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> Chemicals & Drugs > Amino Acid > Paxillin

Paxillin

Paxillin is a focal adhesion-associated adaptor protein that plays a key role in regulating cell adhesion, migration, and signaling.
It serves as a scaffold, interacting with various proteins involved in cytoskeletal organization and signal transduction.
Paxillin is implicated in a variety of cellular processes, including cell motility, cell survival, and cancer metastasis.
Researchers studying paxillin-related mechanisms can leverage PubCompare.ai's AI-powered tools to optimize their research, streamline protocol identification, and enhance the reproducibility and accuracy of their findings.
PubCompare.ai's platform enables easy access to relevant protocols from literature, preprints, and patents, while providing AI-driven comparisons to identify the best protocols and products for paxillin-related studies.

Most cited protocols related to «Paxillin»

1
Cell Migration on Rigidity Gradients
Cited 10 times

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Publication 2012
Cell Nucleus Cells Chemotaxis Haptotaxis Lens, Crystalline Medical Devices Microscopy, Phase-Contrast Migration, Cell Muscle Rigidity Paxillin Reading Frames Strains
2
Western Blot Analysis of Protein Phosphorylation
Cited 7 times
Cells were lysed in SDS sample buffer composed of 1.5% dithiothreitol, 2% SDS, 80 mM Tris-HCl (pH 6.8), 10% glycerol and 0.01% bromophenol blue. The lysates were boiled in the buffer for 5 min and separated by SDS-PAGE. Proteins were transferred to nitrocellulose membranes. The membranes were blocked with bovine serum albumin or milk for 1 h and probed with use of primary antibodies followed by horseradish peroxidase-conjugated secondary antibodies (Fisher Scientific). Proteins were visualized by enhanced chemiluminescence (Fisher Scientific) using the GE Imager 600 System. Antibody used were anti-Plk-1 (Millipore, Cat#05-844, Lot#2477015), anti-c-Abl (Cell Signaling, Cat#2862 S, Lot#13), anti-paxillin (BD Biosciences, Cat#610051, Lot#7208686), anti-GAPDH (glyceraldehyde 3-phosphate dehydrogenase. Ambion, Cat# AM4300, Lot#1311029), anti-MEK1/2 (Santa Cruz, Cat#Sc-436, Lot# H3011), anti-ERK1/2 (Cell Signaling, Cat#4695, Lot#8), anti-p-MEK1/2 (Santa Cruz, Cat# Sc-81503, Lot# I1813), anti-p-ERK1/2 (Cell Signaling, Cat# 9106 S, Lot# 38). Antibodies against phospho-vimentin (Ser-56) and total vimentin were custom made by Synpep Inc (CA, USA) and previously characterized18 (link),36 (link). The levels of proteins were quantified by scanning densitometry of immunoblots (Fuji Multigauge Software). The luminescent signals from all immunoblots were within the linear range.
Liao G., Wang R., Rezey A.C., Gerlach B.D, & Tang D.D. (2018). MicroRNA miR-509 Regulates ERK1/2, the Vimentin Network, and Focal Adhesions by Targeting Plk1. Scientific Reports, 8, 12635.
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Publication 2018
Antibodies Bromphenol Blue Buffers Cells Chemiluminescence Densitometry Dithiothreitol GAPDH protein, human Glyceraldehyde-3-Phosphate Dehydrogenases Glycerin Horseradish Peroxidase Immunoblotting Immunoglobulins Luminescence MAP2K1 protein, human Milk, Cow's Mitogen-Activated Protein Kinase 3 Nitrocellulose Paxillin PLK1 protein, human Proteins SDS-PAGE Serum Albumin, Bovine Tissue, Membrane Tromethamine Vimentin
3
Imaging Substrate Deformation in Cells
Cited 7 times
Cells were imaged in an enclosed 37°C, 5% CO2 incubation chamber. Images were taken on the 561 nm (paxillin TMR) and the 642 nm (beads) channels with a 500 ms exposure time every 5 seconds for 200 frames using a Nikon Ti Total Internal Reflection Fluorescence (TIRF) microscope using a 100× objective with 1.5× additional magnification factor with a Hamamatsu ORCA-D2 CCD camera (Hamamatsu Corporation, Bridgewater. NJ, USA, final resolution: 43 nm/pixel). To obtain a bead image from the undeformed substrate, cells were removed from the substrate by injecting a high dose (0.5%) of 5 mL Trypsin/EDTA (Invitrogen) for 30 min.
Han S.J., Oak Y., Groisman A, & Danuser G. (2015). Traction microscopy to identify force modulation in sub-resolution adhesions. Nature methods, 12(7), 653-656.
Publication 2015
A-factor (Streptomyces) Cells Edetic Acid factor A Factor V Microscopy, Fluorescence Neoplasm Metastasis Orcinus orca Paxillin Reading Frames Reflex Trypsin
