Sermorelin 5mg and 10mg Laboratory Research Peptide - Protide Health
Sermorelin Price range: $55.00 through $105.00
Back to products

Snap-8 Peptide 10mg

$45.00

Snap 8 peptide 10mg product shot featuring a professionally labeled Protide Health 3mL research vial containing white to off-white lyophilized Acetyl Octapeptide-3 powder, with 10mg strength and research-use-only identification displayed against a clean laboratory-style background.

99.48%

SKU: PHIMP-PH-14380 Category:
Description

Snap 8 Peptide 10mg – Protide Health USA

Snap 8 Peptide Overview & Technical Specifications

Snap 8 peptide, commonly called SNAP-8 or Acetyl Octapeptide-3, is a synthetic N-acetylated and C-terminally amidated octapeptide based on the sequence:

Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂

Its abbreviated amino-acid sequence is:

EEMQRRAD

The compound was designed as a short peptide associated with laboratory investigation of SNARE-complex-related molecular interactions. Its structure contains eight amino-acid residues together with N-terminal acetylation and C-terminal amidation.

The supplied SNAP-8 PubChem reference represents the same elemental composition and sequence framework but uses DL/undefined stereochemical representation. For that reason, Protide Health does not use CID 86080331 as the definitive stereochemical identifier for the L-configured Ac-EEMQRRAD-NH₂ research material.

This snap 8 peptide is supplied as 10mg of 99% purity lyophilized material for biochemical assays, molecular interaction research, peptide characterization, and qualified preclinical experimentation.

Technical Specifications

  • Product Name: SNAP-8
  • Chemical Name: Acetyl Octapeptide-3
  • Quantity: 10mg
  • Form: Lyophilized powder
  • Vial Size: 3mL
  • Purity: 99%
  • Testing: HPLC-MS verified; third-party tested
  • Peptide Length: 8 amino acids
  • Sequence: Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂
  • One-Letter Sequence: EEMQRRAD
  • CAS Number: 868844-74-0
  • Molecular Formula: C41H70N16O16S
  • Molecular Weight: Approximately 1075.2 g/mol
  • Appearance: White to off-white lyophilized powder
  • Solubility: Soluble in water
  • Storage: Store sealed at ≤6°C and protected from heat, light, and moisture
  • Research Use: Biochemical, molecular, analytical, peptide-interaction, and qualified laboratory research only

Snap 8 Peptide Mechanism & Research Context

The proposed research rationale for snap 8 peptide centers on molecular interactions associated with the SNARE protein complex, a group of proteins involved in membrane-fusion and vesicle-release processes.

SNARE-associated signaling depends on highly coordinated interactions among proteins that facilitate membrane docking and fusion. Synthetic peptides modeled around portions of these signaling systems have been investigated as tools for studying peptide competition, molecular recognition, and neurotransmitter-release-associated mechanisms.

SNAP-8 was developed as an extended analogue within this broader peptide-design framework. However, direct peer-reviewed mechanistic evidence specifically isolating Acetyl Octapeptide-3 remains considerably more limited than the literature available for established endogenous SNARE proteins.

Researchers can review broader peptide and SNARE-related scientific literature indexed by PubMed when evaluating the biological context surrounding these experimental signaling systems.

Preclinical Research Applications

SNARE-Complex Molecular Research

The most relevant mechanistic area for snap 8 peptide is the study of SNARE-associated molecular interactions.

SNARE proteins participate in membrane fusion by forming tightly organized protein complexes. Short synthetic sequences can be studied experimentally to examine how peptide structure, charge distribution, and amino-acid composition influence protein–protein interactions.

SNAP-8 provides an eight-residue research model for controlled experiments involving these molecular hypotheses.

Peptide Structure-Activity Research

The peptide contains several chemically important features:

  • N-terminal acetylation
  • C-terminal amidation
  • Two glutamic-acid residues
  • Two arginine residues
  • Methionine and glutamine residues
  • An alanine-aspartic-acid terminal region

These structural characteristics affect charge distribution, solubility, molecular recognition, and possible interactions with experimental protein systems.

