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RHOA protein, human

RHOA protein is a small GTPase that plays a key role in regulating the actin cytoskeleton and cellular morphology.
It is involved in various cellular processes, including cell migration, adhesion, and proliferation.
Dysregulation of RHOA has been implicated in a number of diseases, including cancer, cardiovascular disorders, and neurological conditions.
Researchers can leverage PubCompare.ai's AI-driven insights to optimize protocols and boost reproducibility of RHOA protein research, effortlessly locating the best protocols from literature, preprints, and patents using advanced search and comparison tools.
This platform can help identify the optimal products and procedures for RHOA protein experiments, improving research outcomes and driving scientific discovery.

Most cited protocols related to «RHOA protein, human»

1
Fluorescent Protein-tagged Biosensors for RhoA Signaling
Cited 16 times
Mammalian expression vectors are all based on pEGFP-C1 plasmids (Clontech), in which EGFP was replaced by the YFP variant mVenus. The red fluorescent protein monomeric Cherry (mCherry) was used as RFP variant in this paper.
PCR products were ligated into mVenus-C1 plasmids by cutting the vector and PCR product with restriction enzymes BsrGI and KpnI. Restriction sites are marked in bold in primer sequences. In all cases, full length p63RhoGEF16 (link) was used as a template for PCR. To construct YFP-cDH (amino acid 155–347 of p63RhoGEF), p63RhoGEF was amplified using forward primer 5′- GCTGTACAAGTCCAAGAAGGCTCTGGAAAGG-3′ and reverse primer 5′ - ACGGTACCTTAGCCCTCAAATCCCCGCAA-3′. To construct YFP-pmDH (amino acid 1-347 of p63RhoGEF), p63RhoGEF was amplified using forward primer 5′ - GCTGTACAAGTCCCGGGGGGGGCACAAAGGG-3′ and reverse primer 5′-ACGGTACCTTAGCCCTCAAATCCCCGCAA-3′.
RFP variants of these constructs were made by color swapping the mVenus with mCherry with restriction enzymes AgeI and BsrGI.
The RFP-p63RhoGEF and RFP-p63RhoGEF1 (link)2 (link)3 (link)4 (link)5 (link)6 (link)7 (link)8 (link)9 (link)10 11 (link)12 (link)13 (link)14 (link)15 (link)16 (link)17 (link)18 (link)19 (link)20 (link)21 (link)22 (link)23 (link)24 (link)25 (link)26 (link)27 (link)28 (link)29 (link) (amino acid 1–29 of p63RhoGEF) were obtained by cutting the mVenus variants described earlier20 (link) with AgeI and BsrGI and exchanging mVenus for mCherry.
RFP-FKBP12-C1 was obtained as previously described20 (link).
The RFP-FKBP12-cDH was obtained by cutting RFP-FKBP12-C1 with MfeI and Acc651 and inserting the DH domain cut from the RFP-cDH vector with MfeI and BsrGI. A schematic overview of the constructs is depicted in Supplemental Fig. S1.
A Dimerization Optimized Reporter for Activation (DORA) single-chain RhoA biosensor was constructed such that GTP-loading of RhoA is translated into fluorescent protein heterodimerization, thereby increasing FRET.
The DORA-RhoA coding sequence within a pTriEx backbone is MAHHHHHHGSGS-cpPKN-GTGS-cpV-L9H-L9H-L9H-GS-Cer3(1–229)-AS-RhoA. The lay-out is analogous to a previously published RhoA probe21 (link), retaining regulation by Rho GDIs. Introducing the Q63L mutation in RhoA, locking RhoA in the GTP-bound state and mutating PKN1 (L59Q), preventing binding of RhoA, respectively, resulted in constitutive active (RhoAsensor-ca) and non-binding (RhoAsensor-nb) sensors. The detailed development of the sensor will be described elsewhere.
pTriExRhoA1G and pTriExRhoA2G (Addgene plasmid # 40176) were a gift from Olivier Pertz.
EGFP-MKL2 was a kindly provided by J.S. Hinson33 (link). We swapped the EGFP for mVenus with restriction enzymes AgeI and BsrGI.
