|GRB2 in Human Breast Cancer Tissue. GRB2 was detected in immersion fixed paraffin-embedded sections of human breast cancer tissue using 10 µg/mL Human GRB2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3846) overnight at 4 °C. Before incubation with the primary antibody tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
|Detection of Human/Mouse/Rat GRB2 by Western Blot. Western blot shows lysates of HEK293 human embryonic kidney cell line, Jurkat human acute T cell leukemia cell line, Balb/3T3 mouse embryonic fibroblast cell line, and NRK rat normal kidney cell line. PVDF membrane was probed with 1 µg/mL of Human/Mouse/Rat GRB2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3846) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for GRB2 at approximately 27 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
GRB-2 (growth factor receptor-bound protein 2), an adaptor protein involved in signal transduction, contains a central SH2 domain flanked by two SH3 domains. The SH2 domain binds to phosphotyrosine residues in RTKs such as PDGF and EGF, non-RTKs such as Bcr/Abl and FAK, and docking proteins such as FRS-2 and Gab1. The SH3 domains associate with proline rich motifs on the guanine nucleotide releasing factor, Sos, stimulating GTP binding to Ras, which in turn activates MAPK and other signaling pathways. GRB-2 also participates in the endocytosis of EGFR through its recruitment of Cbl. Tyrosine phosphorylation of GRB-2 SH3 domains reduces binding to Sos and negatively regulates downstream signaling pathways including Ras, JNK and MAPK.
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