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- Table of Contents
Facts about Growth factor receptor-bound protein 2.
Human | |
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Gene Name: | GRB2 |
Uniprot: | P62993 |
Entrez: | 2885 |
Belongs to: |
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GRB2/sem-5/DRK family |
abundant SRC homology; Adapter protein GRB2; ASH; EGFRBP-GRB2; epidermal growth factor receptor-binding protein GRB2; GRB2; Grb3-3; growth factor receptor-bound protein 2; growth factor receptor-bound protein 3; HT027; MST084; MSTP084; NCKAP2; Protein Ash; SH2/SH3 adapter GRB2
Mass (kDA):
25.206 kDA
Human | |
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Location: | 17q25.1 |
Sequence: | 17; NC_000017.11 (75318076..75405709, complement) |
Nucleus. Cytoplasm. Endosome. Golgi apparatus.
High-affinity primary antibody companies are best if you are searching for antibodies that will work with the GRB2Marker. For the past 25 years, boster antibodies have been widely used in research. They have also been validated by Western blotting and immunohistochemistry. Boster antibodies can therefore be trusted.
In addition to regulating a wide variety of kinases, GRB2 is critical for many cellular functions. GRB2 is essential for many cellular functions. It can also affect the development of different organisms. This protein can cause disruptions in cell proliferation and transformation. GRB2 is crucial for many functions and plays an important role in epidermal grow factor receptor tyrosinekinase signaling (EGFRTK). GRB2 can be used as a signaling molecular by different tyrosinekinases, and not all kinases.
It is a cytosolic molecule that is involved in energy metabolism, meiosis, and organogenesis. It is called Gfrb2 (GRB2) in animals. It has a SH3-SH2 arrangement. CsGrb2 recombinant was synthesized by using a bacterial purification technique. This product was then identified using mouse immune serum and western blotting.
GRB2 plays a critical role in intracellular signal transmission. This is important for immune system regulation. Repetitive stimuli increase cell responsiveness and improve its ability to discriminate meaningful signals. Moreover, repeated stimuli are critical for tolerance to persisting foreign antigens, averting autoimmunity, and preventing immune pathogenesis. Furthermore, subthreshold contact interactions between mature lymphocytes and self-antigen-presenting cells also influence lymphocyte activation thresholds, providing added flexibility to positive selection in the thymus.
The cytoskeleton remodeling and motility process of cancer cells involves Grb2 and a number of related proteins. These interactions are recapped by a multistep cancer metastaticsis cascade. Grb2 inhibitors are effective in reducing cell motility and cancer metastasis in animal models. We still need to do more research before we can recommend a therapeutic approach.
The coexpression of ErbB2 and EGFR results in distinct potency of EGF stimulation and alters the requirement of clathrin in signaling. Thus, the interaction of ErbB2 and c-Src is selective. It is possible, based on the coexpression GRB2/clathrin, to identify a subset ErbB-signaling profiles.
Principal component analysis revealed that there were several pY-containing proteins. Additionally, the pY marks of several peptides were identical in both Western blot as well as mass spectrometry tests. This confirms that the ErbB2/Neu signaling pathway is governed by the same pY marks. These proteins may play a major role in regulating Fzd9b and Wnt9a signaling.
GRB2 interacts to actin filament machinery, and the cytoskeletal-associated protein WASp. This protein regulates actin and cytoskeleton rearrangement. Mutations in WASp proteins can cause defects in platelets as well as T and B-cell polarization. Patients with the WASp mutation have an increased risk of developing cancer.
The ligand-bound EGFR undergoes clathrin-mediated endocytosis, a major mechanism for internalization of EGFR. The receptor is then integrated into the clathrin-coated holes. Clathrin is an integral component plasma membranes. The receptor's assembly creates lattice structures which recruit additional cytosolic cargo proteins and cargo.