The Lck-FRB-ECFP (W66A) and Lck-FRB-ECFP were a kind gift from M. Putyrski51 (link), FRB-YFP-Giantin and CFP-FRB-MoA were a kind gift from T. Inoue52 (link). We swapped the YFP in FRB-YFP-Giantin for ECFP (W66A) with restriction enzymes AgeI and BsrGI. We swapped the CFP in CFP-FRB-MoA for ECFP (W66A) with restriction enzymes NheI and BsrGI. A bacterial expression plasmid RSET-YCam 3.6 was a kind gift of A.Miyawaki36 (link). To enable expression in eukaryotic cells we cut the YCam 3.6 coding sequence from the plasmid with NheI and EcoRI and inserted the fragment in a Clontech-style pEGFP-C1 plasmid, cut with the same enzymes.
van Unen J., Reinhard N.R., Yin T., Wu Y.I., Postma M., Gadella T.W, & Goedhart J. (2015). Plasma membrane restricted RhoGEF activity is sufficient for RhoA-mediated actin polymerization. Scientific Reports, 5, 14693.
Publication 2015
Amino Acids Bacteria Biosensors Cloning Vectors Deoxyribonuclease EcoRI Dimerization DNA Restriction Enzymes Enzymes Eukaryotic Cells Fluorescence Resonance Energy Transfer macrogolgin Mammals MKL2 protein, human Mutation Oligonucleotide Primers Open Reading Frames Plasmids Proteins Prunus cerasus red fluorescent protein rho-Specific Guanine Nucleotide Dissociation Inhibitors RHOA protein, human Tacrolimus Binding Protein 1A Vertebral Column
2
GTPase Activity Assay for Cdc42, Rac1, and RhoA
Cited 15 times
GTPase activity assays were performed as described (Sander et al. 1998). In brief, lysates of NIH3T3 cells were prepared and incubated with bacterially produced GST-PAK-CD or GST-C21 fusion proteins, bound to glutathione-coupled Sepharose beads. The beads and proteins bound to the fusion protein were washed in an excess of lysis buffer, eluted in Laemmli sample buffer, and analyzed for bound Cdc42, Rac1, or RhoA molecules by Western blot using antibodies against Cdc42 (rabbit polyclonal antibody from Santa Cruz Biotechnology), Rac1 (mAb from Transduction Laboratories or when indicated Upstate Biotechnology Inc.) or RhoA (mAb from Santa Cruz Biotechnology).
Sander E.E., ten Klooster J.P., van Delft S., van der Kammen R.A, & Collard J.G. (1999). Rac Downregulates Rho Activity: Reciprocal Balance between Both Gtpases Determines Cellular Morphology and Migratory Behavior. The Journal of Cell Biology, 147(5), 1009-1022.
Publication 1999
Antibodies Biological Assay Buffers CDC42 protein, human Glutathione Guanosine Triphosphate Phosphohydrolases Immunoglobulins Laemmli buffer NIH 3T3 Cells Proteins Rabbits RHOA protein, human Sepharose Western Blotting
3
Engineered Biosensors for Cellular Imaging
Cited 13 times
The three biosensors were made and used as originally described 4 (link)-6 , with modifications where noted in the text. The Cdc42 biosensor was modified for multiplex imaging by removing EGFP and replacing it with an Alexa750 dye. This produced a biosensor with wavelengths orthogonal to those of the RhoA biosensor. The new Cdc42 biosensor was fused to maltose binding protein to enhance solubility. For control studies a new dual chain RhoA biosensor was constructed by eliminating the linker in the published RhoA biosensor (see Supplementary Material).
Machacek M., Hodgson L., Welch C., Elliott H., Pertz O., Nalbant P., Abell A., Johnson G.L., Hahn K.M, & Danuser G. (2009). Coordination of Rho GTPase activities during cell protrusion. Nature, 461(7260), 99-103.
Publication 2009
Biosensors CDC42 protein, human Maltose-Binding Proteins RHOA protein, human
4
Measurement of Endothelial Barrier Function
Cited 11 times
