Humanin is an endogenous peptide that exhibits anti-apoptotic and neuroprotective activities. Humanin is overexpressed in some cancers and could possibly be used as a biomarker.
CAT No: R1848
CAS No:330936-69-1
Synonyms/Alias:Humanin;330936-69-1;formyl humanin;Protein Humanin (human);HUMANIN TRIFLUOROACETATE;1-24-Protein humanin (human);Protein (human clone 1 humanin sequence homolog);DTXSID70186749;T lymphocyte activation-associated protein PRO86272 (human);1-24-Protein humanin;GTPL1047;CHEMBL4447799;DTXCID60109240;PHN-4384-V;MFCD04118086;Humanin (human) trifluoroacetate salt;AT42451;DA-74322;Humanin (human) trifluoroacetate (H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH);L-Alanine, L-methionyl-L-alanyl-L-prolyl-L-arginylglycyl-L-phenylalanyl-L-seryl-L-cysteinyl-L-leucyl-L-leucyl-L-leucyl-L-leucyl-L-threonyl-L-seryl-L- alpha-glutamyl-L-isoleucyl-L-alpha-aspartyl-L-leucyl-L-prolyl-L-valyl-L-lysyl-L-arginyl-L-arginyl-;L-Alanine, L-methionyl-L-alanyl-L-prolyl-L-arginylglycyl-L-phenylalanyl-L-seryl-L-cysteinyl-L-leucyl-L-leucyl-L-leucyl-L-leucyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-isoleucyl-L-alpha-aspartyl-L-leucyl-L-prolyl-L-valyl-L-lysyl-L-arginyl-L-arginyl-;Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala;
Humanin is a mitochondrial-derived peptide that has garnered significant interest in the biochemical research community due to its unique sequence, evolutionary conservation, and multifaceted biological activities. As a small, bioactive peptide originally identified in human brain tissue, Humanin is notable for its role in modulating cellular stress responses and interacting with various intracellular and extracellular targets. Its ability to influence mitochondrial function and cytoprotective signaling pathways makes it a valuable molecular tool for investigating cellular homeostasis, aging, and neurobiology. The functional versatility of Humanin has positioned it as a key reagent in studies exploring peptide signaling, mitochondrial biology, and cellular protective mechanisms.
Peptide signaling studies: Humanin is widely employed in research elucidating the mechanisms of peptide-mediated intracellular and intercellular communication. Its interactions with specific cell surface receptors and intracellular binding partners provide a model system for dissecting the molecular basis of peptide signaling. Investigators utilize this peptide to probe receptor-ligand interactions, map binding motifs, and characterize downstream signaling cascades relevant to cellular survival and stress adaptation.
Mitochondrial function analysis: The peptide's mitochondrial origin and its regulatory influence on mitochondrial processes make it an important tool for studying mitochondrial dynamics, bioenergetics, and quality control. Researchers leverage Humanin to investigate how mitochondrial-derived peptides participate in the maintenance of mitochondrial integrity, the regulation of apoptosis, and the modulation of reactive oxygen species production. Such studies advance understanding of mitochondrial communication with the rest of the cell and the broader implications for cellular metabolism.
Cellular stress and apoptosis research: Humanin is frequently used to model cellular responses to oxidative stress, endoplasmic reticulum stress, and other cytotoxic insults. Its ability to interact with pro-apoptotic and anti-apoptotic proteins enables detailed examination of the molecular checkpoints governing cell fate decisions. By incorporating this peptide into experimental systems, scientists can delineate the pathways by which cells resist or succumb to apoptotic stimuli, providing insights into stress adaptation and survival mechanisms.
Neurobiology and aging studies: Owing to its initial discovery in neural tissue and its demonstrated protective effects in neuronal models, Humanin serves as a critical reagent in neurobiological research. It is utilized to investigate mechanisms underlying neuroprotection, synaptic maintenance, and age-associated cellular decline. The peptide's influence on neural cell signaling and its potential to modulate processes implicated in cognitive function make it a valuable asset for studies of neurodegeneration and aging biology.
Peptide structure-function analysis: Humanin's relatively short amino acid sequence and well-characterized activity profile render it an excellent candidate for structure-function relationship studies. Researchers employ synthetic analogs, mutational variants, and labeling strategies to probe the contributions of individual residues to biological activity and receptor specificity. These investigations not only deepen understanding of Humanin's mode of action but also inform broader principles of peptide design and functional optimization for research applications.
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