This makes the snap 8 peptide relevant to peptide structure–activity and molecular-interaction studies.

Acetylation and Amidation Research

Both termini of SNAP-8 are modified.

N-terminal acetylation removes the free N-terminal amino functionality, while C-terminal amidation changes the terminal carboxyl group into an amide.

These modifications can alter:

  • Net peptide charge
  • Proteolytic susceptibility
  • Molecular conformation
  • Peptide stability
  • Protein-binding behavior

Researchers should therefore distinguish Acetyl Octapeptide-3 from unmodified EEMQRRAD sequences when designing biochemical experiments.

Formulation and Material Research

Acetyl Octapeptide-3 has appeared in published research involving multi-ingredient experimental formulations.

For example, one study evaluated hyaluronic-acid microneedle patches containing several bioactive ingredients, including Acetyl Octapeptide-3. Because multiple compounds were present simultaneously, the results cannot establish an isolated effect for SNAP-8 itself.

This distinction is important when evaluating claims about snap 8 peptide benefits, because evidence from combination formulations cannot automatically be assigned to a single ingredient.

What Is Snap 8 Peptide?

Researchers asking what is snap 8 peptide are generally referring to Acetyl Octapeptide-3, the synthetic sequence Ac-EEMQRRAD-NH₂.

The molecule is an eight-amino-acid research peptide incorporating terminal acetylation and amidation.

It is commonly associated with experimental SNARE-complex research, but the strength of evidence differs substantially between theoretical mechanism, isolated biochemical studies, and finished multi-ingredient formulation studies.

Protide Health therefore describes SNAP-8 strictly according to laboratory and molecular research contexts rather than making cosmetic or therapeutic claims.

Snap 8 Peptide Benefits: What the Research Supports

The phrase snap 8 peptide benefits often appears in commercial cosmetic discussions, but such language can overstate what peptide-specific research demonstrates.

For scientific purposes, the more appropriate research areas include:

  • SNARE-associated molecular interactions
  • Peptide sequence characterization
  • Structure–activity relationships
  • Terminal modification research
  • Molecular stability
  • Protein-interaction models
  • Experimental formulation research

A published human study involving Acetyl Octapeptide-3 used a multi-component microneedle formulation containing several active ingredients. Because the investigation did not isolate SNAP-8, its findings cannot establish that Acetyl Octapeptide-3 alone caused the observed changes.

Accordingly, snap-8 peptide benefits should not be interpreted as established therapeutic, dermatological, anti-aging, or cosmetic effects of this research product.

Research Limitations

The evidence surrounding snap 8 peptide requires particularly careful interpretation.

Important limitations include:

  • Direct peer-reviewed research isolating SNAP-8 is limited.
  • Many mechanistic descriptions originate from peptide-design hypotheses related to SNARE signaling.
  • Results from formulations containing multiple active ingredients cannot establish the isolated contribution of SNAP-8.
  • Research on Acetyl Hexapeptide-8 should not automatically be applied to Acetyl Octapeptide-3.
  • Chemical similarity does not establish equivalent biological behavior.
  • Cosmetic ingredient studies do not establish therapeutic efficacy.
  • In-vitro or formulation findings should not be extrapolated into medical or clinical claims.

Protide Health therefore supplies this material strictly for controlled research and analytical use.

Literature & Citation Index

Efficacy of Bioactive Peptides Loaded on Hyaluronic Acid Microneedle Patches: A Monocentric Clinical Study

Journal: Journal of Cosmetic Dermatology
Year: 2019
PMID: 31134751
Research Context: Multi-active formulation containing Acetyl Octapeptide-3, other peptides, adenosine, and additional ingredients.

Important limitation: The formulation contained multiple active compounds, so this study does not establish an isolated SNAP-8 effect.