Human pulmonary artery endothelial cells (HPAEC) were obtained from Lonza (Allendale, NJ) and cultured in cell growth medium (EGM-2, Lonza) containing 10% fetal bovine serum (FBS). Cell cultures were maintained at 37°C in a humidified 5% CO2 incubator and used for experiments at passages 5-8. In experiments with agonist stimulation, 10% FBS growth medium was replaced with 2% FBS growth medium for 2 hours prior to experiment. Measurements of transendothelial electrical resistance across a confluent endothelial cell monolayer were performed using the electrical cell-substrate impedance sensing system ECIS-1600 (Applied Biophysics, Troy, NY). Transient transfections with cMyc-tagged RhoA-V14 or Rho kinase-CAT (6-553) were performed using PolyJet transfection reagent (SignaGen, Rockville, MD) according to the manufacturer's protocol. In brief, HPAEC were seeded on 35 mm diameter cell culture dishes with biotinylated gelatin-treated coverslips at a density of 5×105 cells per dish. After 24 hours cells were transfected with 1 μg of plasmid DNA per dish (ratio: 1 μg of DNA per 3 μl of PolyJet). Permeability visualization experiments were performed 24 hours after transfection.
Dubrovskyi O., Birukova A.A, & Birukov K.G. (2012). Measurement of local permeability at subcellular level in cell models of agonist- and ventilator-induced lung injury. Laboratory investigation; a journal of technical methods and pathology, 93(2), 254-263.
Publication 2012
Cell Culture Techniques Cells Culture Media Endothelial Cells Fetal Bovine Serum Gelatins Homo sapiens Hyperostosis, Diffuse Idiopathic Skeletal Impedance, Electric Permeability Plasmids Pulmonary Artery Resistance, Electrical RHOA protein, human ROCK1 protein, human Transfection Transients
5
Monoclonal Antibody and Polyclonal Antibody Generation for GEF-H1 and Tight Junction Proteins
Cited 11 times
mAb B4/7 was derived from a mouse immunized with a protein fraction isolated from detergent extracts of MDCK cells using fusion proteins containing the cytoplasmic domain of low density lipoprotein receptor. Binding of GEF-H1 to this fusion protein was not specific. Hybridoma production and subcloning were as described (Hauri et al., 1985 (link)). Five subclones of the originally isolated hybridoma line were isolated and found to recognize all the same protein in immunoblots and to produce the same pattern in immunofluorescence experiments.
All peptides and antipeptide antibodies were produced by Gramsch Laboratories. The following peptides were used to generate rabbit polyclonal antibodies: anti–cGEF-H1 NH2 terminus, MSRIESLTRARTERC; anti–cGEF-H1 COOH terminus, CDFTRMQDIPEETES; anti–cGEF-H1 alternative domain, CRGHDRLDLSVTIRSVH; anti–ZO-1, YTDQELDETLNDEVC; and anti–claudin-4, PRTDKPYSAKYSAAC. The peptides were conjugated to epoxy-activated Sepharose (Amersham Biosciences), and the antibodies were affinity purified as described (Balda et al., 1996 (link)). For α-tubulin, mAb 1A2 was used (Kreis, 1987 (link)), and in some immunofluorescence experiments ZO-1 was detected with rat monoclonal R40.76 (Anderson et al., 1988 (link)) or with a rabbit polyclonal antibody (Sheth et al., 1997 (link)). α-Catenin was detected with the M12K rabbit polyclonal antibody (Herrenknecht et al., 1991 (link)). GTPases were detected by immunoblotting using the following anti-GTPase antibodies: Rho, rabbit polyclonal antibody sc-179 anti-RhoA (Santa Cruz Biotechnology, Inc.) and Rac1, mouse mAb 102 (BD Transduction Laboratories).
Benais-Pont G., Punn A., Flores-Maldonado C., Eckert J., Raposo G., Fleming T.P., Cereijido M., Balda M.S, & Matter K. (2003). Identification of a tight junction–associated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability. The Journal of Cell Biology, 160(5), 729-740.
Publication 2003
alpha-Tubulin Anti-Antibodies Antibodies Catenins Claudin-4 Cytoplasm Detergents Epoxy Resins Fluorescent Antibody Technique Guanosine Triphosphate Phosphohydrolases Hybridomas Immunoglobulins KIAA0651 protein, human Low Density Lipoprotein Receptor Madin Darby Canine Kidney Cells Mice, House Peptides Proteins Rabbits RHOA protein, human Sepharose Staphylococcal Protein A

