, and offset intensity.
Li Z., Belozertseva E., Parlakian A., Bascetin R., Louis H., Kawamura Y., Blanc J., Gao-Li J., Pinet F., Lacy-Hulbert A., Challande P., Humphrey J.D., Regnault V, & Lacolley P. (2023). Smooth muscle αv integrins regulate vascular fibrosis via CD109 downregulation of TGF-β signalling. European Heart Journal Open, 3(2), oead010.
Publication 2023
Acetone Adventitia Antibodies Antibodies, Anti-Idiotypic Arteries Birefringence Carotid Arteries Collagen Fibrillar Collagen Fibrosis Fingers Fluorescent Antibody Technique Formalin Goat Integrin alphaV Light Microscopy Microscopy, Confocal Paraffin Embedding paraform Pressure Protein Subunits Rabbits Serum Albumin, Bovine Streptavidin Triton X-100 Tween 20
2
Flow Cytometry Analysis of Integrin Expression
Cell surface expression of various integrin receptor subunits or SLC3A2/CD98hc was measured by standard flow cytometry as previously described [32 (link)]. Briefly, the cells (1 × 106) were resuspended in the blocking buffer (DMEM supplemented with 2% BSA and 2% FCS) for 30 min on ice. The cells were then incubated with appropriate primary antibody: Chemicon (anti-integrin β1 MAB 1997 (clone MB1.2); anti-integrin α5 5H10-27 (clone MFR-5); anti-integrin α6 MAB 1378 (clone NKI-GoH3)); BD Pharmingen (anti-integrin β4 553745; anti-integrin αv 552,299 (clone RMV); anti-integrin β3 553343; anti-CD98hc H202-141); Invitrogen (anti-integrin β5 14-0497-82 (clone KN52); anti-integrin α2 14-5971-85 (clone DX5)) or matched isotype control diluted in labelling buffer (DMEM supplemented with 2% FCS) for 1 h on ice. Unbound antibodies were removed by washing twice with PBS, 2% FCS, and the cells were treated with an appropriate fluorescein isothiocyanate (FITC)-conjugated secondary antibody in a labelling buffer for 45 min on ice. The cells were washed again as above and stained with the viability dye 4′, 6′- diamidino-2-phenylindole (DAPI at 0.5 µg/mL) immediately prior to analysis on a BD FACS Canto II Flow Cytometer (BD Biosciences).
Nagpal A., Needham K., Lane D.J., Ayton S., Redvers R.P., John M., Selistre-de-Araujo H.S., Denoyer D, & Pouliot N. (2023). Integrin αvβ3 Is a Master Regulator of Resistance to TKI-Induced Ferroptosis in HER2-Positive Breast Cancer. Cancers, 15(4), 1216.
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Publication 2023
Antibodies Buffers Cells Clone Cells DAPI Flow Cytometry Fluorescein Immunoglobulin Isotypes Immunoglobulins Integrin alpha2 Integrin alphaV Integrins isothiocyanate Protein Subunits Receptors, Cell Surface
3
Protein Isolation and Western Blot Analysis
RIPA buffer (ThermoScientific, Rockford, IL, USA) and complete ULTRA Mini Tablets (Roche, Mannheim, Germany) was used to isolate protein from thrombus and IVC segments and cultured BMDMs or immortalized murine macrophages (RAW264.7 cells). For MMP9 and urokinase analysis, BMDMs and RAW264.7 cells were treated with either IL6 (20 ng/mL) or Brefeldin A (protein transport inhibitor; 500 ng/mL for 3 h). Protein concentration of these lysates was determined using the BCA assay (Thermo Fisher). Protein separation was then