Sermorelin 20MG

$179.00

Full Name: Sermorelin
Alternative Names: GRF (1-29) Amide, GHRH (1-29) Amide
Parent CAS #: 86168-78-7
Molecular Formula: C₁₄₉H₂₄₆N₄₄O₄₂S
Molecular Weight (M.W.): Approximately 3357.9 g/mol
Sequence: Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH₂
One-Letter Sequence: YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂
Length: 29 amino-acid residues
Product Type: Synthetic Research Peptide Amide

Category:

Description

Sermorelin is a synthetic 29-residue peptide supplied for controlled laboratory, analytical, and scientific research.

Its defined amino-acid sequence and C-terminal amidation form part of its complete molecular identity. This structure supports sequence verification, molecular-mass assessment, chromatographic characterization, terminal-state analysis, and comparative peptide research.

Sermorelin may also be supplied in salt-associated forms such as acetate, which have different molecular specifications from the parent peptide. Exact product form should therefore be confirmed using the applicable Certificate of Analysis.

Research Applications

Sermorelin may be examined in controlled non-clinical research involving:

  • Peptide identity and characterization
  • Sequence verification
  • C-terminal modification analysis
  • Ligand-receptor interaction studies
  • Molecular signaling research
  • Structure-function analysis
  • Comparative peptide research
  • Chromatographic characterization
  • Stability assessment

Experimental observations should remain specific to the applicable research system and should not be interpreted as evidence of hormonal, growth-related, performance-related, therapeutic, or clinical effectiveness.

Structural Information

Sermorelin is commonly represented as:

YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂

Key structural characteristics include:

  • 29 amino-acid residues
  • Linear peptide architecture
  • C-terminal amidation
  • Defined synthetic sequence
  • Product-dependent salt or counter-ion form

Distinguish the amidated parent peptide from non-amidated GRF/GHRH fragments and structurally modified analogues.

Analytical Identification

Relevant analytical characterization may include:

  • Amino-acid sequence confirmation
  • Molecular-mass assessment
  • C-terminal amidation verification
  • Chromatographic purity testing
  • Peptide identity confirmation
  • Counter-ion assessment
  • Structural characterization
  • Lot-specific quality analysis

Specifications & Documentation

Lot-specific documentation should be reviewed for:

  • Sermorelin identity
  • CAS number
  • Amino-acid sequence
  • Molecular formula
  • Molecular weight
  • C-terminal state
  • Salt or counter-ion form
  • Purity specification
  • Analytical testing
  • Lot or batch information
  • Certificate of Analysis
  • Storage requirements

Authenticated product-specific documentation should take precedence over generalized reference values.

Storage & Handling

Store according to the conditions specified on the product label and Certificate of Analysis. Protect the material from environmental conditions that could compromise peptide integrity.

Follow established laboratory procedures appropriate for research peptide materials.

Research Use Only

Sermorelin is supplied exclusively for laboratory research, analytical testing, and scientific reference purposes.

Disclaimer

For research use only. Not for human or veterinary use. Not intended for consumption, administration, hormonal use, growth-related use, performance enhancement, diagnosis, treatment, mitigation, cure, or prevention of any disease. No therapeutic, hormonal, growth-related, performance-related, medical, or clinical claims are made or implied. Product information is supplied solely for scientific identification, documentation, and research reference.

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