Most recents protocols related to «RHOA protein, human»

1
Statins Alleviate LS Membrane Remodeling
Not available on PMC !

Example 2

This example demonstrates that statins alleviate LS membrane remodeling phenotypes.

Statins decrease cholesterol (Cho) biosynthesis by inhibiting 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (FIG. 2A and McFarland et al., Int J Mol Sci 15: 20607-20637 (2014)); consequently, they also down-modulate the downstream synthesis of two intermediates (farnesyl-pyrophosphate and geranyl-geranyl-pyrophosphate) required for RhoA prenylation, which in turn is essential for GTPase membrane anchoring and activation (del Real et al., J Exp Med 200: 541-547 (2004); Demierre et al., Nat Rev Cancer 5: 930-942 (2005); and FIG. 2A). They also have been shown to be active against the RhoA hyperactivation observed in certain cancers (Zhong et al., Cancer Treat Rev 41: 554-567 (2015)).

Several generation statins (Maji et al., Indian J Endocrinol Metab 17: 636-646 (2013)), including fluvastatin, atorvastatin, pitavastatin and rosuvastatin, were tested for their ability to ameliorate LS spreading defects. All statins mitigated to a certain extent the LS spreading phenotype; however, rosuvastatin produced the best results (rosuvastatin>pitavastatin>>>simvastatin and others) in terms of maximizing rescue effect over needed dose and toxicity (FIG. 2B and data not shown).

Phenotype alleviation was observed following the use of an acute rosuvastatin dose (100 μM for 1 h), but similar effect was also evident using lower concentrations (1-10 μM) sustained over longer periods of time (≥72 h; FIG. 2B). Importantly, the latter usage scheme better emulated currently approved treatment conditions with statins that render an effective concentration of free drug in plasma of up to 10 μM (Bjorkhem-Bergman et al., Br J Clin Pharmacol 72: 164-165 (2011)). Following exposure to statins, viability and stress-induced changes in morphology were determined for LS cells (FIG. 2C). Our results showed that rosuvastatin had minimal toxicity, while other statins including pitavastatin and cerivastatin were substantially toxic (FIG. 2C, D). It should be noted that the latter was recalled from the market due to severe rhabdomyolysis effects (Maji et al. (2013), supra). In addition, and to monitor the magnitude of the statins' effects on HMG-CoA reductase in LS cells, we incubated patient fibroblasts in Cho-free media supplemented with vehicle or statins and determined the uptake of fluorescently labeled Cho. While vehicle-treated cells had normal production of endogenous Cho, the ones exposed to statins (due to their HMG-CoA reductase inhibitory activity) were Cho-depleted at a different extent as evidenced by a substantial increase in the uptake of exogenous, fluorescently labeled Cho (FIG. 2E). Our results suggested that rosuvastatin in addition to being less toxic at the chronic dose, led to a less acute inhibition of cholesterol biosynthesis (and consequently to a lower demand of exogenous, fluorescent-analog uptake). However, in contrast with the relatively innocuous chronic exposure (10 μM for ≥72 h), we observed that acute doses of rosuvastatin (100 μM) induced toxicity when exposure time≥15 h (data not shown).