4
Imaging Substrate Deformation in Cells
Cited 7 times
Cells were imaged in an enclosed 37°C, 5% CO2 incubation chamber. Images were taken on the 561 nm (paxillin TMR) and the 642 nm (beads) channels with a 500 ms exposure time every 5 seconds for 200 frames using a Nikon Ti Total Internal Reflection Fluorescence (TIRF) microscope using a 100× objective with 1.5× additional magnification factor with a Hamamatsu ORCA-D2 CCD camera (Hamamatsu Corporation, Bridgewater. NJ, USA, final resolution: 43 nm/pixel). To obtain a bead image from the undeformed substrate, cells were removed from the substrate by injecting a high dose (0.5%) of 5 mL Trypsin/EDTA (Invitrogen) for 30 min.
Han S.J., Oak Y., Groisman A, & Danuser G. (2015). Traction microscopy to identify force modulation in sub-resolution adhesions. Nature methods, 12(7), 653-656.
Publication 2015
A-factor (Streptomyces) Cells Edetic Acid factor A Factor V Microscopy, Fluorescence Neoplasm Metastasis Orcinus orca Paxillin Reading Frames Reflex Trypsin
5
mCardinal Protein Fusion Constructs
Cited 6 times
mCardinal cDNA was PCR amplified with a 5′ primer encoding an AgeI site and a 3′ primer encoding either a BspEI (C1) or NotI (N1) site for C-terminal and N-terminal fusions (with regards to the FP), respectively. The purified and digested PCR products were ligated into similarly digested pEGFP-C1 and pEGFP-N1 cloning vectors to create pmCardinal-C1 and pmCardinal-N1. A cDNA fragment encoding each protein domain was PCR amplified with primers containing the appropriate restriction enzyme sites and ligated into pmCardinal-C1 or pmCardinal-N1. To prepare fusions at the N-terminus of mCardinal, the following digests were performed: human non-muscle α-actinin (GenBank accession number NM_001130005.1, source: Tom Keller, Florida State University, Tallahassee, FL, U.S.A.), EcoRI and NotI; human calnexin (NM_001746.3, Origene), AgeI and NotI; human centromere protein B (NM_001810.5, Alexey Khodjakov, Wadsworth Center, Albany, NY, U.S.A.), BamHI and NotI; rat β-2 connexin-26 (NM_001004099.1, Matthias Falk, Lehigh University, Bethlehem, PA, U.S.A.), EcoRI and BamHI; human keratin 18 (NM_199187.1, Open Biosystems), EcoRI and NotI; yeast Lifeact (IDT DNA), BamHI and NotI; human pyruvate dehydrogenase, (NM_000284, Origene), AgeI and NotI; human peroxisomal membrane protein (NM_018663.1, Origene), NotI and AgeI; human vimentin (NM_003380.3, Origene), NheI and BamHI; chicken paxillin (NM_204984.1, Clare Waterman, NIH, Bethesda, MD, U.S.A), NheI and BamHI; mouse mannosidase II (NM_008549.2, Jennifer Lippincott-Schwartz, NIH), NheI and BamHI; and human histone H1 (NM_008197.3, David Gilbert, Florida State University), BamHI and NheI. To prepare C-terminal fusions to mCardinal, the following digests were performed: human β-actin (NM_001101.3, Clontech), NheI and BglII; human α-tubulin (NM_006082, Clontech), NheI and BglII; human Rab4a (NM_004578.2, Viki Allen, University of Manchester, U.K.), BspEI and BamHI; human lamin B1 (NM_005573.2, George Patterson, NIH), EcoRI and BamHI; human myotilin (NM_006790.1, Origene), AgeI and BspEI; human fibrillarin (NM_001436.3, Evrogen), BglII and BamHI; human tight junction protein ZO1 (NM_003257.1, Origene), AgeI and BspEI; human VE cadherin (NM_001795.3, Origene), BglII and EcoRI; and the 20-amino-acid farnesylation signal from c-Ha-Ras (NM_001130442.1, Clontech), AgeI and BspEI. Full sequences of plasmids are available upon request.
Chu J., Haynes R.D., Corbel S.Y., Li P., González-González E., Burg J.S., Ataie N.J., Lam A.J., Cranfill P.J., Baird M.A., Davidson M.W., Ng H.L., Garcia K.C., Contag C.H., Shen K., Blau H.M, & Lin M.Z. (2014). Non-invasive intravital imaging of cellular differentiation with a bright red-excitable fluorescent protein. Nature methods, 11(5), 572-578.
Publication 2014
Actinin Actins alpha-D-mannosidase II alpha-Tubulin Amino Acids Calnexin CDH5 protein, human CENPB protein, human Chickens Cloning Vectors Deoxyribonuclease EcoRI DNA, Complementary DNA Restriction Enzymes Farnesylation fibrillarin Gjb2 protein, rat Histone H1 Homo sapiens HRAS protein, human KRT18 protein, human LMNB1 protein, human Mice, Laboratory Muscle Tissue NR4A2 protein, human Oligonucleotide Primers Oxidoreductase Paxillin Peroxisome Plasmids Protein Domain Pyruvates Saccharomyces cerevisiae Tissue, Membrane TJP1 protein, human Vimentin

