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GRB2 protein, human

Q: What are the different variations or types of the GRB2 protein?

The GRB2 (Growth Factor Receptor-Bound Protein 2) is a single protein that does not have distinct variations or types. It is a highly conserved adaptor protein that plays a central role in various signal transduction pathways across different cell types and organisms. While the GRB2 protein itself does not have distinct isoforms or variants, it can interact with a wide range of other signaling proteins and receptors, leading to diverse cellular responses depending on the specific cellular context and inputs.

Q: How can the GRB2 protein be utilized in different applications?

The GRB2 protein has numerous applications in cell biology research and the development of targeted therapies: - It is a key signaling node in pathways regulating cell growth, differentiation, and survival, making it a potential target for cancer therapeutics. - Studying the interactions between GRB2 and receptor tyrosine kinases can provide insights into signal transduction mechanisms and help identify new drug targets. - Monitoring GRB2 localization and activity can serve as a readout for the activation status of signaling pathways in various cellular contexts. - Recombinant GRB2 protein can be used in in vitro assays to investigate its binding partners and downstream effects. - Geneticly engineered cell lines with GRB2 knockdown or overexpression are valuable tools for dissecting its role in specific signaling cascades.

Q: What are some common challenges in working with the GRB2 protein?

Some common challenges in working with the GRB2 portein include: - Ensuring specificity of GRB2 interactions, as it can bind to multiple phosphorylated tyrosine residues on different receptors and signaling proteins. - Difficulty in isolating and purifying the GRB2 protein while maintaining its native conformation and binding affinities. - Measuring the dynamic changes in GRB2 localization and activation in live cells in response to various stimuli. - Developing assays that can accurately quantify the strength and kinetics of GRB2 interactions with its binding partners. - Translating findings from cell-based studies to in vivo models, as the role of GRB2 can be context-dependent.

Q: How can PubCompare.ai assist researchers working with the GRB2 protein?

PubCompare.ai is a powerful tool that can greatly assist researchers working with the GRB2 protein in the following ways: 1. Screeining protocol literature more effciently: The platform's AI-driven search and analysis capabilities can help researchers quickly identify the most relevant and effective protocols from published literature, preprints, and patents related to working with the GRB2 protein. 2. Leveraging AI to pinpoint critical insights: PubCompare.ai's AI algorithms can analyze and compare multiple GRB2 protein protocols, highlighting key differences in their effectiveness, reproducibility, and suitability for specific research goals. This enables researchers to make more informed decisions when selecting the best protocols. 3. Enhancing reproducibility and accuracy: By providing a structured, data-driven comparison of GRB2 protein protocols, PubCompare.ai helps researchers choose the most robust and reliable methods, improving the reproducibility and accuracy of their experiments.

GRB2 (Growth Factor Receptor-Bound Protein 2) is an adaptor protein that plays a crucial role in signal transduction pathways involved in cell growth, differentiation, and survival.
It acts as a linlk between activated receptor tyrosine kinases and downstream signaling cascades, such as the Ras/MAPK pathway.
GRB2 contains Src homology (SH) domains that facilitate interactions with specific phosphorylated tyrosine residues on receptors and other signaling proteins.
The GRB2 protein is essential for proper cellular function and its dysregulation has been implicated in various disease states, including cancer.
Understanding the role and regulation of GRB2 is of great interest for researchers studying cell biology and developing targeted therapies.

Most cited protocols related to «GRB2 protein, human»

