GRB2 Rabbit Pab

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Leader in Biomolecular Solutions for Life Science GRB2 Rabbit pAb Catalog No.: A5689 Basic Information Background Catalog No. The protein encoded by this gene binds the epidermal growth factor receptor and A5689 contains one SH2 domain and two SH3 domains. Its two SH3 domains direct complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine Observed MW phosphorylated sequences. This gene is similar to the Sem5 gene of C.elegans, which is 33kDa involved in the signal transduction pathway. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene. Calculated MW 20kDa/25kDa Category Primary antibody Applications WB,IHC,IF Cross-Reactivity Human, Mouse Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 2885 P62993 IHC 1:50 - 1:200 Immunogen 1:10 - 1:100 IF Recombinant fusion protein containing a sequence corresponding to amino acids 1-217 of human GRB2 (NP_002077.1). Synonyms ASH;EGFRBP-GRB2;Grb3-3;MST084;MSTP084;NCKAP2;GRB2 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using GRB2 antibody (A5689) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 90s. Immunohistochemistry of paraffin- Immunofluorescence analysis of HeLa cells embedded mouse kidney using GRB2 using GRB2 antibody (A5689). Blue: DAPI antibody (A5689) at dilution of 1:100 (40x for nuclear staining. lens). Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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A Network Model of Early Events in Epidermal Growth Factor Receptor Signaling That Accounts for Combinatorial Complexity Michael L
BioSystems 83 (2006) 136–151 A network model of early events in epidermal growth factor receptor signaling that accounts for combinatorial complexity Michael L. Blinov, James R. Faeder, Byron Goldstein, William S. Hlavacek ∗ Theoretical Biology and Biophysics Group, Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA Received 8 January 2005; received in revised form 6 May 2005; accepted 21 June 2005 Abstract We consider a model of early events in signaling by the epidermal growth factor (EGF) receptor (EGFR). The model includes EGF, EGFR, the adapter proteins Grb2 and Shc, and the guanine nucleotide exchange factor Sos, which is activated through EGF- induced formation of EGFR–Grb2–Sos and EGFR–Shc–Grb2–Sos assemblies at the plasma membrane. The protein interactions involved in signaling can potentially generate a diversity of protein complexes and phosphoforms; however, this diversity has been largely ignored in models of EGFR signaling. Here, we develop a model that accounts more fully for potential molecular diversity by specifying rules for protein interactions and then using these rules to generate a reaction network that includes all chemical species and reactions implied by the protein interactions. We obtain a model that predicts the dynamics of 356 molecular species, which are connected through 3749 unidirectional reactions. This network model is compared with a previously developed model that includes only 18 chemical species but incorporates the same scope of protein interactions. The predictions of this model are reproduced by the network model, which also yields new predictions. For example, the network model predicts distinct temporal patterns of autophosphorylation for different tyrosine residues of EGFR.
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HER2 Stabilizes EGFR and Itself by Altering Autophosphorylation Patterns in a Manner That Overcomes Regulatory Mechanisms and Pr
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Paxillin: a Crossroad in Pathological Cell Migration Ana María López-Colomé*, Irene Lee-Rivera, Regina Benavides-Hidalgo and Edith López
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