Most recents protocols related to «Paxillin»

1
Genistein Modulates Gene Expression in Cell Lines
Cells were grown with or without different doses of genistein and solvent control for 5 h. Total RNA was isolated using the RNeasy Plus Mini Kit. The cDNA was synthesized using a reverse transcription reagent kit (Selleck, Shanghai, China). Target genes were amplified with the following specific primers in the Light Cycler® 96 Real-Time PCR System (Roche, Indianapolis, IN, USA):
GAPDH: 5′-GGAGCGAGATCCCTCCAAAAT-3′ (forward) and
5′-GGCTGTTGTCATACTTCTCATGG-3′ (reverse);
FAK: 5′-TGGTGCAATGGAGCGAGTATT-3′(forward) and
5′-CAGTGAACCTCCTCTGACCG-3′(reverse);
Paxillin: 5′-CTGCTGGAACTGAACGCTGTA-3′ (forward) and
5′-GGGGCTGTTAGTCTCTGGGA-3′ (reverse);
Snail: 5′-TCGGAAGCCTAACTACAGCGA-3′ (forward) and
5′-AGATGAGCATTGGCAGCGAG-3′ (reverse);
Twist: 5′-GTCCGCAGTCTTACGAGGAG-3′ (forward) and
5′-GCTTGAGGGTCTGAATCTTGCT-3′ (reverse).
GAPDH was used as a normalization control. Each treatment was tested in triplicate. The relative expression levels of genes were normalized using the 2−ΔΔCt method.
Chen T., Wang J., Li M., Wu Q, & Cui S. (2023). Genistein Inhibits Proliferation and Metastasis in Human Cervical Cancer Cells through the Focal Adhesion Kinase Signaling Pathway: A Network Pharmacology-Based In Vitro Study in HeLa Cells. Molecules, 28(4), 1919.
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Publication 2023
Cells DNA, Complementary GAPDH protein, human Gene Expression Genes Genistein Light Oligonucleotide Primers Paxillin Reverse Transcription Snails Solvents
2
Immunofluorescence Analysis of Cell Markers
Cells were seeded on glass coverslips, fixed with 4% PFA (Sigma-Aldrich) and incubated overnight at 4°C with the following primary antibodies: anti-PanCytokeratin (Mouse 1:200, Dako, Glostrup, Denmark), anti-Epcam (Mouse 1:1000, clone HEA-125, GeneTex, Irvine, CA, USA), anti-AQ-1 (Mouse 1:50, clone B-11, Santa Cruz Biotechnology, Heidelberg, Germany), anti-CD13-PE (Mouse 1:25, Biolegend, San Diego, CA, USA), anti-CD13-FITC (Mouse 1:25, Abcam, Cambridge, UK), anti-N-cadherin (Rabbit 1:50, Abcam, and Mouse 1:50, clone 32/N, Becton Dickinson, San Josè, CA, USA), anti-Calbindin (Mouse 1:100, clone CB-955, Sigma-Aldrich), anti-E-cadherin (Mouse 1:50, Becton Dickinson, and Rabbit 1:50, Cell Signalling Technology, Danvers, MA, USA) and anti-Paxillin (Mouse 1:50, Becton Dickinson). When necessary, the secondary antibodies Alexa 488 conjugated anti-mouse IgG and Alexa 594 conjugated anti-rabbit IgG (1:100, Molecular Probes, Carlsberg, CA, USA) were used. Stress fibers were labeled by Alexa-Fluor-594-phalloidin (1:100, Molecular Probes) and nuclei counterstained with Mounting DAPI (Molecular Probes). Immunofluorescence images were obtained with a Zeiss LSM810 confocal microscope, using a 63x objective, equipped with Zen2009 software (Zeiss, Oberkochen, Germany).
Torsello B., De Marco S., Bombelli S., Cifola I., Morabito I., Invernizzi L., Meregalli C., Zucchini N., Strada G., Perego R.A, & Bianchi C. (2023). High glucose induces an activated state of partial epithelial-mesenchymal transition in human primary tubular cell cultures. PLOS ONE, 18(2), e0279655.