US11857549B2. Compositions and methods for the treatment of Lowe syndrome (2024-01-02). Purdue Research Foundation [US]. Inventors: Ruben Claudio Aguilar [US].
Patent 2024
Anabolism Atorvastatin Cells cerivastatin Cholesterol cholesterol reductase Coenzyme A farnesyl pyrophosphate Fibroblasts Fluvastatin geranylgeranyl pyrophosphate Guanosine Triphosphate Phosphohydrolases Lanugo Malignant Neoplasms Oculocerebrorenal Syndrome Oxidoreductase Patients Pharmaceutical Preparations Phenotype pitavastatin Plasma Prenylation Psychological Inhibition Rhabdomyolysis RHOA protein, human Rosuvastatin Simvastatin Tissue, Membrane Training Programs
2
Immunoblotting Analysis of Cellular Proteins
SaOS2, 293T, and HeLa cell lines were cultured in six-well plates. At 90% confluence, cells were harvested and lyzed using 250 μl of 1 × SDS loading buffer. After heating for 10 min at 100 °C, 20 μl cell lysate was loaded into wells within an SDS-PAGE gel for electrophoresis. After that, immunoblotting was performed using antibodies against the factors, including FLNA (Ab76289, Abcam), TFAP2A (Ab108311, Abcam), HA (H9658, Sigma-Aldrich), GAPDH (RAB0101, Frdbrio), BRF1 (SC-81405, Santa Cruz Biotech), GTF3C2 (SC-81406, Santa Cruz Biotech), c-MYC (SC-40, Santa Cruz Biotech), MDM2 (SC-965, Santa Cruz Biotech), p53 (SC-126, Santa Cruz Biotech), RhoA (SC-418, Santa Cruz Biotech), mCherry (TAG0080, Frdbio), TBP (SC-421, Santa Cruz Biotech), and PTEN (SC7974, Santa Cruz Biotech).
Wang J., Chen Q., Peng F., Zhao S., Zhang C., Song X., Yu D., Wu Z., Du J., Ni H., Deng H, & Deng W. (2023). Transcription factor AP-2α activates RNA polymerase III–directed transcription and tumor cell proliferation by controlling expression of c-MYC and p53. The Journal of Biological Chemistry, 299(3), 102945.
Publication 2023
Antibodies Buffers Cell Lines Cells Electrophoresis GAPDH protein, human HeLa Cells MDM2 protein, human Oncogenes, myc PTEN protein, human RHOA protein, human SDS-PAGE TFAP2A protein, human
3
Osteoclast Rho GTPase Activation
Osteoclasts were starved for 4 h in 2% FBS containing α-MEM, and then stimulated with 20 ng/ml M-CSF and 30 ng/ml RANKL for 15 min and lysed. Cell lysates were harvested, and Rho GTPase activity analyzed using RhoA/Rac1 G-LISA Activation Assay kits (BK135; Cytoskeleton) according to the manufacturer’s instructions.
Zhu L., Tang Y., Li X.Y., Kerk S.A., Lyssiotis C.A., Sun X., Wang Z., Cho J.S., Ma J, & Weiss S.J. (2023). Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption. The Journal of Cell Biology, 222(4), e202206121.
Publication 2023
Biological Assay Cells Cytoskeleton Macrophage Colony-Stimulating Factor Osteoclasts RHOA protein, human rho GTP-Binding Proteins TNFSF11 protein, human
4
Manipulation of MMP9, MMP14, and RhoA in BMDMs
Where indicated, BMDMs were transduced with either a control vector, wild-type human MMP9, a catalytically inactive MMP9 E402/A mutant (Orgaz et al., 2014 (link)), wild-type human MMP14, a catalytically inactive MMP14 E240/A mutant expression vector (Shimizu-Hirota et al., 2012 (link)), or a constitutively active human RhoA L63 expression vector (RTV-204; Cell Biolabs). The MMP9 and MMP14 constructs were cloned into the pLentilox-IRES-GFP lentiviral vector, while the RhoA constructs were inserted into pBABEhygro retroviral vector. Expression of the recombinant proteins was confirmed by Western blot.
Zhu L., Tang Y., Li X.Y., Kerk S.A., Lyssiotis C.A., Sun X., Wang Z., Cho J.S., Ma J, & Weiss S.J. (2023). Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption. The Journal of Cell Biology, 222(4), e202206121.
Publication 2023
Cells Cloning Vectors Homo sapiens Internal Ribosome Entry Sites MMP9 protein, human MMP14 protein, human Recombinant Proteins Retroviridae RHOA protein, human Western Blot
5
Osteoclast Dysfunction Pathways
Fig. S1 displays mitochondrial abundance and OXPHOS expression in Mmp9/Mmp14 DKO osteoclasts. Fig. S2 shows the identification and quantitative analysis of the metabolome in Mmp9/Mmp14 DKO osteoclasts. Fig. S3 depicts that active RhoA rescues defects in sealing zone formation and bone resorption in DKO osteoclasts. Fig. S4 shows that galectin-3 surface binding antagonist reverses functional defects in DKO osteoclasts. Fig. S5 depicts a galectin-3–Lrp1 axis regulates RhoA activation and sealing zone formation in osteoclasts. Table S1 is the list of the genotyping PCR primers. Table S2 lists the quantitative real-time PCR primers. Table S3 shows the list of galectin-3 interacting partners through mass spectrometry.
Zhu L., Tang Y., Li X.Y., Kerk S.A., Lyssiotis C.A., Sun X., Wang Z., Cho J.S., Ma J, & Weiss S.J. (2023). Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption. The Journal of Cell Biology, 222(4), e202206121.
Publication 2023
Bone Resorption Epistropheus Galectin 3 Mass Spectrometry Metabolome Mitochondria MMP9 protein, human MMP14 protein, human Oligonucleotide Primers Osteoclasts Real-Time Polymerase Chain Reaction RHOA protein, human

