📡 Signaling

740 Y-P: Complete Guide

A phosphopeptide derived from IRS-1 protein that activates PI3K signaling. Studied in preclinical models for its role in insulin-like metabolic and proliferative pathways.

Signaling peptides play fundamental roles in cell-to-cell communication and intracellular pathways. 740 Y-P is being studied for its role in cellular signaling and potential research applications.

A phosphopeptide derived from IRS-1 protein that activates PI3K signaling. Studied in preclinical models for its role in insulin-like metabolic and proliferative pathways.

Also Known As

740Y-P

What is 740 Y-P?

740 Y-P is classified under the Signaling category of peptides. A phosphopeptide derived from IRS-1 protein that activates PI3K signaling. Studied in preclinical models for its role in insulin-like metabolic and proliferative pathways.

Mechanism of Action: PI3K activator that binds to the p85 regulatory subunit, mimicking receptor tyrosine kinase signaling to activate the PI3K/Akt pathway.

Cell Signaling Research

Primary Research Areas: Cell survival signaling, insulin sensitivity research, PI3K pathway studies, metabolic regulation.

Key Research Findings: Has been used extensively in cell biology research to activate PI3K signaling. Studies show it can promote cell survival and proliferation through Akt phosphorylation.

Safety Profile & Considerations

Research compound with limited in vivo safety data. PI3K activation must be carefully controlled as excessive signaling can promote abnormal cell growth.

Important Safety Notice: All information presented here is for educational purposes only. 740 Y-P should only be used under the guidance of qualified healthcare professionals or within properly controlled research settings. Individual responses to any compound can vary significantly.

Related Research Topics

Understanding 740 Y-P requires familiarity with these related concepts in signaling research. Each topic represents a broader field that intersects with current peptide research.

References & Further Reading

Derossi D, et al. Cell internalization of the third helix of Antennapedia homeodomain. J Biol Chem. 1996;271(30):18188-93.

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