EGF Receptor Substrate 2 [DADE-pY-LIPQQG], Biotinylated

Product Name: EGF Receptor Substrate 2 [DADE-pY-LIPQQG], Biotinylated

Sequence One Letter Code: Biotin-DADE-pY-LIPQQG

Sequence Three Letter Code: Biotin-Asp-Ala-Asp-Glu-pTyr-Leu-Ile-Pro-Gln-Gln-Gly-OH

Chemical Formula:C64H96N15O26PS

Molecular Weight: 1554.7

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: peptide substrate

Source / Species: Mammal

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: EGF Receptor Substrate 2 is a biotinylated phosphopeptide derived from the EGFR autophosphorylation site at Tyr992 and optimized for protein tyrosine phosphatase assays. This labeled peptide serves as an efficient substrate for mammalian protein tyrosine phosphatase 1B (PTP1B), exhibiting a Km of approximately 3.9 µM, and is also dephosphorylated by Yersinia PTP. Enzymatic removal of the phosphate group produces a marked increase in intrinsic fluorescence, enabling direct monitoring with excitation at 282 nm and emission at 305 nm. The biotin tag facilitates affinity capture, immobilization, and flexible assay configuration in microplate-based formats. EGF Receptor Substrate 2 is widely used for phosphatase kinetics, inhibitor screening, and mechanistic studies of tyrosine dephosphorylation. It supports research into signal attenuation pathways, metabolic regulation involving PTP1B, and the development of phosphatase-targeted therapeutic strategies.

Current Research: EGF Receptor Substrate 2 is a biotinylated phosphopeptide derived from the epidermal growth factor receptor (EGFR) autophosphorylation site at Tyr992, specifically optimized for protein tyrosine phosphatase (PTP) assays. This sequence reproduces a physiologically relevant phosphorylation motif while incorporating features that enhance assay sensitivity and versatility. As a result, it provides a reliable biochemical substrate for investigating tyrosine dephosphorylation mechanisms in both purified enzyme systems and inhibitor screening platforms. The peptide functions as an efficient substrate for mammalian protein tyrosine phosphatase 1B (PTP1B), a key regulator of receptor tyrosine kinase signaling and metabolic pathways. With a Km of approximately 3.9 µM for PTP1B, the substrate supports accurate kinetic characterization under physiologically meaningful conditions. In addition to mammalian phosphatases, it is also dephosphorylated by Yersinia PTP, enabling comparative analyses across distinct phosphatase families and facilitating studies of conserved catalytic mechanisms. A defining feature of EGF Receptor Substrate 2 is its fluorescence-based detection capability. Upon enzymatic removal of the phosphate group from the tyrosine residue, the peptide exhibits a marked increase in intrinsic fluorescence. This change can be monitored directly, with excitation at 282 nm and emission at 305 nm, allowing real-time or endpoint measurement of dephosphorylation without the need for secondary reagents or coupled detection systems. The intrinsic fluorescence shift provides a convenient and quantitative readout of phosphatase activity, improving assay efficiency and reducing experimental complexity. The incorporation of a biotin tag further enhances the flexibility of this substrate. Biotin enables affinity capture via streptavidin-coated surfaces, supporting immobilization strategies in microplate-based assays or surface-binding formats. This feature allows for adaptable assay design, including wash-based protocols, multiplexed detection systems, or integration with high-throughput screening workflows. Immobilization can also facilitate separation of substrate and enzyme components when required for downstream analytical applications. EGF Receptor Substrate 2 is widely employed in kinetic analyses to determine catalytic parameters such as Km, Vmax, and turnover rates for PTP1B and related phosphatases. These measurements are essential for understanding substrate specificity, catalytic efficiency, and regulatory modulation. The peptide’s defined structure ensures reproducibility across experiments and enables consistent comparison of enzyme variants, including catalytically impaired mutants or regulatory domain modifications. In pharmacological research, this substrate plays an important role in inhibitor screening campaigns. PTP1B has been extensively investigated as a therapeutic target in metabolic disorders, including type 2 diabetes and obesity, due to its role in attenuating insulin receptor signaling. By providing a sensitive and quantitative assay platform, EGF Receptor Substrate 2 supports evaluation of small-molecule phosphatase inhibitors and characterization of their potency and mechanism of action. The intrinsic fluorescence response allows rapid identification of inhibitory effects in microplate-based formats suitable for medium- to high-throughput screening. Beyond metabolic regulation, tyrosine dephosphorylation is central to signal attenuation in growth factor pathways. EGFR signaling must be tightly controlled to prevent aberrant proliferation and oncogenic transformation. By modeling dephosphorylation at the Tyr992 site, this substrate contributes to mechanistic studies examining how phosphatases modulate receptor activity and downstream signaling cascades. Overall, EGF Receptor Substrate 2 provides a versatile and sensitive tool for investigating protein tyrosine phosphatase activity. Its physiologically derived sequence, intrinsic fluorescence-based detection, and biotin-enabled assay flexibility make it well suited for kinetic studies, inhibitor development, and mechanistic exploration of tyrosine dephosphorylation pathways in metabolic and signaling research.