Research Peptide

Snap 8

SNARE-Related Octapeptide · MW 1,075.2 g/mol

Snap 8 is an acetylated octapeptide studied as a SNARE-complex-related research peptide in neuromuscular junction, vesicle-release, and cosmetic biochemistry models. Laboratory research focuses on peptide interaction with SNAP-25-related pathways and neurotransmitter-release assays.

≥99% HPLC MS Confirmed 3rd Party Tested San Diego
Overview

What is Snap 8?

Snap 8 is an acetylated octapeptide studied as a SNARE-complex-related research peptide in neuromuscular junction, vesicle-release, and cosmetic biochemistry models. Laboratory research focuses on peptide interaction with SNAP-25-related pathways and neurotransmitter-release assays.

Snap 8 (Acetyl Octapeptide-3) is supplied strictly as a reference material for in vitro and preclinical investigation. All characterization data described here is drawn from peer-reviewed literature and laboratory analysis; nothing herein constitutes a claim of clinical effect in humans.

Investigational Scope

Documented Research Areas

The following domains summarize directions explored across published studies and laboratory models. Each reflects observations reported in rodent models, in vitro systems, or the peer-reviewed record.

SNARE Biology

Vesicle Release Models

Snap 8 is studied in models related to SNARE complex assembly and regulated vesicle release.

Neuromuscular

Neurotransmitter Release Assays

Research examines peptide effects on exocytosis-associated pathways and neuromuscular signaling markers.

Cosmetic Science

Expression Line Models

In vitro cosmetic biochemistry studies evaluate peptide activity in skin and muscle-contraction signaling models.

Peptide Design

SNAP-25 Mimetic Research

Snap 8 is used as a designed peptide analogue for examining sequence-specific interaction with SNARE-related proteins.

Proposed Mechanism

Mechanistic Pathway

Mechanistic steps below are hypothesized from in vitro assays and animal-model data reported in the literature. They describe biochemical interactions observed under controlled experimental conditions.

  1. 1

    SNAP-25 Motif Mimicry

    The peptide is designed from SNAP-25-related sequence motifs and is studied for interference with SNARE complex dynamics.

  2. 2

    Exocytosis Pathway Modulation

    Research models examine whether the peptide alters vesicle docking or release-associated protein interactions.

  3. 3

    Acetylated Peptide Stability

    N-terminal acetylation is used in peptide design to influence stability and biochemical handling in assay systems.

  4. 4

    Localized Signaling Models

    Studies focus on controlled topical or cell-culture systems rather than systemic receptor pharmacology.

Technical Data

Molecular Specifications

Amino Acid SequenceAc-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2
Molecular Weight1,075.2 g/mol
Molecular FormulaC41H70N16O16S
CAS Number868844-74-0
Storage-20°C long-term, protected from moisture
References

Selected Literature

The following peer-reviewed references informed the research summaries on this page. Citations are provided for scientific context only.

  1. Blanes-Mira C, et al. (2002). A synthetic hexapeptide that inhibits neurotransmitter release and reduces wrinkles. International Journal of Cosmetic Science, 24(5), 303-310.
  2. Gutierrez LM, et al. (1997). A peptide that mimics the C-terminal domain of SNAP-25 blocks Ca2+-dependent exocytosis. FEBS Letters, 409(3), 393-397.
  3. Jahn R & Scheller RH. (2006). SNAREs: engines for membrane fusion. Nature Reviews Molecular Cell Biology, 7(9), 631-643.
  4. Söllner T, et al. (1993). SNAP receptors implicated in vesicle targeting and fusion. Nature, 362(6418), 318-324.
  5. Wickelgren I. (2003). Cosmetic neuroscience: peptides and neuromuscular signaling. Science, 299(5611), 1325.

Research Disclaimer

This product is intended strictly for laboratory research purposes only. It is not a drug, food, cosmetic, or dietary supplement and is not intended to diagnose, treat, cure, or prevent any disease. It is not for human or animal consumption. All information presented is derived from published scientific literature and is provided for educational reference only. By purchasing, the buyer affirms they are a qualified researcher or institution and assume full responsibility for the safe and lawful handling of this material.