achieved by electrophoresis using either NuPAGE 4–12% Bis Tris gels (Invitrogen, Carlsbad, CA) or fixed on percentage SDS polyacrylamide gels. Proteins were then transferred onto PVDF membranes (Millipore, Billerica, MA, USA) and probed with the indicated primary antibodies (and antibody concentration): IL-6 (@1:1000, NB600-1131, Novus Biologicals, Centennial CO), gp130 (@1:1000, bs-1459R, Bioss Biocompare, Woburn, MA), CD126 (@1:1000, GTX37399, GeneTex, Irvine, CA), fibronectin (@1:1000, ab2413, Abcam, Cambridge, MA), MMP9 (@ 1:1000, ab38898, Abcam, Cambridge, MA), integrin α V, (@1:1000, ab179475, Abcam, Cambridge, MA), urokinase (@1:1000, ab24121, Abcam, Cambridge, MA) Bound antibodies were subsequently probed with the indicated secondary antibodies: Goat Anti-Rabbit IgG H&L (Cy2 ®) preadsorbed (@ 1:1,000, ab6940, Abcam, Cambridge, MA), Goat Anti-Mouse IgG H&L (Cy3 ®) preadsorbed (@1:1,000, ab97035, Abcam, Cambridge, MA). Immunoreactive bands were detected using SuperSignal West Pico Chemiluminescent Substrate (REF34577, ThermoScientific, Rockford, IL) and GE Amersham 600 fluorescent imager. Optical densities were normalized to β actin (1:25,000, Santa Cruz Biotechnology, Dallas, Tx) and total protein loading as assayed by colloidal coomassie staining of PVDF membranes and immunoblot band quantitation was performed using Image J software.
Obi A.T., Sharma S.B., Elfline M.A., Luke C.E., Dowling A.R., Cai Q., Kimball A.S., Hollinstat M., Stanger L., Moore B.B., Jaffer F.A, & Henke P.K. (2023). Experimental venous thrombus resolution is driven by IL-6 mediated monocyte actions. Scientific Reports, 13, 3253.
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Publication 2023
Actins anti-IgG Antibodies Biological Factors Bistris Brefeldin A Buffers Electrophoresis FN1 protein, human Gels Goat IL6ST protein, human Immunoblotting Immunoglobulins Integrin alphaV Interleukin 6 Receptor Macrophage MMP9 protein, human Mus Novus polyacrylamide gels polyvinylidene fluoride Proteins Protein Transport Rabbits Radioimmunoprecipitation Assay RAW 264.7 Cells Thrombus Tissue, Membrane Urokinase Vision
4
Cytoskeleton Dynamics Modulation by Inhibitors
Inhibition experiments were performed with blebbistatin (Sigma-Aldrich, USA) or with the ROCK inhibitor Y27632 (Sigma-Aldrich, USA) at concentrations as indicated. Cells were fixed with 2% paraformaldehyde (Sigma-Aldrich, USA) in PBS. Actin cytoskeleton was visualized with phalloidin-Alexa Fluor 647 (ThermoFisher, USA). For flow cytometry, integrin β6 was stained as described previously with an antibody developed by the antibody facility at the University of Geneva (Kessler et al., 2022 (link)). Integrin αV was stained with a commercial antibody (ThermoFisher, USA, clone RMV-7, 1:1000 diluted). Labeling of primary antibodies was visualized with anti-mouse PE and anti-rat PE (both Southern Biotech, USA, 1:1000 diluted). Actin in living cells was visualized with SiR actin (Spirochrome, Switzerland).
Bachmann M., Kessler J., Burri E, & Wehrle-Haller B. (2023). New tools to study the interaction between integrins and latent TGFβ1. bioRxiv.