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Publication 2023
Alexa594 anti-IgG Antibodies Cadherins Calbindins Cell Nucleus Cells Clone Cells DAPI Fluorescein-5-isothiocyanate Immunofluorescence Immunoglobulin G Microscopy, Confocal Molecular Probes Mus Paxillin Phalloidine Rabbits Stress Fibers TACSTD1 protein, human
3
Quantifying Focal Adhesions and Actin Cytoskeleton
Seeded cells were washed with PBS, fixed for 30 min with 4% PFA, washed with PBS 3 times for 5 min, and permeabilized for 5 min with 0.3% Triton. Cells were then blocked for 1 h with 10% BSA and 3% milk diluted in PBS at room temperature (RT). Cells were next immunolabeled for 2 h with a primary anti-paxillin antibody (Merck Millipore, Burlington, MA, USA, dilution of 1:200), then incubated for 1 h at RT with an Alexa Fluor secondary antibody (ThermoFisher, Waltham, MA, USA, 1:500), Alexa Fluor Phalloidin (ThermoFisher, 1 U/mL), and Hoechst (ThermoFisher, 1:1000), all diluted in 1% PBS/BSA solution. Cells were then washed with PBS 3 times for 5 min. Coverslips containing resting cells were mounted with Dako Faramount Aqueous Mounting Medium on SuperFrost Plus microscope slides, and migrating cells were directly visualized in Ibidi chambers using the COSD confocal microscope with a plan-Apochromat 63x/1.4 water-immersion objective. The quantification of FA number and cell surface occupancy was performed as previously described [27 (link),46 (link)]. The number of FAs was then normalized to the total cell surface, while surface occupancy distinguished the cell front, center, and rear. The quantification of actin cytoskeleton cell surface occupancy was performed using the same method. The quantification of FA and F-actin polarization was determined by the proportion of FA or F-actin area at the cell front, center, or rear compared to the total area of FA or F-actin.
Vanderroost J., Avalosse N., Mohammed D., Hoffmann D., Henriet P., Pierreux C.E., Alsteens D, & Tyteca D. (2023). Cholesterol and Sphingomyelin Polarize at the Leading Edge of Migrating Myoblasts and Involve Their Clustering in Submicrometric Domains. Biomolecules, 13(2), 319.
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Publication 2023
Antibodies, Anti-Idiotypic Cells F-Actin Forehead Immunoglobulins Microfilaments Microscopy Microscopy, Confocal Milk, Cow's Paxillin Phalloidine Submersion Technique, Dilution
4
Paxillin Protein Immunoprecipitation Protocol
1,000 µg total protein was incubated with 5 µg rabbit anti-Paxillin (STJ94969; antibodyplus, isotype IgG) overnight at 4°C. The next day, 1.5 mg precleared Dynabeads Protein G (10003D) were added to the protein-antibody mixture and rotated for 2 h at 4°C, followed by three washes with RIPA lysis buffer. Finally, the protein was eluted using 2× Laemmli sample buffer (1610747; Bio-rad) with a reducing agent. Samples were further analyzed by Western blot.
Xue Q., Varady S.R., Waddell T.Q., Roman M.R., Carrington J, & Roh-Johnson M. (2023). Lack of Paxillin phosphorylation promotes single-cell migration in vivo. The Journal of Cell Biology, 222(3), e202206078.
