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OriGene
human grb2 ![]() Human Grb2, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/human+grb2+variant+1+cdna/GRB2+%2F+ASH+(1-217%2C+His-tag)+Human+Protein/pm24697349-46-0-18 Average 90 stars, based on 1 article reviews
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OriGene
human grb2 variant 1 cdna ![]() Human Grb2 Variant 1 Cdna, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/human+grb2+variant+1+cdna/GRB2+(NM_203506)+Human+Tagged+ORF+Clone/pmc03074567-231-8-14 Average 90 stars, based on 1 article reviews
human grb2 variant 1 cdna - by Bioz Stars,
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Image Search Results
Journal: Biochemistry
Article Title: Recruitment of the adaptor protein Grb2 to EGFR tetramers.
doi: 10.1021/bi500182x
Figure Lengend Snippet: Figure 1. Proteins (EGF, EGFR, and Grb2), EGFR component states, and protein−protein interfaces considered in our computational model. The EGFR ectodomain is taken to be free or bound to EGF. A cytoplasmic domain of EGFR, comprising the juxtamembrane region (JM) and kinase domain, is taken to be locked (i.e., unavailable for interaction) or freed (i.e., available for interaction). The C-terminal tail of EGFR is taken to contain, as a simplification, a single docking site for Grb2, which can be unphosphorylated (Y) and inactive or phosphorylated (pY) and active.
Article Snippet:
Techniques:
Journal: Biochemistry
Article Title: Recruitment of the adaptor protein Grb2 to EGFR tetramers.
doi: 10.1021/bi500182x
Figure Lengend Snippet: Figure 2. Illustration of the rules for interactions in our computational, rule-based model. The model, which captures the mass-action chemical kinetics of the indicated interactions, consists of 16 rules, which are either reversible (and associated with two rate constants) or unidirectional (and associated with a single rate constant). Each rule represents an interaction. The glyphs used here to represent proteins and protein components are the same as those presented in Figure 1. Here, in illustrating a rule, we use a question mark (?) to indicate a missing protein component or component state that is not depicted explicitly; the missing component or state is taken to have zero influence on the interaction represented by the rule. Similarly, representation of an EGFR ectodomain by a dotted triangle is meant to indicate that the ectodomain may or may not be present in a complex, without influence on the interaction of concern. The model is the same as that presented in our earlier report25 except that a rule for Grb2 binding to phosphorylated EGFR has been added. This rule is illustrated in the lower left box.
Article Snippet:
Techniques: Binding Assay
Journal: Biochemistry
Article Title: Recruitment of the adaptor protein Grb2 to EGFR tetramers.
doi: 10.1021/bi500182x
Figure Lengend Snippet: Figure 4. FLIM data of individual living BaF/3 cells represented on a phasor diagram. Data points correspond to BaF/3 cells transfected with EGFR−eGFP alone (blue diamond), EGFR−eGFP + EGF (second blue diamond), EGFR−eGFP/Grb2−mRFP (red-filled diamond), EGFR−eGFP/Grb2−mRFP + EGF (red-filled triangle), and untransfected control cells (blue filled circle). Blue solid line denotes trajectory for mixtures of background and EGFR−eGFP. Red line indicates trajectory for EGFR−eGFP/Grb2−mRFP FRET complex mixing with background and EGFR−eGFP fluorescence.
Article Snippet:
Techniques: Transfection, Control
Journal: Biochemistry
Article Title: Recruitment of the adaptor protein Grb2 to EGFR tetramers.
doi: 10.1021/bi500182x
Figure Lengend Snippet: Figure 3. FLIM data of living BaF/3 cell populations represented on a phasor diagram. (A) Phasor diagram over a limited data range. (B) Phasor diagram on an expanded scale. Individual data points represent the cell-phasor components [x = m cos(φ); y = m sin(φ)] averaged from >20 cells. Data points correspond to BaF/3 cells transfected with EGFR−eGFP alone (blue diamond), EGFR−eGFP + EGF (second blue diamond), EGFR−eGFP/Grb2−mRFP (red-filled diamond), EGFR−eGFP/Grb2−mRFP + EGF (red-filled triangle), and un- transfected control cells (blue filled circle).
Article Snippet:
Techniques: Transfection, Control
Journal: Biochemistry
Article Title: Recruitment of the adaptor protein Grb2 to EGFR tetramers.
doi: 10.1021/bi500182x
Figure Lengend Snippet: Figure 5. FRET−FLIM−ICS on living BaF/3 cells cotransfected with EGFR−eGFP and Grb2−mRFP. (A) Fluorescence image of EGFR− eGFP/Grb2−mRFP complexes. (B) Spatial autocorrelation image of EGFR−eGFP/Grb2−mRFP complexes. (C) Density of Grb2−mRFP- bound EGFR−EGFP clusters as a function of the density of Grb2− free EGFR−eGFP clusters. The solid line is fit to a Hill function (CDbound = A/(1 + ((Kd/CDfree)(N−1)), with N = 4.1, A = 27, and Kd = 18 clusters).
Article Snippet:
Techniques: Fluorescence
Journal: Biochemistry
Article Title: Recruitment of the adaptor protein Grb2 to EGFR tetramers.
doi: 10.1021/bi500182x
Figure Lengend Snippet: Figure 6. (A) Plot of simulation results depicting the cluster distribution of Grb2-bound EGFR as a function of EGF concentration. Note that at all concentrations of EGF the EGFR tetramer is the predominant form associated with Grb2. The curves corresponding to dimer and trimer are indistinguishable from monomer because the total number of these oligomeric forms bound to Grb2 is almost negligible. (B) Cluster size distribution of EGFR bound to Grb2 and unbound (free) to Grb2 from simulation with 10 nM EGF.
Article Snippet:
Techniques: Concentration Assay