EGFR Signaling Pathway Regulation

Cited 8 times

Unless otherwise indicated, all reagents were of analytical grade and obtained from Sigma-Aldrich (St. Louis, MO). Cell culture media were purchased from Invitrogen (Carlsbad, CA). Activated EGFR kinase and phospho-tyrosine monoclonal antibody (mAb) were purchased from Cell Signaling Technology (Danvers, MA). Silencer Negative Control #1 small interfering RNA (siRNA) and siRNA Gα_i3 were purchased from Ambion (Austin, TX) and Santa Cruz Biotechnology (Santa Cruz, CA), respectively. Streptavidin-horseradish peroxidase (HRP), biotinylated EGF, and mouse submaxillary EGF were purchased from Invitrogen, and Rhodamine Red X-anti-HRP was from Jackson ImmunoResearch Laboratories (West Grove, PA). Antibodies against GIV that were used in this work include rabbit serum and affinity-purified anti-GIV coiled-coil immunoglobulin (Ig)G (GIV-ccAb) raised against the coiled-coil domain of GIV (Le-Niculescu et al., 2005 (link); Ghosh et al., 2008 (link)), and affinity-purified anti-Girdin C terminus (GIV-CTAb) raised against the last 19 aa of GIV's C terminus (IBL America, Minneapolis, MN). To visualize total EGFR by immunofluorescence, mAb #225 raised against the ectodomain (gift from Gordon Gill, University of California San Diego [UCSD], La Jolla, CA; Gill et al., 1984 (link)) or polyclonal antibody (pAb) anti-EGFR against the C-terminus of EGFR (Cell Signaling Technology). Polyclonal phosphosite-specific EGFR antibodies (pY992, pY1045, and pY1068; Cell Signaling Technology), mAb pY845 (Millipore, Billerica, MA), and total EGFR (tEGFR) antibodies (Cell Signaling Technology and Santa Cruz Biotechnology) were used for immunoblotting. Rabbit polyclonal antibodies (pAb) against Gαi3 (Calbiochem, San Diego, CA) for immunofluorescence, Gαi3 (M-14, Santa Cruz Biotechnology) for immunoblotting, STAT5b and Grb2 (Santa Cruz Biotechnology), phospho-Y527 Src, PLCγ1, phospho-Y783 PLCγ1, phospho-S473 Akt, and phospho-ERK1/2 (Cell Signaling Technology), were obtained commercially. Mouse monoclonal antibodies (mAb) against phospho-Y845 EGFR and phospho-Y694/Y699-STAT5b (Millipore), Akt and EEA1 (BD Biosciences, San Jose, CA), c-Src (Santa Cruz Biotechnology), ERK1/2 (Cell Signaling Technology), and tubulin (Sigma-Aldrich) were obtained from commercial sources. Anti-mouse and anti-rabbit Alexa-594– and Alexa-488–coupled goat secondary antibodies for immunofluorescence (IF) were purchased from Invitrogen. Goat anti-rabbit and goat anti-mouse Alexa Fluor 680 or IRDye 800 F(ab`)2 for immunoblotting were from LI-COR Biosciences (Lincoln, NE). Control mouse and rabbit IgGs for immunoprecipitations were purchased from Bio-Rad Laboratories (Hercules, CA) and Sigma-Aldrich, respectively.

Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M, & Farquhar M.G. (2010). A Gαi–GIV Molecular Complex Binds Epidermal Growth Factor Receptor and Determines Whether Cells Migrate or Proliferate. Molecular Biology of the Cell, 21(13), 2338-2354.

Publication 2010

Alexa594 anti-c antibody Antibodies Antibodies, Anti-Idiotypic austin c-src Genes Cell Culture Techniques Cells Cetrimonium Bromide Culture Media EGFR protein, human Gills Goat GRB2 protein, human Horseradish Peroxidase Immunofluorescence Immunoglobulins Immunoprecipitation IRDye800 Mitogen-Activated Protein Kinase 3 Monoclonal Antibodies Mus Phosphotransferases PLCG1 protein, human Rabbits Rhodamine RNA, Small Interfering Serum STAT5B protein, human Streptavidin Tubulin Tyrosine

Genetic Mouse Models Reveal Pericyte Reduction

Cited 7 times

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Publication 2010

Brain Embryo Genome GRB2 protein, human HMN (Hereditary Motor Neuropathy) Proximal Type I Immunoglobulin Domains Institutional Animal Care and Use Committees Isoleucine Kidney Mice, Laboratory Neurocirculatory Asthenia Pericytes Phenylalanine Phosphatidylinositol 3-Kinases Phospholipase C gamma Platelet-Derived Growth Factor beta Receptor Point Mutation PTPN11 protein, human ras GTPase-Activating Proteins Signal Peptides Signal Transduction Pathways Tyrosine

Molecular Cloning and Mutagenesis of LRRK1, LRRK2, and Rab Proteins

Cited 6 times

Human LRRK1 cDNA was subcloned into vector pGFP-C1 (Clontech), pCMV or pCS2. LRRK1(4PA), LRRK1(K1243M) and LRRK1(S625N) were generated using the QuickChange Site-Directed Mutagenesis Kit according to the manufacturer's protocol (Stratagene). siRNA-resistant LRRK1 was generated by mutating the target sequence of the LRRK1 siRNA (5′-GCAGGAACAGGAAAGTCACCATTTA-3′) into 5′-GTCGAAATCGAAAAGTCACCATTTA-3′. Human LRRK2 (Park8) cDNA was subcloned into vector pCMV. HA-Grb2(P49L), HA-Grb2(S90N), HA-Grb2(G203R) and HA-Grb2(P49L/G203R) were generated using the mutagenesis kit described above and subcloned into vector pSRα37 (link). Human Rab5 and Rab7 were subcloned into vector pGFP-C1 or pDsRed-C1 (Clontech; catalogue number 632466), and Rab5(Q79L) was generated using the mutagenesis kit described above. pDsRed-C1 produces the monomer form of DsRed. Deletion constructs of STAM1 were generated by PCR-based mutagenesis and subcloned into pCMV-Flag.

