SNAP-8 is a synthetic peptide derived from SNAP-25, a key protein involved in synaptic vesicle fusion and neurotransmitter release.
The peptide has attracted attention in biochemical research due to its interaction with signalling pathways related to cellular communication and protein complexes.
Its role in modulating components of the SNARE complex has made it a subject of interest in studies exploring neurotransmission and intracellular signalling.
QUICK PEPTIDE OVERVIEW
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Property
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Information
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Peptide Name
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SNAP-8
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Full Name
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Acetyl Octapeptide-3
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Peptide Type
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Synthetic peptide fragment
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Amino Acid Length
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8 amino acids
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Molecular Formula
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(Sequence-dependent)
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Molecular Weight
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~1075 g/mol (approx.)
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Research Category
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Neuro / Cellular Signalling Research
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CHEMICAL PROPERTIES & MOLECULAR DATA
Understanding the molecular characteristics of SNAP-8 is important for researchers studying protein interactions and cellular signalling pathways.
SNAP-8 is a short peptide fragment derived from SNAP-25, designed to interact with protein complexes involved in vesicle transport and membrane fusion.
Peptides that interact with these systems are of interest in research because they can influence cellular communication and signalling dynamics.
Ongoing studies continue to investigate how peptide fragments such as SNAP-8 affect intracellular processes and protein interactions.
WHAT IS SNAP-8?
SNAP-8 is a synthetic peptide developed from a fragment of SNAP-25, a protein involved in synaptic signalling.
In research environments, it is studied for its interaction with protein complexes responsible for neurotransmitter release and vesicle fusion.
Its role in cellular communication pathways has made it a valuable subject in laboratory investigations of signalling mechanisms.
MECHANISM OF ACTION
In laboratory studies, SNAP-8 is investigated for its interaction with the SNARE protein complex.
Research suggests the peptide may influence biological processes associated with:
- vesicle fusion mechanisms
- neurotransmitter release pathways
- SNARE complex interaction
- cellular communication signalling
These mechanisms are studied to better understand how protein interactions regulate signalling at the cellular level.
AREAS OF SCIENTIFIC RESEARCH
Due to its interaction with protein complexes and signalling pathways, SNAP-8 is studied across several areas of research.
Common research topics include:
- neurobiology studies
- synaptic signalling research
- protein interaction analysis
- cellular communication pathways
- vesicle transport mechanisms
These research areas continue to expand as scientists investigate the role of peptide fragments in regulating biological systems.
RECONSTITUTION OF SNAP-8
In research environments, SNAP-8 is typically supplied as a lyophilised (freeze-dried) peptide to maintain stability.
Before use, the peptide is reconstituted using a suitable sterile research solvent.
The solvent is generally introduced slowly along the vial wall to allow gradual dissolution. Gentle swirling may assist the process, while vigorous shaking is typically avoided to preserve peptide integrity.
Researchers calculate concentrations prior to preparation to ensure consistency within experimental protocols.
STORAGE OF SNAP-8
Proper storage conditions are essential for maintaining peptide stability.
Lyophilised SNAP-8 is typically stored in cool, dry environments, often under refrigeration or freezing conditions.
Protection from moisture, light exposure, and temperature fluctuations helps minimise degradation.
Once reconstituted, solutions are generally stored at low temperatures and handled according to standard laboratory practices.
SUMMARY
SNAP-8 is a synthetic peptide fragment derived from SNAP-25, studied in research for its interaction with protein complexes involved in cellular signalling and neurotransmission.
Its role in modulating vesicle fusion and communication pathways makes it an important subject in neurobiology and intracellular signalling research.
As scientific investigation continues, SNAP-8 contributes to a deeper understanding of protein interactions and cellular communication systems.