When exploring advanced biochemical research, one frequently encounters the term pt 161 peptide, often conflated with various synthetic compounds in literature. It is essential to clarify that in scientific databases, the primary subject of interest is ATN-161, a well-documented five-amino acid peptide that serves as a focal point for researchers studying cell signaling and receptor dynamics.
The Biochemical Profile of ATN-161
ATN-161 is a non-RGD based integrin binding peptide derived from the synergy region of fibronectin. Its chemical structure, often noted as Ac-PHSCN-NH2, makes it a specialized tool for laboratory investigations. Unlike standard RGD motifs, this small peptide antagonist of integrin alpha5beta1 interacts specifically with the N-terminus of the beta-1 region, which is a critical area of focus for those analyzing angiogenesis and cellular migration.
As someone who tracks peptide research, I find the specificity of the PHSCN peptide (licensed as ATN-161) to be particularly fascinating. It acts as an alpha v beta 1 inhibitor and is recognized as a novel integrin alpha5beta1 antagonist. Because it selectively binds to and blocks the receptor for integrin, it has been a frequent subject in studies regarding the inhibition of tumor growth, angiogenesis, and metastasis.
E-E-A-T and Research Integrity
When reviewing data on The Integrin Binding Peptide, ATN-161, it is vital to rely on peer-reviewed literature and high-quality chemical suppliers. Many of the studies cited in academic repositories, such as PubMed, underscore the importance of purity and structural integrity in these compounds. Whether you are looking ATN 161 peptide at the Bcl-2-like protein 11 142-161 or the SHBG141–161 peptide, the nomenclature can be confusing. However, ATN 161 is a α5β1 integrin receptor antagonist that remains distinct from other epitope markers.
Key Technical Specifications
* Molecular Composition: Five-amino acid sequence (Ac-PHSCN-NH2).
* Primary Function: Integrin receptor antagonism (specifically α5β1 and αvβ3).
* Research Appl SHBG141–161 peptide ication: Investigated for antiangiogenic properties and cell a by W Wang · 2011 · Cited by 68 — This study evaluated the antiangiogenic effects of ATN-161, a small peptide inhibitor of integrin α5β1, in human choroidal endothelial cells (hCECs) and in dhesion inhibition.
* Synthesis: Often produced via squaric acid-mediated synthesis in ATN-161 peptide functionalized reversibly crosslinked materials.
Observations on Experimental Use
In my experience analyzing laboratory reports, the distinction between ATN-161 and other compounds with "161" in their name—such as Tb-161 (a radionuclide) or MAGE-1 Antigen (161-169)—is paramount. A Phase 1 Trial of the Antiangiogenic Peptide ATN-161 highlighted its potential in modulating biological pathways, yet it is crucial to remember that these are strict ATN-161 is a non-RGD based integrin binding peptide derived from the synergy region of fibronectin that inhibits the receptors for integrins alpha-v beta-3 and ly for controlled research environments.
The Integrin-binding peptide ATN-161 is frequently utilized in murine models to evaluate its capacity to reduce liver metastasis. Its role as a non-competitive inhibitor of the fibronectin synergy site is what sets it apart from traditional antagonists.
Conclusion
Whether you are a student of biochemistry or a researcher focusing on cellular signaling, understanding the nuance of ATN-161 is key. It is not merely a number; it is a meticulously designed five amino acid peptide, ATN 161, that provides significant value in the study of integrin-mediated ATN-161 Peptide Functionalized Reversibly Cross-Linked processes. Always ensure that when sourcing these Product Description. ATN 161 is a α5β1 integrin receptor antagonist. Reduces liver metastasis and improves survival in combination with 5-FU (Cat. No. materials, you prioritize suppliers who provide comprehensive HPLC analysis to confirm the iden The Integrin Binding Peptide, ATN-161, as a Novel - PubMed tity and purity of the peptide. By focusing on the verified mechanisms of this small peptide antagonist of integrin alpha5beta1, we can better appreciate the complex nature of protein-protein interactions in experimental settings.