(Gly14)-Humanin (human), sHNG, [Gly14]-HN peptide

(Gly14)-Humanin (human), sHNG, [Gly14]-HN peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

MAPRGFSCLLLLTGEIDLPVKRRA

H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Gly-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH

24

95.14%

C₁₁₈H₂₀₂N₃₄O₃₁S₂

2657.18

330936-70-4

Synthetic

Powder

(Gly14)-Humanin (human), also referred to as sHNG or [Gly14]-HN, is a synthetic derivative of Humanin (HN), a 24-residue peptide originally identified through functional expression screening for its ability to suppress neuronal cell death induced by familial Alzheimer's disease genes and amyloid beta (Aβ). The native HN sequence is MAPRGFSCLLLLTSEIDLPVKRRA. In sHNG, glycine is substituted for serine at position 14 (S14G). This single amino acid substitution significantly enhances the neuroprotective potency of the peptide. While native synthetic HN (sHN) requires micromolar concentrations to achieve full protection against neuronal death caused by mutant APP, presenilin-1, and presenilin-2 genes, sHNG is fully protective at nanomolar concentrations. sHNG also protects primary cortical neurons from Aβ-induced toxicity with similarly high potency, whereas the C8A mutant (sHNA) is inactive. The mechanism of action involves extracellular binding to specific cell-surface sites, triggering a tyrosine kinase-dependent signaling pathway that inhibits activation of procaspase-3, a key step in apoptosis. The protective effect is specific to Alzheimer's disease-relevant insults, as sHNG does not affect cell death caused by polyglutamine expansion (Q79) or mutant SOD1.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Hashimoto Y, Niikura T, Tajima H, Yasukawa T, Sudo H, Ito Y, Kita Y, Kawasumi M, Kouyama K, Doyu M, Sobue G, Koide T, Tsuji S, Lang J, Kurokawa K, Nishimoto I. A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Abeta. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6336-41. doi: 10.1073/pnas.101133498. Erratum in: Proc Natl Acad Sci U S A 2001 Oct 23;98(22):12854. PMID: 11371646; PMCID: PMC33469.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.