Despite the complex nature of this pathway the results prove that GRB2 plays a central role in the downstream ErbB2/Neu pathway. These results will enable further research into the role of this protein for ErbB2/Neu signaling. The work suggests that this kinase is involved in the regulation of EGFR phosphorylation.
GRB2 plays a crucial role in activating the ErbB2/Neu pathway. This kinase-dependent signaling pathway is mediated by the CMV tyr1a gene. The development disease-fighting immunity begins with the cytokine response.
It is unclear what Grb2's role in adhesion signalsing is. Although the protein has been implicated with multiple tumor metastasis and proliferation, its exact function is still unknown. The protein has several functions, including recruitment of CBL and regulating kinetic properties of activated RTKs. It may also promote cell movements through its association of GRB2 and Gab1.
FAK's focal adhesion target domain can exist in monomeric and arm-exchanged dimers, but it must undergo a transition into an intermediate open state in order for it to interact directly with Grb2. This will allow it to activate signaling pathways and cause pathological cardiac hypertrophy. Targeted molecular dynamic simulations of proteins involved in this transition have shown the structure of the intermediate by unfolding Helix1 at an acute angle and then folding it back to a full turn. GRB2 is a key adapter protein that could play a role with adhesion signalsing.
The interactions between Grb2 and SOS1 in tumors have been reported in the literature, including direct and indirect interactions with cytoskeleton remodeling and motility molecules. These interactions can be reconstructed in a multistep pathway for cancer metastasis. Inhibitors of Grb2SH2 domain binding have decreased tumor metastasis rates in animal models. Inhibitors of Grb2 are also useful as anticancer drugs.
It also interacts with the actin filament machinery, as well as cytoskeletal associated protein WASp. This protein regulates the rearrangement and migration of actin filaments. Patients who have mutations in WASp are more likely to experience defects in platelets, T- and B-cell polarization, or migration in response. Moreover, patients with WASp mutations have a greater risk of developing malignancies, which affect their ability to respond to other types of immune response.
GRB2 is important for adhesion signaling and platelet activation. It is a signaling mediator in platelets by stabilizing LAT signalosomes. Grb2 is also important for platelet coagulation. It is important to note that Grb2 plays a vital role in adhesion signaling.
Researchers can detect GRB2 levels in cancer cells using a novel ELISA method that increases the sensitivity of the test to the picogram range. Picokine(tm), a flexible ELISA kit with high sensitivity that has been validated for a wide variety of samples, is now available. A detailed procedure and image are available upon request. Picoband, a polymer-based secondary antibody, saves up to 30 minutes of IHC. The proprietary technology behind Picoband is based upon insights into the design immunogens. Technical support is provided by Sanbio, BeNeLux distributor.
GRB2 is a marker that has been linked to cancer. This may make it a target for anticancer therapeutics. The antibody emits 177Lub-particles and is very specific. This technology has the potential of speeding up the translation from the lab to a clinic of new discoveries. Theranostics also allows for the validation of a target and can ensure that therapy is accessible to patients who are most likely be benefited.
Glycans are a valuable target for anti-cancer neoantigens. Glycans can be used as therapeutic antibodies targets. They are also useful neoantigens. Most vaccines target the polysaccharides of pathogens. However, most therapeutic antibodies are geared towards targeting proteins. Practical reasons account for the lack of suitable glycan-neoantigens. To be effective, mammalian Glycans must be broken down through tolerance due to their high expression during embryonic development and low levels in normal tissues.
This antibody binds Siglec-10. It acts as an antagonist of macrophages' phagocytosis and functions in the same manner as the CD47/SIRPa. The antibody blocks Siglec, a tumor related protein's ligand-binding ability. The anti-Siglec antibody improved the phagocytosis CD24-positive tumour cells. This suggests the potential for a new form of cancer immunotherapy.
PMID: 1322798 by Lowenstein E.J., et al. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling.
PMID: 1384039 by Matuoka K., et al. Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries.