pp60(v-SRC) Autophosphorylation Site, Phosphorylated

Product Name: pp60(v-SRC) Autophosphorylation Site, Phosphorylated

Sequence One Letter Code: RRLIEDNE-pY-TARG

Sequence Three Letter Code: H-Arg-Arg-Leu-Ile-Glu-Asp-Asn-Glu-pTyr-Thr-Ala-Arg-Gly-OH

Chemical Formula:C66H110N23O26P

Molecular Weight: 1672.8

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: RSV

Conjugation: Unconjugated

Code Nacres: NA.26

Application: pp60(v-SRC) Autophosphorylation Site, Phosphorylated is a synthetic phosphotyrosine-containing peptide corresponding to the autophosphorylation motif of the Rous sarcoma virus–encoded Src oncoprotein. This sequence represents the activated signaling state of Src family kinases and serves as a defined ligand for SH2 domain–mediated interactions. The peptide is widely used in binding assays, antibody validation, and studies of tyrosine kinase–dependent signal transduction. It provides a controlled platform for investigating phosphorylation-dependent protein–protein interactions and oncogenic Src signaling mechanisms in cancer biology research.

Current Research: pp60(v-SRC) Autophosphorylation Site, Phosphorylated is a synthetic phosphotyrosine-containing peptide corresponding to the autophosphorylation motif of the Rous sarcoma virus–encoded Src oncoprotein (v-Src). This sequence represents the activated state of Src family kinases (SFKs), in which autophosphorylation at a key tyrosine residue enhances catalytic activity and creates a docking site for SH2 domain–containing signaling proteins. As a defined phosphopeptide, it provides a precise experimental tool for studying phosphorylation-dependent protein–protein interactions and tyrosine kinase–mediated signal transduction. Src Family Kinase Activation Src family kinases are non-receptor tyrosine kinases that regulate cell proliferation, adhesion, migration, and survival. In the activated state, Src undergoes autophosphorylation at a conserved tyrosine residue within its activation loop (corresponding to Tyr416 in c-Src). This phosphorylation event stabilizes the kinase in an open conformation, increases catalytic efficiency, and promotes recruitment of downstream signaling partners. The v-Src oncoprotein, encoded by Rous sarcoma virus, lacks normal regulatory control mechanisms and remains constitutively active. Its persistent autophosphorylation and downstream signaling drive oncogenic transformation, making Src signaling a central model in cancer biology. SH2 Domain Recognition Phosphorylated tyrosine motifs function as high-affinity ligands for Src homology 2 (SH2) domains. The pp60(v-SRC) autophosphorylation site peptide reproduces this phosphotyrosine-containing motif, allowing controlled study of SH2-mediated interactions in isolation from full-length proteins. This peptide is widely used to: Characterize SH2 domain binding specificity Quantify binding affinity in fluorescence polarization or surface plasmon resonance (SPR) assays Evaluate competitive inhibition of SH2–phosphotyrosine interactions Study signal complex assembly downstream of activated Src Because SH2 domain engagement is central to propagation of tyrosine kinase signaling, this peptide provides a clean and reproducible interaction platform. Applications in Cancer Signaling Research Src activation contributes to tumor cell proliferation, invasion, angiogenesis, and metastasis. Persistent phosphorylation at the activation loop correlates with enhanced oncogenic signaling. The phosphorylated autophosphorylation motif is therefore a valuable tool for investigating: Tyrosine kinase signaling cascades Adaptor protein recruitment (e.g., Grb2, Shc) Downstream MAPK and PI3K pathway activation Mechanisms of Src-driven transformation In experimental systems, the peptide supports mechanistic dissection of phosphorylation-dependent complex formation independent of kinase catalytic activity. Antibody Validation and Assay Development Phospho-specific antibodies targeting activated Src require validation against defined phosphorylated epitopes. This peptide serves as a positive control in: Western blot and ELISA validation workflows Immunoprecipitation assay optimization Phosphotyrosine antibody specificity testing Competitive binding assays Its defined phosphotyrosine residue ensures consistent and reproducible assay performance. Experimental Advantages Contains authentic Src activation-loop phosphotyrosine motif Represents activated kinase signaling state Suitable for SH2 domain binding studies Useful in antibody validation and assay calibration Enables mechanistic analysis of phosphorylation-dependent interactions Research Significance pp60(v-SRC) Autophosphorylation Site, Phosphorylated provides a controlled and well-defined model for studying Src activation and phosphotyrosine-mediated signaling. By isolating the key activation-loop motif, it enables precise investigation of SH2-dependent protein recruitment and oncogenic signal propagation. Its utility in binding assays, antibody validation, and mechanistic cancer research makes it a foundational reagent in studies of tyrosine kinase–driven transformation and signal transduction.