Angiogenin (108-122) TFA

Angiogenin (108-122) TFA is a synthetic peptide fragment corresponding to amino acids 108 through 122 of the human angiogenin protein, supplied as the trifluoroacetate (TFA) salt. As a segment derived from the C-terminal region of angiogenin, this peptide is of considerable interest in the study of protein-protein interactions, enzymatic activity mapping, and the functional dissection of angiogenic pathways. Researchers utilize such peptide fragments to elucidate sequence-specific roles within the full-length protein, supporting efforts to decode the molecular mechanisms underlying angiogenesis and related cellular processes. The defined sequence and synthetic origin of Angiogenin (108-122) TFA make it a valuable tool for controlled experimental approaches in biochemistry, cell biology, and peptide-based assay development.

Peptide mapping: Angiogenin (108-122) TFA is frequently employed in peptide mapping studies designed to identify functional domains within the parent angiogenin protein. By isolating and characterizing the activity of this specific segment, researchers can determine its contribution to the protein's overall biochemical properties, such as ribonuclease activity or receptor binding. This approach aids in pinpointing critical residues involved in angiogenin's biological functions, supporting the rational design of further mutagenesis or structure-function analyses.

Protein interaction studies: The peptide serves as a molecular probe in investigations of protein-protein and protein-ligand interactions. By introducing Angiogenin (108-122) into binding assays or surface plasmon resonance experiments, scientists can assess how this region interfaces with cellular receptors, extracellular matrix components, or regulatory proteins. Such studies provide insight into the mechanisms by which angiogenin modulates signaling pathways involved in cell migration, proliferation, and vascular development.

Antibody epitope mapping: Researchers utilize this peptide as a defined epitope for generating or characterizing antibodies against angiogenin. By employing Angiogenin (108-122) TFA in immunoassays, it is possible to map antibody binding sites, verify specificity, and optimize detection reagents for use in Western blotting, ELISA, or immunohistochemistry. This application is particularly valuable in the validation of antibody-based tools for basic research and analytical workflows.

Peptide-based assay development: The defined sequence and physicochemical properties of Angiogenin (108-122) TFA make it suitable for use as a standard or control in peptide-based assays. It can serve as a calibration reference in high-performance liquid chromatography (HPLC), mass spectrometry, or capillary electrophoresis methods developed to quantify or characterize angiogenin fragments in biological samples. This supports the development of robust, reproducible analytical protocols in proteomics and biomarker discovery.

Structure-activity relationship (SAR) studies: The peptide is instrumental in SAR investigations aimed at dissecting the relationship between sequence, structure, and biological activity within angiogenin. By synthesizing and testing Angiogenin (108-122) alongside related fragments or modified analogs, researchers can evaluate the impact of specific amino acid substitutions or truncations. Such studies inform the design of peptide mimetics, inhibitors, or functional probes for advanced research into angiogenic regulation and molecular recognition events.

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