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Publication 2023
Buffers G-substrate Immunoglobulin Isotypes Immunoglobulins Laemmli buffer Paxillin Proteins Rabbits Radioimmunoprecipitation Assay Reducing Agents Western Blotting
5
Western Blot Analysis of Cell Signaling
Cells in culture were lysed in RIPA lysis buffer (89900; Thermo Fisher Scientific) with proteinase and phosphatase inhibitor cocktail (P8340, 524635; Sigma-Aldrich) directly from cell culture plates. Tumor tissue was dissociated by OMNI tissue homogenizer and then lysed in the same conditions as described above. Lysates were centrifuged at 14,000 g in 4°C and the protein concentration was measured with Pierce BCA Protein Assay Kit (23225; Thermo Fisher Scientific).
15 µg protein was mixed with 4× Laemmli sample buffer (1610747; Bio-Rad) with a reducing agent and was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A 45 µm nitrocellulose membrane (1620115; Bio-Rad) was used to transfer protein from SDS-polyacrylamide gels. The blocking buffer was either 5% BSA (in TBS/0.1% TWEEN 20) for detecting phospho-specific protein or 5% non-fat dry milk (in TBS/0.1% TWEEN 20) for non-phospho-specific protein. Primary antibodies used were rabbit anti-Paxillin (1:1,000, STJ94969; Antibodyplus), rabbit anti-pY118-Paxillin (1:1,000, 9369; Cell Signaling Technology), rabbit anti-FAK (1:1,000, 3285; Cell Signaling Technology), rabbit anti-pFAK397 (1:1,000, 3283; Cell Signaling Technology), chicken anti-GFP (1:500, ab13970; Abcam), mouse anti-CrkII (1:1,000610035; BD Bioscience), mouse anti-DOCK180 (1:500, sc-13163; Santa Cruz Biotechnology), mouse anti-C3G (1:250, sc-178403; Santa Cruz Biotechnology), rabbit p-ERK (1:1,000, 9101S; Cell Signaling Technology), and rabbit anti-pY31-Paxillin (1:1,000, 44-720G; Thermo Fisher Scientific). Secondary antibodies used were goat anti-chicken IgY(H + L) conjugated with HRP (1:10,000, A16054; Thermo Fisher Scientific), goat anti-mouse IgG(H + L) antibody conjugated with HRP (1:10,000, A28177; Thermo Fisher Scientific), and donkey anti-rabbit IgG(H + L) antibody conjugated with HRP (1:10,000, NA934V; GE Healthcare). Antibody signals were detected using SuperSignal West Pico Plus Chemiluminescent Substrate (34580; Thermo Fisher Scientific) and were further quantified using densitometric analysis on FIJI software.
Xue Q., Varady S.R., Waddell T.Q., Roman M.R., Carrington J, & Roh-Johnson M. (2023). Lack of Paxillin phosphorylation promotes single-cell migration in vivo. The Journal of Cell Biology, 222(3), e202206078.
Full text: Click here
Publication 2023
anti-IgG Antibodies Biological Assay Buffers Cell Culture Techniques Chickens Densitometry Endopeptidases Equus asinus Goat Immunoglobulins Laemmli buffer Milk, Cow's Mitogen-Activated Protein Kinase 3 Mus Neoplasms Nitrocellulose Paxillin Phosphoric Monoester Hydrolases polyacrylamide gels Proteins Rabbits Radioimmunoprecipitation Assay Reducing Agents SDS-PAGE Tissue, Membrane Tissues Tween 20

