HIF-1 alpha (556-574) is a short hypoxia-inducible factor-1 (HIF-1) 19 residues fragment. HIF-1 functions as master regulator of response to oxygen homeostasis.
CAT No: R1421
CAS No:1201633-99-9
Synonyms/Alias:HIF-1 alpha 556-574;1201633-99-9;
HIF-1 alpha 556-574 is a synthetic peptide fragment derived from the C-terminal transactivation domain of hypoxia-inducible factor 1-alpha (HIF-1α), a key transcription factor involved in cellular adaptation to hypoxic stress. This peptide encompasses amino acids 556 to 574 of the HIF-1α protein, a region critical for mediating protein-protein interactions and post-translational modifications that regulate HIF-1α stability and activity. As an essential component of hypoxia signaling pathways, this peptide segment is frequently utilized in biochemical research to dissect HIF-1α-mediated gene regulation, protein binding dynamics, and the molecular mechanisms underlying cellular responses to low oxygen environments. Its defined sequence and biological relevance make it a valuable tool for investigating the functional domains of HIF-1α and their interactions with various cellular partners.
Protein-protein interaction studies: The HIF-1 alpha 556-574 peptide is widely used to probe and characterize interactions between HIF-1α and its regulatory partners, including coactivators, corepressors, and ubiquitin ligases. By serving as a defined binding motif, it enables detailed mapping of interaction sites and affinity measurements using techniques such as surface plasmon resonance, isothermal titration calorimetry, or pull-down assays. These studies help elucidate the molecular determinants of HIF-1α regulation, providing insights into how hypoxia-responsive transcriptional programs are modulated at the protein level.
Post-translational modification analysis: Researchers employ this peptide fragment as a substrate for in vitro assays aimed at studying post-translational modifications, such as hydroxylation, acetylation, and phosphorylation, that occur within the HIF-1α C-terminal domain. Using mass spectrometry or immunochemical approaches, the peptide serves as a model to identify modification sites, assess enzyme specificity, and quantify modification kinetics. Such analyses are critical for understanding how specific modifications influence HIF-1α stability, localization, and transcriptional activity under varying oxygen tensions.
Antibody validation and epitope mapping: The defined sequence of the HIF-1 alpha 556-574 peptide makes it an ideal standard for antibody generation, specificity testing, and epitope mapping. Researchers utilize the peptide to screen and validate antibodies targeting the C-terminal transactivation domain, ensuring reagent quality and selectivity for applications such as western blotting, immunoprecipitation, or immunofluorescence. Accurate antibody validation is essential for reliable detection and quantification of HIF-1α in complex biological samples.
Cell signaling pathway dissection: In mechanistic studies of hypoxia signaling, this peptide is used to competitively inhibit or mimic the activity of the corresponding region within the full-length HIF-1α protein. By introducing the peptide into in vitro or cell-based systems, investigators can assess the functional consequences of disrupting specific protein-protein interactions or signaling events. These experiments provide valuable data on the role of the 556-574 domain in mediating downstream gene expression, cofactor recruitment, or response to hypoxic stress.
Peptide-based assay development: The HIF-1 alpha 556-574 sequence is frequently incorporated into custom assay platforms designed to monitor HIF-1α activity, binding events, or enzymatic modifications. Its well-characterized structure and functional relevance enable the development of sensitive, quantitative assays for high-throughput screening or mechanistic studies. Such assay systems support drug discovery efforts targeting the HIF pathway, as well as fundamental research into the regulation of oxygen homeostasis at the molecular level.
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