autophosphorylation

The pp60 (v-SRC) Autophosphorylation Site, Phosphorylated is a phosphorylated peptide derived from an EGFR substrate, used as a critical tool for quantifying phosphorylated substrates in the screening of EGFR Kinase inhibitors.

Siamycin I is a tricyclic peptide originally isolated from Streptomyces and has antiviral and antibacterial activities. It is active against laboratory strains and clinical isolates of HIV-1 (ED50s = 0.05-0.45 and 0.89-5.7 μM, respectively), as well as the CBL-20 strain of HIV-2 (ED50 = 0.45 μM), in vitro. Siamycin I inhibits HIV-induced fusion of C8166 T cells with HIV-1-infected CEM-SS cells with an ED50 value of 0.08 μM. It is also active against B. subtilis, M. luteus, and S. aureus (MICs = 1.6-6.3 μg/ml). Siamycin I inhibits autophosphorylation of the E. faecalis quorum sensing kinase FsrC induced by gelatinase biosynthesis-activating pheromone (GBAP).

[pTyr5] EGFR (988-993) TFA, derived from the Tyr992 autophosphorylation site of the epidermal growth factor receptor (EGFR 988-993), often complexes with catalytically inactive protein-tyrosine phosphate 1B (PTP1B) [1].

EGF Receptor Substrate 2 (Phospho-Tyr5) is a biologically active peptide derived from an autophosphorylation site (Tyr992) of EGFR.