Hanafusa H., Ishikawa K., Kedashiro S., Saigo T., Iemura S.I., Natsume T., Komada M., Shibuya H., Nara A, & Matsumoto K. (2011). Leucine-rich repeat kinase LRRK1 regulates endosomal trafficking of the EGF receptor. Nature Communications, 2, 158-.

Publication 2011

Cloning Vectors Deletion Mutation DNA, Complementary GRB2 protein, human Homo sapiens leucine-rich repeat kinase 1, human LRRK2 protein, human Mutagenesis Mutagenesis, Site-Directed RNA, Small Interfering STAM-1

Antibody Production and Characterization

Cited 5 times

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Publication 2017

Amino Acids Antibodies Antibody Formation Cardiac Arrest Cysteine GRB2 protein, human Immune Sera Immunoblotting Immunoglobulins Institutional Animal Care and Use Committees keyhole-limpet hemocyanin Monoclonal Antibodies Oryctolagus cuniculus Peptides Rabbits SH3 Domain WWOX protein, human

Grb2 SUMOylation Assay in HEK293T

Cited 5 times

Grb2 SUMOylation was analysed in HEK293T by the method of in vivo SUMOylation assay using Ni²⁺-NTA beads as previously described [12 (link),19 (link)]. In vitro E.coli BL21-based SUMOylation assay with the plasmid pE1E2S1 was conducted as previously described [14 (link)].

Qu Y., Chen Q., Lai X., Zhu C., Chen C., Zhao X., Deng R., Xu M., Yuan H., Wang Y., Yu J, & Huang J. (2014). SUMOylation of Grb2 enhances the ERK activity by increasing its binding with Sos1. Molecular Cancer, 13, 95.

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Publication 2014

Biological Assay Escherichia coli GRB2 protein, human Plasmids Sumoylation

Most recents protocols related to «GRB2 protein, human»

SAXS Structural Analysis Workflow

SAXS data reduction, buffer subtraction, and further analysis were performed using BioXTAS RAW version 2.1.1^{107 (link)}. An average of 30 frames prior to an eluted peak was used for buffer subtraction. Protein peaks were also run through evolving factor analysis (EFA) to deconvolute peaks into the individual scattering components where applicable. The forward scattering intensity I(0) and radius of gyration (R_g) were calculated from the Guinier fit. The normalized Kratky plot, pair distance distribution plot, or P(r), and Porod volume (V_P) were calculated using the program GNOM embedded in the BioXTAS RAW software^{86 (link)}. The calculation of theoretical scattering curves for the crystal structure PDB 1GRI was performed using the program CRYSOL, part of the ATSAS software package (version 3.1.0)^{86 (link),87 (link)}. The initial all-atom model of the full-length SH2/SH2 domain-swapped dimer was generated with PyMOL version 2.5.2 using PDB structures 1GRI (full-length GRB2 dimer) and 6ICH (SH2 domain-only dimer)^{60 (link),71 (link),108}. Each chain of the 1GRI dimer was superimposed over one of the SH2 domains comprising the 6ICH dimer. Intermodular linkers were built, N-terminal His-tags added, and missing amino acids inserted using YASARA^{109 (link)}. Reconstruction of the electron density was calculated from SAXS data using the program DENSS version 1.6 embedded in the BioXTAS RAW software^{89 (link)}. The final representative model was colorized and annotated using PyMOL and Chimera version 1.16^{110 (link)}.

Sandouk A., Xu Z., Baruah S., Tremblay M., Hopkins J.B., Chakravarthy S., Gakhar L., Schnicker N.J, & Houtman J.C. (2023). GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production. Scientific Reports, 13, 3505.

