Sermorelin | Peptide Reference Material
RESEARCH PEPTIDE

Sermorelin | Peptide Reference Material

GHRH(1-29)-NH₂ — Peptide Reference Material
$59.00
Sermorelin is an amidated 29-amino-acid GHRH(1-29) research peptide studied in pituitary signaling and structure–activity research. Velora lot VBL-SR10-1 is independently verified by ILS Laboratories at 99.74% purity with identity confirmed.Velora Sermorelin 10 mg is supplied...
✓ Identity Verified
✓ Batch Documentation
✓ QR Lot Verification
✓ Research Use Only
✓ U.S. Fulfillment
✓ Batch Verification Available View verification →
Lot Verification Variant-specific documentation
Traceable Lots VBL lot identification
Primary Literature Peer-reviewed sources
Research Use Only Laboratory research materials

Scientific Specifications

Reference characteristics for laboratory research materials.

CAS Number
86168-78-7 (parent Sermorelin reference)
Molecular Formula
C149H246N44O42S (parent peptide reference)
Molecular Weight
3357.9 g/mol (parent peptide reference)
Appearance
Lyophilized peptide research material
Research Classification
Research Use Only (RUO). Not for human or veterinary use.

SCIENTIFIC OVERVIEW

Scientific background and research classification for this laboratory reference material.

Sermorelin is a synthetic amidated 29-amino-acid peptide corresponding to residues 1–29 of human growth hormone-releasing hormone (GHRH/GRF). The parent peptide designation is GHRH(1-29)-NH₂ / GRF(1-29)-NH₂ with sequence YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂. This N-terminal fragment has been characterized in research involving GHRH receptor biology, pituitary signaling, growth-hormone secretory responses, and peptide structure–activity relationships. Velora Sermorelin 10 mg is supplied as lyophilized peptide reference material with lot-specific independent analytical documentation. Research use only.

Primary Research Category
Growth Hormone Research
Material Type
Lyophilized Peptide
Intended Use
Laboratory Research
Research Categories
Growth Hormone Axis Endocrine Research Hormonal Regulation Receptor Pharmacology Structural Biology Pharmacokinetics

Mechanism of Action

Molecular interaction profile describing how this research material engages receptor systems and influences downstream biological signaling pathways.

GHRH(1-29)-NH₂ represents the biologically active N-terminal region of human GHRH. Published research characterizes GHRH signaling through the growth hormone-releasing hormone receptor (GHRHR) on anterior pituitary somatotroph cells in relation to endogenous growth-hormone secretory responses. In-vitro GHRH(1-29)-NH₂ structure–activity studies identify residues and conformational properties associated with receptor activation. These mechanistic findings are scientific context only and do not establish the activity, performance, safety, or intended use of the Velora material.

Biological Pathways
  • Growth Hormone Signaling
Primary Organ Systems
  • Endocrine System

Research Documentation

Laboratory documentation is presented when available for the selected product specification and current lot.

Batch Verified
Independent Batch Verification

Independent laboratory verification for this batch:

  • Identity Confirmation
  • HPLC Purity Analysis
  • Net Peptide Content
  • Endotoxin Testing
  • Analytical Chromatogram
  • Independent Laboratory Verification
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Scientific References
Peer-Reviewed Literature

Explore published literature, clinical investigations, and foundational scientific research.

View References →
Laboratory Resources
Technical Guidance

Storage guidance, handling recommendations, analytical methods, and laboratory best practices.

Related Research
Companion Materials

Discover complementary research materials frequently studied alongside this compound.

Research Center

Source-supported research categories for this laboratory reference material.

Scientific Context
GHRH Receptor Biology

Sermorelin provides a defined parent-peptide reference for studies of the receptor-active N-terminal region of human GHRH. Structure–activity research on GHRH(1-29)-NH₂ analogues has examined residue substitution, helical and amphiphilic features, conformational constraints, and receptor-agonist activity in experimental systems.

Browse References →
Scientific Context
Structure–Activity Relationships

Research categories include GHRH receptor biology, anterior-pituitary somatotroph signaling, GHRH(1-29)-NH₂ structure–activity relationships, peptide conformation studies, stability and pharmacokinetic research context, and controlled historical endocrine-response research. Historical human studies are cited as published research literature only, not as instructions or endorsement for use of this RUO material.

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Scientific Context
Peptide Stability & Pharmacokinetics

Published review literature describes relatively short circulating persistence for parent GRF(1-29) in historical research, with renal ultrafiltration and N-terminal enzymatic degradation discussed as contributing factors. PEGylated analogue studies are distinct modified-material research and are not attributes of unmodified Sermorelin or lot VBL-SR10-1.

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Scientific Context
Endocrine Response Research

GHRH(1-29)-NH₂ represents the biologically active N-terminal region of human GHRH. Published research characterizes GHRH signaling through the growth hormone-releasing hormone receptor (GHRHR) on anterior pituitary somatotroph cells in relation to endogenous growth-hormone secretory responses. In-vitro GHRH(1-29)-NH₂ structure–activity studies identify residues and conformational properties associated with receptor activation. These mechanistic findings are scientific context only and do not establish the activity, performance, safety, or intended use of the Velora material.

Browse References →

Research Library

Curated peer-reviewed literature selected to provide scientific context for this research material.

Clinical Trial•Peptides• 1985

Growth hormone responses to growth hormone-releasing hormone (1-29)-NH2 and a D-Ala2 analog in normal men.

Historical study of GHRH(1-29)-NH₂ and a D-Ala2 analogue in five normal men, reporting growth-hormone responses under the specific study conditions.
Velora Research Insight
Historical endocrine-response context only; not evidence of current product performance, safety, diagnosis, treatment, or intended use.
PubMed →DOI →
Structural Biology•Journal of Medicinal Chemistry• 1998

Human growth hormone-releasing hormone hGHRH(1-29)-NH2: systematic structure-activity relationship studies.

In-vitro structure–activity study of GHRH(1-29)-NH₂ analogues examining residue substitutions and conformational constraints relevant to receptor activation.
Velora Research Insight
Analogue-focused in-vitro SAR context; it does not establish clinical superiority, human safety, or unmodified Sermorelin stability.
PubMed →DOI →
Review Article•Advanced Drug Delivery Reviews• 2003

PEGylation of growth hormone-releasing hormone (GRF) analogues.

Review of GRF analogue stability and PEGylation research, including historical context for parent GRF(1-29) circulating persistence and degradation.
Velora Research Insight
PEGylated conjugates are distinct modified materials; their results are not attributes of unmodified Sermorelin or lot VBL-SR10-1.
PubMed →DOI →
Review Article•BioDrugs• 1999

Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth hormone deficiency.

Historical review of Sermorelin literature in pediatric idiopathic growth hormone deficiency.
Velora Research Insight
Historical clinical research context only; not a current approval, indication, dosing statement, or claim for Velora RUO material.
PubMed →DOI →
Analytical Study•Analytical and Bioanalytical Chemistry• 2016

Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS.

Analytical LC-HRMS/MS study listing the GHRH(1-29)-NH₂ sequence and parent-mass context in its assay table.
Velora Research Insight
Analytical reference context only; it does not establish the chemical form, quality attributes, or performance of Velora lot VBL-SR10-1.
PubMed →DOI →