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Publication Preprint 2023
Actins Alexa Fluor 647 Antibodies blebbistatin Cells Clone Cells Flow Cytometry Immunoglobulins Integrin alphaV Integrins Microfilaments Mus paraform Phalloidine Psychological Inhibition Y 27632
5
Osteoclast Differentiation Protocol
Acacetin and linarin were purchased from Sigma-Aldrich Chemical (St. Louis, MO, USA), as were all other reagents, unless specifically stated elsewhere. Antibodies of mouse CAII and ClC-7 were provided by Abcam Biochemicals (Cambridge, UK). Antibodies of mouse V-ATPase, mouse MMP-9, mouse cathepsin K, mouse integrin αv, mouse osteocalcin, mouse osteopontin, mouse TNSALP, and mouse collagen type I were obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Mouse integrin β3 antibody was purchased from Cell Signaling Technology (Beverly, MA, USA). Horseradish peroxidase (HRP)-conjugated goat anti-rabbit IgG, donkey anti-goat IgG, and goat anti-mouse IgG were supplied by Jackson ImmunoResearch Laboratory (West Grove, PA, USA). Mouse monoclonal β-actin antibody was purchased from Sigma-Aldrich Chemical (St. Louis, MO, USA).
Oh M.S., Kim S.I., Sim Y.E., Park S.H., Kang M.K., Kang I.J., Lim S.S, & Kang Y.H. (2023). Cirsium Setidens Water Extracts Containing Linarin Block Estrogen Deprivation-Induced Bone Loss in Mice. International Journal of Molecular Sciences, 24(2), 1620.
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Publication 2023
acacetin Actins Adenosinetriphosphatase ALPL protein, human anti-IgG Antibodies carbonic anhydrase II protein, human Cathepsin K CLCN7 protein, human Collagen Type I Equus asinus Goat Horseradish Peroxidase Immunoglobulins Immunoglobulin Variable Region Integrin alphaV Integrins linarin MMP9 protein, human Monoclonal Antibodies Mus Osteocalcin Osteopontin Rabbits

Top products related to «Integrin alphaV»

1
Integrin αv by Cell Signaling Technology
Sourced in United States
Integrin αV is a cell surface receptor that binds to a variety of extracellular matrix proteins. It plays a role in cell adhesion, migration, and signaling.
2
Ab179475 by Abcam
Sourced in United Kingdom, United States
Ab179475 is a laboratory product manufactured by Abcam. It serves as a tool for research purposes. No further details on its core function can be provided while maintaining an unbiased and factual approach.
3
Integrin αv by Santa Cruz Biotechnology
Sourced in United States
Integrin αv is a cell surface receptor that mediates cell-cell and cell-extracellular matrix interactions. It acts as a receptor for various ligands including vitronectin, fibronectin, and osteopontin. Integrin αv plays a role in cell adhesion, migration, and signaling.
4
Anti integrin αv by Abcam
Sourced in United States, United Kingdom
Anti-integrin αv is a laboratory reagent that binds to the integrin αv protein. Integrins are cell surface receptors that mediate cell-cell and cell-extracellular matrix interactions. The integrin αv subunit forms heterodimeric complexes with various β subunits, such as β1, β3, β5, β6, and β8.
5
Pvdf membrane by Merck Group
Sourced in United States, Germany, China, United Kingdom, Morocco, Ireland, France, Italy, Japan, Canada, Spain, Switzerland, New Zealand, India, Hong Kong, Sao Tome and Principe, Sweden, Netherlands, Australia, Belgium, Austria
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.
6
Integrin αv by Abcam
Sourced in United Kingdom
Integrin αV is a cell surface adhesion receptor protein that mediates cell-cell and cell-extracellular matrix interactions. It is a subunit that forms part of the integrin αVβ complex, which plays a role in various cellular processes such as cell migration, invasion, and survival.
7
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.
8
β actin by Merck Group
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β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.
9
Integrin α5 by Cell Signaling Technology
Sourced in United States
Integrin α5 is a cell surface receptor protein that functions in cell-cell and cell-extracellular matrix adhesion. It is a member of the integrin family of proteins.
10
β actin by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Germany, Japan, Canada, Morocco, Sweden, Netherlands, Switzerland, Italy, Belgium, Australia, France, India, Ireland
β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is an important component of the microfilament system and is involved in various cellular processes such as cell motility, structure, and integrity.

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