Chemical Identity Research Context

Chemical databases identify Acetyl Octapeptide-3 / SNAP-8 with the sequence:

Ac-EEMQRRAD-NH₂

and CAS:

868844-74-0

The L-configured peptide is chemically distinct from database entries using undefined or DL stereochemistry, even when elemental formulas appear identical.

Related Protide Health Research Products

Researchers investigating other short regulatory peptides can review the Selank 10mg research peptide for a structurally distinct heptapeptide research model.

The Tesamorelin, Ipamorelin, BPC-157 & TB-500 Research Bundle contains chemically distinct research peptides intended for separate experimental pathways.

Researchers can also examine the BPC-157, TB-500 & MOTS-c Research Bundle when comparing multi-peptide laboratory formulations.

These compounds have different sequences, structures, and experimental targets and should not be considered mechanistically interchangeable with SNAP-8.

Frequently Asked Questions

What is a Snap 8 peptide?

A snap 8 peptide is Acetyl Octapeptide-3, a synthetic eight-amino-acid peptide with the sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂.

Is SNAP-8 the same as Acetyl Octapeptide-3?

Yes. SNAP-8 is a commonly used name for Acetyl Octapeptide-3.

What is the SNAP-8 amino-acid sequence?

The sequence is:

Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂

The one-letter sequence is EEMQRRAD.

What does SNAP-8 research focus on?

Research interest primarily concerns peptide structure, SNARE-associated molecular hypotheses, terminal peptide modification, molecular interactions, and experimental formulation systems.

What does research say about Snap 8 peptide benefits?

Available research does not establish therapeutic or cosmetic benefits for this laboratory material. Some formulation studies have included Acetyl Octapeptide-3 alongside other ingredients, but those studies cannot isolate its individual contribution.

Is SNAP-8 the same as Acetyl Hexapeptide-8?

No. Acetyl Octapeptide-3 and Acetyl Hexapeptide-8 are chemically distinct peptides with different sequences. Findings for one should not automatically be attributed to the other.

What purity does Protide Health specify?

The supplied product specification states 99% purity, with HPLC-MS verification and third-party testing.

What form is SNAP-8 supplied in?

It is supplied as 10mg of white to off-white lyophilized powder in a 3mL vial.

Is SNAP-8 intended for human or cosmetic use?

No. The Protide Health product is supplied exclusively for biochemical, analytical, molecular, and qualified laboratory research.

Laboratory Terms & Compliance

Laboratory Research Use Only

This product is supplied exclusively for laboratory research, analytical testing, in-vitro studies, preclinical research, and qualified scientific experimentation.

It is not intended for human or veterinary consumption, diagnostic use, medical use, therapeutic use, cosmetic treatment, anti-aging treatment, or clinical administration.

No human application, dosing, administration, injection, formulation, or cosmetic-use instructions are provided.

The purchaser is responsible for appropriate laboratory handling, storage, and use in accordance with applicable institutional, federal, state, and local requirements.

For research use only.

 

Reviews (0)

Reviews

There are no reviews yet.

Be the first to review “Snap-8 Peptide 10mg”

Your email address will not be published. Required fields are marked *

Shipping & Delivery

MAECENAS IACULIS

Vestibulum curae torquent diam diam commodo parturient penatibus nunc dui adipiscing convallis bulum parturient suspendisse parturient a.Parturient in parturient scelerisque nibh lectus quam a natoque adipiscing a vestibulum hendrerit et pharetra fames nunc natoque dui.

ADIPISCING CONVALLIS BULUM

  • Vestibulum penatibus nunc dui adipiscing convallis bulum parturient suspendisse.
  • Abitur parturient praesent lectus quam a natoque adipiscing a vestibulum hendre.
  • Diam parturient dictumst parturient scelerisque nibh lectus.

Scelerisque adipiscing bibendum sem vestibulum et in a a a purus lectus faucibus lobortis tincidunt purus lectus nisl class eros.Condimentum a et ullamcorper dictumst mus et tristique elementum nam inceptos hac parturient scelerisque vestibulum amet elit ut volutpat.