Humanin
10 mg × 10 vials
For laboratory procurement

- Catalog number
- HU10
- Listed specification
- 10 mg
- Vials per pack
- 10 vials
- Test reports
- No report published for this SKU
- Current supply lot
- Lot documents with your quote
Compound profile
Humanin is a 24-residue peptide recorded under MT-RNR2 and examined in molecular studies of BAX and mitochondrial membranes.
Identity
- Sequence
H-MAPRGFSCLLLLTSEIDLPVKRRA-OH- Residues
- 24
- Molecular formula
- C119H204N34O32S2
- Average molecular weight
- 2687.2 g/mol
- Monoisotopic mass (calculated)
- 2685.4822 Da
- CAS number
- 330936-69-1
- PubChem CID
- 16131438
- Other names
- HN
The identity uses the 24-residue UniProt sequence. A shorter 21-residue form can result from mitochondrial-code translation; the endogenous source remains unresolved. The formula excludes counterions and N-formylation. An intact SMILES representation was not verified.
Identity data from: PubChem CID 16131438 · UniProtKB Q8IVG9
Research overview
Humanin is a short peptide whose 24-residue sequence is recorded in UniProt Q8IVG9. Work on its molecular interactions examined the BAX protein, a member of the BCL-2 family associated with mitochondrial membrane permeabilization. In the first cited study, investigators examined Humanin–Bax binding, the movement of Bax from the cytosol toward mitochondria, and cytochrome c release from isolated mitochondria. They also used small interfering RNA to examine the relationship between endogenous peptide expression and Bax localization. These experiments combined cellular observations with isolated-organellar assays, allowing several steps of the interaction to be considered separately [1].
The later study investigated how Humanin and BAX organize together at the protein level. Recombinant-protein experiments employed light scattering, circular dichroism, fluorescence spectroscopy and negative-stain electron microscopy. The authors observed fibers containing both molecules and described changes in the secondary and tertiary structure of BAX. Its membrane-associated C-terminal helix was implicated in fiber formation, while Humanin mutations changed fiber morphology. This gives a specific in vitro model of molecular association. It should be distinguished from identifying the physiological source of Humanin or assuming that the same assembly occurs in every cellular environment [2].
Laboratory storage and handling
Keep the sealed vial cold, dry and protected from light, following the conditions in the documentation supplied with the lot. Let the vial reach room temperature before opening to limit moisture condensation. Avoid repeated freezing and thawing of laboratory stocks. Record the lot identifier and the material form with each experiment, and use standard laboratory protective equipment.
Questions about Humanin
Which Humanin form does this identity describe?
The identity describes the 24-residue sequence in UniProt Q8IVG9. The record also discusses a shorter form and uncertainty about the endogenous source of the peptide.
What was examined with isolated mitochondria?
The original study examined Bax association with isolated mitochondria and cytochrome c release alongside cell-based observations of Bax localization and Humanin expression [1].
How were Humanin–BAX fibers examined?
The later work combined recombinant-protein experiments with spectroscopy, light scattering and electron microscopy. It examined fiber organization and changes in BAX structure in vitro [2].
References
- Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature 2003. PMID 12732850
- Humanin induces conformational changes in the apoptosis regulator BAX and sequesters it into fibers, preventing mitochondrial outer-membrane permeabilization. J Biol Chem 2019. PMID 31690630
Identity data checked on 2026-10-03. Literature summaries describe published research models and are not specifications of any product lot.
Compare specifications
1 catalog entryTest reports
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