HGH Fragment 176-191 5mg

 49,00

HGH Fragment 176-191 5 mg – Grail Formula Quality.
Researched and verified with Liquilabs s.r.o. Czechia.
Analytical testing confirms 99.6 % purity, assay content verified at 3.64 mg, molecular ion mass identified at 1800 Da and endotoxin levels below 0.001 EU/mg.
Supplied as a 5 mg lyophilized peptide with full COA traceability.
For research use only — not for human or veterinary use.

Availability: In stock: ships within 1 day after payment confirmation.

HGH Fragment 176-191 5 mg is a high-purity lyophilized peptide research compound supplied exclusively for scientific investigation and controlled laboratory experimentation.

For research use only — not for human or veterinary use.


Product Overview

HGH Fragment 176-191 is a synthetic peptide research compound derived from a specific region of growth hormone and frequently investigated in controlled laboratory environments focused on peptide signalling systems, molecular communication pathways and regulatory biological mechanisms.

The compound has attracted considerable scientific interest due to its defined amino acid sequence, reproducible analytical profile and extensive use within peptide-focused laboratory research.

This preparation contains 5 mg of lyophilized HGH Fragment 176-191 supplied in a sealed research vial. Lyophilization helps preserve peptide stability during storage while allowing controlled reconstitution for laboratory applications.

Due to its clearly defined molecular characteristics and well-documented analytical profile, HGH Fragment 176-191 remains a recognised research material within peptide science and controlled in vitro experimentation.


Peptide Overview

HGH Fragment 176-191 is a synthetic peptide commonly studied in controlled laboratory settings examining peptide-mediated signalling pathways, molecular communication systems and cellular interaction networks.

Researchers frequently utilise HGH Fragment 176-191 in experimental models investigating peptide behaviour, receptor interactions and regulatory signalling mechanisms.

The peptide’s reproducible analytical characteristics and clearly defined molecular structure have contributed to its continued relevance within scientific peptide research.

Its ongoing presence in peptide-focused investigations has established HGH Fragment 176-191 as a recognised compound for advanced laboratory studies and molecular pathway analysis.


Historical Background and Scientific Context

Scientific interest in peptide fragments expanded significantly as researchers sought to better understand structure-function relationships within naturally occurring peptide hormones.

Advances in peptide synthesis and analytical chemistry enabled specific peptide regions to be isolated and investigated independently under controlled laboratory conditions.

HGH Fragment 176-191 subsequently became a frequently studied research compound due to its defined sequence and suitability for biochemical and molecular investigations.

Today, the compound continues to be referenced in scientific literature involving peptide chemistry, molecular signalling and laboratory-based biological research.


Mechanistic Focus in Research

Within controlled laboratory settings, HGH Fragment 176-191 is commonly studied in relation to peptide-mediated molecular signalling pathways and cellular communication systems.

Research investigations frequently explore:

  • Peptide signalling pathways
  • Molecular interaction dynamics
  • Cellular communication systems
  • Signal transduction mechanisms
  • Comparative peptide research
  • Molecular pathway analysis
  • Regulatory signalling investigations

These experimental models allow researchers to investigate complex molecular communication processes and peptide-mediated biological systems.


Analytical Verification (COA)

Each batch of HGH Fragment 176-191 supplied by Grail Formula undergoes independent third-party laboratory verification to confirm peptide identity, assay content, purity and microbiological safety.

Analytical testing for this batch was performed by Liquilabs s.r.o. (Czechia) using validated chromatographic, spectrometric and microbiological techniques.

Batch: GF-HGHFR-B241

  • Assay Content: 3.64 mg
  • Purity: 99.6 percent
  • Identification by FTIR Spectrum: 989
  • Identification by Retention Time: 0.996
  • Molecular Ion Mass Identification: 1800 Da
  • Bacterial Endotoxins: below 0.001 EU/mg
  • Total Aerobic Microbial Count: 0 CFU/g
  • Total Yeast and Mold Count: 0 CFU/g

Independent elemental impurity screening confirmed no detectable arsenic, cadmium, mercury, lead, nickel, vanadium or cobalt, all measured below 0.001 ppm.

Microbiological screening confirmed no detectable microbial contamination, supporting laboratory-grade quality standards.

These analytical procedures provide confirmation of identity, purity, traceability and batch consistency.


Research Applications

In controlled laboratory environments, HGH Fragment 176-191 may be utilised in experimental models designed to investigate peptide signalling systems and molecular interaction pathways.

Examples of research applications include:

  • Peptide signalling investigations
  • Molecular communication studies
  • Comparative peptide analysis
  • Cellular pathway research
  • Signal transduction modelling
  • Laboratory interaction studies
  • Controlled in vitro peptide experiments

These applications are intended exclusively for scientific and laboratory investigation.


Grail Formula Quality

Every Grail Formula research compound is supported by extensive independent analytical verification and full batch traceability.

Each batch undergoes testing for:

  • Peptide identity confirmation
  • Assay content verification
  • Purity assessment
  • Molecular ion mass verification
  • Endotoxin analysis
  • Microbial contamination screening
  • Heavy metal screening
  • Batch traceability

Independent testing helps ensure consistent laboratory-grade research material suitable for controlled scientific applications.


When You Choose Grail Formula

When selecting Grail Formula, researchers gain access to independently verified research compounds supported by detailed Certificates of Analysis and transparent batch-specific testing.

Our quality programme includes assay verification, purity confirmation, FTIR spectrum identification, retention time analysis, molecular ion mass identification, endotoxin screening, microbial testing and elemental impurity analysis.

Every batch is supported by a downloadable COA issued by Liquilabs s.r.o. Czechia, providing full traceability and independent laboratory verification.


Research Use Limitation

  • Used solely for laboratory and in vitro research
  • Not approved for human consumption
  • Not approved for veterinary use
  • Not intended for diagnostic purposes
  • Not intended for therapeutic applications
  • Not permitted for clinical administration
  • For research use only
  • Independently analysed by Liquilabs s.r.o. Czechia
  • 99.6 % purity confirmed by COA
  • Assay content verified at 3.64 mg
  • Identification confirmed by FTIR spectrum and retention time analysis
  • Molecular ion mass identified at 1800 Da
  • Endotoxin level below 0.001 EU/mg
  • No detectable heavy metals or microbial contamination
  • Research-grade peptide compound
  • For research use only – not for human or veterinary use

For laboratory research only. Not intended for human consumption, injection, or cosmetic use.

This product is for research purposes only. Not for human use or diagnostic/therapeutic applications. Keep out of reach of children.

Third-Party Tested

Public COAs

Batch Verified

EU Shipping

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