Top products related to «Paxillin»

1
Ab32084 by Abcam
Sourced in United States, United Kingdom
Ab32084 is a laboratory reagent. It is a monoclonal antibody that can be used for research applications.
2
Paxillin by BD
Sourced in United States
Paxillin is a cytoskeletal protein that functions as an adapter, linking cell surface receptors to the actin cytoskeleton. It plays a role in the regulation of cell adhesion, motility, and signaling pathways.
3
Paxillin by Cell Signaling Technology
Sourced in United States, United Kingdom
Paxillin is a focal adhesion-associated protein that serves as a molecular scaffold, facilitating the assembly of multi-protein complexes involved in cell signaling pathways. It plays a crucial role in the regulation of cell adhesion, migration, and cytoskeletal organization.
4
Fetal bovine serum (fbs) by Thermo Fisher Scientific
Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal
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.
5
4 6 diamidino 2 phenylindole (dapi) by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, Japan, China, Canada, Italy, Australia, France, Switzerland, Spain, Belgium, Denmark, Panama, Poland, Singapore, Austria, Morocco, Netherlands, Sweden, Argentina, India, Finland, Pakistan, Cameroon, New Zealand
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.
6
Paxillin by Abcam
Sourced in United States
Paxillin is a cytoplasmic focal adhesion protein that plays a crucial role in the organization of the actin cytoskeleton. It serves as a platform for the assembly of signaling complexes involved in cell adhesion, migration, and differentiation.
7
Anti paxillin by BD
Sourced in United States
Anti-paxillin is a laboratory reagent used for the detection and analysis of the paxillin protein in cell samples. Paxillin is a focal adhesion-associated protein that plays a role in the regulation of cell adhesion and migration. The anti-paxillin reagent can be used in various cell biology research applications, such as immunofluorescence microscopy and Western blotting, to visualize and quantify the expression and localization of paxillin within cells.
8
P paxillin by Cell Signaling Technology
Sourced in United States
P-paxillin is a primary antibody that detects paxillin phosphorylated at tyrosine 118. Paxillin is a focal adhesion-associated protein that functions in the regulation of cell migration and adhesion. This antibody can be used to detect the phosphorylation state of paxillin in various cell and tissue samples using techniques such as Western blotting or immunohistochemistry.
9
E cadherin by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Germany, Canada, Japan, France, Macao, Morocco
E-cadherin is a cell-cell adhesion molecule that plays a crucial role in maintaining the structural and functional integrity of epithelial tissues. It is a transmembrane protein that mediates homophilic interactions between neighboring cells, contributing to the formation and stability of adherens junctions.
10
Rhodamine phalloidin by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, China, Japan, India, Panama, Australia, Switzerland, Morocco
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.

More about "Paxillin"

Paxillin is a crucial focal adhesion-associated adaptor protein that plays a pivotal role in regulating cell adhesion, migration, and signaling.
It serves as a dynamic scaffold, interacting with various proteins involved in cytoskeletal organization and signal transduction.
This multifunctional protein is implicated in a wide range of cellular processes, including cell motility, cell survival, and cancer metastasis.
Researchers studying paxillin-related mechanisms can leverage PubCompare.ai's cutting-edge AI-powered tools to optimize their research, streamline protocol identification, and enhance the reproducibility and accuracy of their findings.
PubCompare.ai's platform enables easy access to relevant protocols from literature, preprints, and patents, while providing AI-driven comparisons to identify the best protocols and products for paxillin-related studies.
Paxillin is closely associated with other key proteins and cellular structures, such as Ab32084, FBS, DAPI, Anti-paxillin, P-paxillin, E-cadherin, and Rhodamine phalloidin.
These interrelated components play vital roles in cell adhesion, cytoskeletal organization, and signal transduction pathways involving paxillin.
By understanding the intricate relationships and functions of paxillin and its associated elements, researchers can gain deeper insights into the underlying mechanisms governing cellular processes and disease pathogenesis.
PubCompare.ai's AI-driven tools and comprehensive resource library can help researchers streamline their paxillin-related studies, optimizing experimental design, improving protocol selection, and enhancing the overall reproducibility and accuracy of their findings.
Leveraging this innovative platform can be a game-changer in advancing paxillin research and unlocking new discoveries in cell biology, cancer, and beyond.