Recombinant Human GRB2 protein (Tagged) is a Human Full Length protein, in the 2 to 217 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
M A S M T G G Q Q M G R G H H H H H H E N L Y F Q G G S E A I A K Y D F K A T A D D E L S F K R G D I L K V L N E E C D Q N W Y K A E L N G K D G F I P K N Y I E M K P H P W F F G K I P R A K A E E M L S K Q R H D G A F L I R E S E S A P G D F S L S V K F G N D V Q H F K V L R D G A G K Y F L W V V K F N S L N E L V D Y H R S T S V S R N Q Q I F L R D I E Q V P Q Q P T Y V Q A L F D F D P Q E D G E L G F R R G D F I H V M D N S D P N W W K G A C H G Q T G M F P R N Y V T P V N R N V
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Non-enzymatic adapter protein that plays a pivotal role in precisely regulated signaling cascades from cell surface receptors to cellular responses, including signaling transduction and gene expression (PubMed:11726515, PubMed:37626338). Thus, participates in many biological processes including regulation of innate and adaptive immunity, autophagy, DNA repair or necroptosis (PubMed:35831301, PubMed:37626338, PubMed:38182563). Controls signaling complexes at the T-cell antigen receptor to facilitate the activation, differentiation, and function of T-cells (PubMed:36864087, PubMed:9489702). Mechanistically, engagement of the TCR leads to phosphorylation of the adapter protein LAT, which serves as docking site for GRB2 (PubMed:9489702). In turn, GRB2 establishes a a connection with SOS1 that acts as a guanine nucleotide exchange factor and serves as a critical regulator of KRAS/RAF1 leading to MAPKs translocation to the nucleus and activation (PubMed:12171928, PubMed:25870599). Functions also a role in B-cell activation by amplifying Ca(2+) mobilization and activation of the ERK MAP kinase pathway upon recruitment to the phosphorylated B-cell antigen receptor (BCR) (PubMed:25413232, PubMed:29523808). Plays a role in switching between autophagy and programmed necrosis upstream of EGFR by interacting with components of necrosomes including RIPK1 and with autophagy regulators SQSTM1 and BECN1 (PubMed:35831301, PubMed:38182563). Regulates miRNA biogenesis by forming a functional ternary complex with AGO2 and DICER1 (PubMed:37328606). Functions in the replication stress response by protecting DNA at stalled replication forks from MRE11-mediated degradation. Mechanistically, inhibits RAD51 ATPase activity to stabilize RAD51 on stalled replication forks (PubMed:38459011). Additionally, directly recruits and later releases MRE11 at DNA damage sites during the homology-directed repair (HDR) process (PubMed:34348893). Isoform 2. Does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced transactivation of a RAS-responsive element. Acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death. Mechanistically, inhibits RAS-ERK signaling and downstream cell proliferation by competing with GRB2 for SOS1 binding and thus by regulating SOS1 membrane recruitment (PubMed:36171279).
ASH, GRB2, Growth factor receptor-bound protein 2, Adapter protein GRB2, Protein Ash, SH2/SH3 adapter GRB2
Recombinant Human GRB2 protein (Tagged) is a Human Full Length protein, in the 2 to 217 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 0.32% Tris HCl
Non-enzymatic adapter protein that plays a pivotal role in precisely regulated signaling cascades from cell surface receptors to cellular responses, including signaling transduction and gene expression (PubMed:11726515, PubMed:37626338). Thus, participates in many biological processes including regulation of innate and adaptive immunity, autophagy, DNA repair or necroptosis (PubMed:35831301, PubMed:37626338, PubMed:38182563). Controls signaling complexes at the T-cell antigen receptor to facilitate the activation, differentiation, and function of T-cells (PubMed:36864087, PubMed:9489702). Mechanistically, engagement of the TCR leads to phosphorylation of the adapter protein LAT, which serves as docking site for GRB2 (PubMed:9489702). In turn, GRB2 establishes a a connection with SOS1 that acts as a guanine nucleotide exchange factor and serves as a critical regulator of KRAS/RAF1 leading to MAPKs translocation to the nucleus and activation (PubMed:12171928, PubMed:25870599). Functions also a role in B-cell activation by amplifying Ca(2+) mobilization and activation of the ERK MAP kinase pathway upon recruitment to the phosphorylated B-cell antigen receptor (BCR) (PubMed:25413232, PubMed:29523808). Plays a role in switching between autophagy and programmed necrosis upstream of EGFR by interacting with components of necrosomes including RIPK1 and with autophagy regulators SQSTM1 and BECN1 (PubMed:35831301, PubMed:38182563). Regulates miRNA biogenesis by forming a functional ternary complex with AGO2 and DICER1 (PubMed:37328606). Functions in the replication stress response by protecting DNA at stalled replication forks from MRE11-mediated degradation. Mechanistically, inhibits RAD51 ATPase activity to stabilize RAD51 on stalled replication forks (PubMed:38459011). Additionally, directly recruits and later releases MRE11 at DNA damage sites during the homology-directed repair (HDR) process (PubMed:34348893).
Belongs to the GRB2/sem-5/DRK family.
Phosphorylation of Tyr-209 in the C-terminal SH3 domain reduces its binding to SOS1.
The GRB2 protein also known as growth factor receptor-bound protein 2 is instrumental in signal transduction. GRB2 has a molecular weight of about 25 kDa. It comprises one SH2 domain and two SH3 domains which facilitate its role in linking receptor tyrosine kinases to downstream signaling molecules. GRB2 is ubiquitously expressed in various tissues signifying its importance in diverse cellular functions.
GRB2 functions as an adaptor protein that connects activated receptor tyrosine kinases to intracellular pathways. It often forms complexes with other proteins such as the SOS protein which further propagates signaling cascades critical for cell proliferation and differentiation. GRB2’s ability to mediate these interactions contributes to cellular responses to external stimuli including growth factors and hormones.
GRB2 plays an important role in the Ras-MAPK signaling pathway. It interacts with proteins like SOS and Ras enabling signal transduction from the cell surface to the nucleus which is vital for processes such as cell growth and survival. GRB2 is also implicated in the PI3K-Akt pathway connecting it to another set of signaling proteins that regulate metabolism growth and survival.
GRB2 has significant associations with cancer and immune disorders. Aberrant activation of pathways involving GRB2 can lead to uncontrolled cell proliferation contributing to oncogenesis in different cancers. Additionally GRB2’s interactions with proteins like BCR-ABL in chronic myeloid leukemia highlight its potential role as a therapeutic target. GRB2 inhibitors could therefore offer promising avenues for treating such conditions by disrupting its pathological signaling interactions.
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