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Publication 2023

Amino Acids Buffers Chimera Electrons GRB2 protein, human Proteins Radius Reading Frames Reconstructive Surgical Procedures SH2 Domain

Generation of Pseudo-Typed Lentiviral Particles

To generate pseudo-typed lentiviral particles, shRNA-encoding pLK4 vectors were transfected into 293 T cells along with pCL-Eco and Pax2 packaging vectors and VSV-G envelope vector. At 18–24 h prior to transfection, 7.5 × 10⁶ cells were seeded into one 15 cm tissue culture dish in cDMEM and incubated overnight. At 1–2 h prior to transfection, the media was replaced with fresh cDMEM. Lentiviral DNA was introduced into 293 T cells using the calcium phosphate transfection method. Per transfection, plasmids were combined at a ratio of 6:4:3 (30 ug lentiviral plasmid containing the desired construct, 20 ug packaging vectors, and 15 ug envelope vector) with CaCl₂ at a final concentration of 125 mM and HEPES-buffered saline at a final concentration of 50 mM HEPES pH 7.05, 140 mM NaCl, and 1.5 mM Na₂HPO₄). DNA was allowed to precipitate for 30 min at room temperature, then added drop-wise to 293 T cells. After 12–18 h, the transfection media was replaced with fresh cDMEM media combined with unsupplemented DMEM at a ratio of 20/80 for a final FBS concentration of 2%. Viral supernatant was harvested at 24 h intervals over the following 3 days, then spun down and filtered through 0.45-um Durapore Millex (Millipore) filters. Virus was diluted in a solution of 10% (w/v) PEG-8000 and 300 mM NaCl, rotated overnight at 4 °C, and spun down at 3000 g for 1 h at 4 °C. The viral pellet was held overnight at 4 °C in 1× PBS at 1/100th the original volume of the viral supernatant and spun down to pellet serum protein and other particulates. Concentrated virus was stored at -80 °C or used immediately to transduction. HUT 78 T lymphocytes at 0.5 × 10⁶ cells/mL were allowed to grow for 2–3 days in the presence of concentrated virus and hexadimethrine bromide (Polybrene) transfection reagent (Sigma Aldrich) at a concentration of 8 μg/mL before removal of the virus and initiation of puromycin selection. Cells were allowed to expand in the presence of increasing puromycin concentration, from 0.25 μg/mL to a final selection concentration of 1 μg/mL. Whole cell lysates were probed for loss of GRB2 expression and expression of GRB2 mutants after 2–3 passages in puromycin.

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Publication 2023

ARID1A protein, human Calcium Phosphates Cells Cloning Vectors GRB2 protein, human HEK293 Cells HEPES Hexadimethrine Bromide Hyperostosis, Diffuse Idiopathic Skeletal PAX2 protein, human Plasmids Polybrene polyethylene glycol 8000 Puromycin Saline Solution Serum Proteins Short Hairpin RNA Sodium Chloride T-Lymphocyte Tissues Transfection Virus

Genetic manipulation of GRB2 in T cells

For mammalian expression, HUT 78 T lymphocytes were transduced with pLK4 lentiviruses containing GRB2 shRNAs alone or with sequences encoding add-back wild-type or mutant GRB2 as previously described^{106 (link)}. Six silent mutations were introduced to the add-back GRB2 sequences to generate GRB2 messenger resistant to shRNA-mediated degradation. GRB2 derivatives bearing the mutations discussed were constructed by site-directed mutagenesis. The V123D putative monomer mutation was introduced by PCR using the following primers: 5′-GAAGTACTTCCTCTGGGTGGATAAGTTCAATTC-3′ and 5′-AGCTCATTCAAAGAATTGAACTTATCCACCCAGAG-3′. For the V122P/V123P putative dimer mutant, the primers were the following: 5′-CGGGAAGTACTTCCTCTGGCCGCCGAAGTTCAATT-3′ and 5′-GCTCATTCAAAGAATTGAACTTCGGCGGCCAGAGGAAG-3′. The N188D mutation was introduced by overlap extension PCR using the following primer pairs: 5′-CTTCAAGGTGCTCCGAGATGGAG-3′ and 5′-GGGTCTGAGTCATCCATGACATGGATAAAATCTC-3′; 5′-GTCATGGATGACTCAGACCCCAACTGGTG-3′ and 5′-GGGCGACCGGACTCTAGAG-3′. The N214D mutation was introduced using the following primers: 5′-GGACATAGAACAGGTGCCACAGCAG-3′ and 5′-AGTCGCGGCCGCTTAGACGTTCCGGTCCACGGGGGTGAC-3′. Primers were purchased from Integrated DNA Technologies (Coralville, IA). Expression of shRNA was under control of the U6 promoter, whereas add-back GRB2 expression was under control of the EF-1α promoter. Transduced cells were kept in selection with 1 μg/mL puromycin (Santa Cruz). For bacterial expression, the sequence encoding full-length, wild-type human GRB2 was cloned into the pET-28a(+) vector (Novagen, cat. no. 69864) and E. coli BL21 (DE3) cells transformed with the vectors as previously described^{36 (link)}. The same primers as listed above were used to generated Histidine-tagged variants of GRB2 for recombinant expression.