Top products related to «RHOA protein, human»

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
Anti rhoa by Cell Signaling Technology
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Anti-RhoA is a primary antibody that recognizes the RhoA protein, a small GTPase involved in cytoskeletal organization and cell signaling. It can be used for various applications, such as Western blotting, immunoprecipitation, and immunofluorescence.
3
Rhoa g lisa activation assay kit by Cytoskeleton
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The RhoA G-LISA Activation Assay Kit is a laboratory equipment product designed to measure the activation of the RhoA protein. It utilizes a Rho-binding domain (RBD) to selectively capture the active, GTP-bound form of RhoA from cell lysates. The kit includes the necessary reagents and materials to perform the assay.
4
Y 27632 by Merck Group
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Y-27632 is a selective and potent Rho-associated protein kinase (ROCK) inhibitor. It functions by inhibiting the activity of ROCK, a key enzyme involved in various cellular processes.
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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.
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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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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.
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Anti rhoa by Santa Cruz Biotechnology
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Anti-RhoA is an antibody product that specifically recognizes the RhoA protein. RhoA is a small GTPase that plays a key role in regulating the organization of the actin cytoskeleton. The Anti-RhoA antibody can be used to detect and study the expression and localization of RhoA in various experimental systems.
10
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.

More about "RHOA protein, human"

RHOA (Ras Homolog Family Member A) is a small GTPase that plays a critical role in regulating the actin cytoskeleton and cellular morphology.
This versatile protein is involved in a variety of cellular processes, including cell migration, adhesion, and proliferation.
Dysregulation of RHOA has been implicated in numerous diseases, such as cancer, cardiovascular disorders, and neurological conditions.
Researchers can leverage the powerful tools and AI-driven insights provided by PubCompare.ai to optimize their RHOA protein research protocols and boost reproducibility.
This platform allows users to effortlessly locate the best protocols from the literature, preprints, and patents using advanced search and comparison functionalities.
By utilizing PubCompare.ai, researchers can identify the optimal products and procedures for their RHOA protein experiments, improving research outcomes and driving scientific discovery.
For example, the platform can provide guidance on the use of transfection reagents like Lipofectamine 2000, antibodies such as Anti-RhoA, and assay kits like the RhoA G-LISA Activation Assay Kit.
Additionally, researchers may find insights on the use of cell culture supplements like FBS, reference genes like GAPDH, and laboratory materials like PVDF membranes and TRIzol reagent.
Unlock the full potential of your RHOA protein research with PubCompare.ai.
Leveraging the platform's AI-driven insights, you can optimize your protocols, enhance reproducibility, and accelerate your scientific discoveries, ultimately contributing to a better understanding of this crucial small GTPase and its role in health and disease.