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Publication 2023

Bacteria Cells Cloning Vectors derivatives Escherichia coli GRB2 protein, human Histidine Homo sapiens Lentivirus Mammals Mutagenesis, Site-Directed Mutation Oligonucleotide Primers Puromycin Short Hairpin RNA Silent Mutation T-Lymphocyte

Western Blot Analysis of Signaling Proteins

Following SDS-PAGE, resolved proteins were transferred onto a PVDF membrane (Millipore) and then blocked for 1 h at room temperature in a 1:1 solution of SEA Block buffer (Thermo Scientific) in 1X PBS. Membranes were incubated for 1 h at room temperature or overnight at 4 °C with primary antibodies followed by two washes in 0.05% Tween-20 in 1X PBS. Secondary anti-mouse or anti-rabbit DyLight 680- or 800-conjugated antibodies were applied for 1 h at room temperature followed by 2 washes. Blots were then visualized using the Licor Odyssey Infrared detector. Densitometric analysis of protein bands was performed using Odyssey’s v3.0 software and normalized to GAPDH. The followed primary antibodies were used: GRB2 (BD Pharmingen or Cell Signaling Technology); LAT pY226 (clone J96-1238.58.93, BD Pharmingen); and GAPDH (Meridian Bioscience).

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Publication 2023

Antibodies Buffers Clone Cells Densitometry GAPDH protein, human GRB2 protein, human Meridians Mus polyvinylidene fluoride Proteins Rabbits SDS-PAGE Tissue, Membrane Tween 20

GRB2 Protein Structural Analysis

SEC–MALS–SAXS data sets were collected using the 18-ID-D BioCAT Beamline at the Advanced Proton Source (APS) at Argonne National Laboratory (Chicago, IL). Samples were centrifuged for 5 min at 13,000 rpm to remove any potential aggregates prior to column loading. Samples containing 4–9 mg/mL of GRB2 WT or mutants in 250 μL were injected onto a 24 mL Superdex 75 Increase 10/300 analytical-grade column (GE) equilibrated with 20 mM Tris pH 8.0, 150 mM NaCl, and 1 mM DTT at a flow rate of 0.5 mL/minute on an Agilent 1300 chromatography system. Column eluant was analyzed in line by the UV absorbance detector of the Agilent 1300 chromatography system, then subsequently directed into the DAWN Heleos-II light scattering (LS) and OptiLab T-rEX refractive index detectors in series. Finally, the elution trajectory directed samples into a 1.0 mm ID quartz capillary SAXS sample cell. Scattering data were collected every 1 s using a 0.5 s exposure and detected with a Pilatus 3 1 M pixel detector (DECTRIS) with a 12 keV (1.033 Å wavelength) X-ray beam covering a q-range of 0.0045 < q < 0.35 Å − 1 (q = 4π/λsinθ, where λ is the wavelength and 2θ is the scattering angle). Accurate protein molecular weights from MALS data were determined using the ASTRA software (Wyatt Technology).

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Publication 2023

Capillaries Chromatography GRB2 protein, human Hereditary Diseases Light Proteins Protons Quartz Radiography Sodium Chloride Tromethamine

Top products related to «GRB2 protein, human»

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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.

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.

Protease inhibitor cocktail by Merck Group

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Anti grb2 by Cell Signaling Technology

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Anti-Grb2 is a primary antibody that detects the Grb2 protein. Grb2 is an adapter protein involved in various cell signaling pathways. The antibody can be used for applications such as Western blotting to identify and quantify Grb2 expression in cellular samples.

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.

Anti grb2 by BD

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Anti-Grb2 is a laboratory reagent that inhibits the function of the Grb2 (Growth factor receptor-bound protein 2) adaptor protein. Grb2 plays a crucial role in various cellular signaling pathways, making it a valuable target for research and investigation in biological systems.

Gapdh by Cell Signaling Technology

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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.

β actin by Cell Signaling Technology

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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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PhosSTOP is a phosphatase inhibitor cocktail designed for the inhibition of serine/threonine and tyrosine phosphatases during protein extraction and sample preparation for downstream analysis.

Trizol reagent by Thermo Fisher Scientific

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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.

What are the different variations or types of the GRB2 protein?

The GRB2 (Growth Factor Receptor-Bound Protein 2) is a single protein that does not have distinct variations or types. It is a highly conserved adaptor protein that plays a central role in various signal transduction pathways across different cell types and organisms. While the GRB2 protein itself does not have distinct isoforms or variants, it can interact with a wide range of other signaling proteins and receptors, leading to diverse cellular responses depending on the specific cellular context and inputs.

How can the GRB2 protein be utilized in different applications?

The GRB2 protein has numerous applications in cell biology research and the development of targeted therapies: - It is a key signaling node in pathways regulating cell growth, differentiation, and survival, making it a potential target for cancer therapeutics. - Studying the interactions between GRB2 and receptor tyrosine kinases can provide insights into signal transduction mechanisms and help identify new drug targets. - Monitoring GRB2 localization and activity can serve as a readout for the activation status of signaling pathways in various cellular contexts. - Recombinant GRB2 protein can be used in in vitro assays to investigate its binding partners and downstream effects. - Geneticly engineered cell lines with GRB2 knockdown or overexpression are valuable tools for dissecting its role in specific signaling cascades.

What are some common challenges in working with the GRB2 protein?

Some common challenges in working with the GRB2 portein include: - Ensuring specificity of GRB2 interactions, as it can bind to multiple phosphorylated tyrosine residues on different receptors and signaling proteins. - Difficulty in isolating and purifying the GRB2 protein while maintaining its native conformation and binding affinities. - Measuring the dynamic changes in GRB2 localization and activation in live cells in response to various stimuli. - Developing assays that can accurately quantify the strength and kinetics of GRB2 interactions with its binding partners. - Translating findings from cell-based studies to in vivo models, as the role of GRB2 can be context-dependent.

How can PubCompare.ai assist researchers working with the GRB2 protein?

PubCompare.ai is a powerful tool that can greatly assist researchers working with the GRB2 protein in the following ways: 1. Screeining protocol literature more effciently: The platform's AI-driven search and analysis capabilities can help researchers quickly identify the most relevant and effective protocols from published literature, preprints, and patents related to working with the GRB2 protein. 2. Leveraging AI to pinpoint critical insights: PubCompare.ai's AI algorithms can analyze and compare multiple GRB2 protein protocols, highlighting key differences in their effectiveness, reproducibility, and suitability for specific research goals. This enables researchers to make more informed decisions when selecting the best protocols. 3. Enhancing reproducibility and accuracy: By providing a structured, data-driven comparison of GRB2 protein protocols, PubCompare.ai helps researchers choose the most robust and reliable methods, improving the reproducibility and accuracy of their experiments.

More about "GRB2 protein, human"

GRB2, also known as Growth Factor Receptor-Bound Protein 2, is a crucial adaptor protein that plays a pivotal role in various cellular signaling pathways.
This SH2/SH3 domain-containing protein acts as a linker, facilitating the communication between activated receptor tyrosine kinases and downstream signaling cascades, such as the Ras/MAPK pathway.
GRB2 is essential for proper cell growth, differentiation, and survival.
Researchers studying cell biology and developing targeted therapies often utilize various techniques to investigate the role and regulation of GRB2.
Common experimental approaches include the use of PVDF membranes for Western blotting, Lipofectamine 2000 for transfection, and protease inhibitor cocktails to preserve protein integrity.
Anti-Grb2 antibodies are frequently employed for immunoprecipitation and immunoblotting studies.
Supplementing cell culture media with FBS can provide the necessary growth factors, while GAPDH and β-actin are commonly used as loading controls.
PhosSTOP, a phosphatase inhibitor, can help maintain the phosphorylation state of GRB2 and associated proteins.
The TRIzol reagent is often used for RNA extraction to analyze the transcriptional regulation of GRB2.
Understanding the complex interplay of GRB2 and its involvement in signaling pathways is crucial for advancements in cell biology and the development of targeted therapies, particularly in the context of diseases like cancer where GRB2 dysregulation has been implicated.
By leveraging the insights gained from the MeSH term description and the metadescription, researchers can optimze their GRB2 protein research using cutting-edge tools like PubCompare.ai, which can help locate the best protocols from literature, preprints, and patents to enhance reproducibility and accuracy.