Sermorelin Research Peptide | GHRH 1-29 Analog

Description

Sermorelin Research Peptide

Sermorelin research peptide is a synthetic 29-amino-acid peptide corresponding to the amino-terminal portion of human growth hormone-releasing hormone (GHRH). It is also described in chemical databases as GHRH(1-29)-NH₂. PubChem lists Sermorelin with a molecular weight of approximately 3,357.9 g/mol and molecular formula C149H246N44O42S.

At LV Longevity Peptides, Sermorelin research peptide can be positioned as a research-grade peptide material for qualified laboratory and analytical applications.

Its defined peptide sequence makes it relevant to research involving peptide-receptor interactions, structural characterization, stability, degradation, and controlled signaling-model investigations.

The exact purity, quantity, physical form, storage requirements, and batch characteristics offered by LV Longevity Peptides should always be verified using the applicable batch-specific Certificate of Analysis (COA).

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What Is  Sermorelin research peptide?

Sermorelin is a synthetic GHRH-derived peptide consisting of 29 amino acids. It corresponds to the amino-terminal segment of naturally occurring human growth hormone-releasing hormone.

The standardized peptide sequence recorded by PubChem is:

YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂

This corresponds to the GHRH 1–29 amide research structure.

Sermorelin Chemical Information

PubChem confirms the formula, molecular weight, 29-residue sequence, and CAS identifier.

Chemical Information:

• Molecular Formula: C₁₄₉H₂₄₆N₄₄O₄₂S
• Molecular Weight: 3357.93 g/mol
• Sequence: H-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
• Molecular Structure:

Sermorelin Peptide Sequence

One-letter sequence

YADAIFTNSYRKVLGQLSARKLLQDIMSR

Structural representation

H-YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂

The C-terminal amidation is an important part of the defined Sermorelin structure. PubChem identifies the compound as an amidated 29-amino-acid peptide.

This information can be particularly useful for researchers performing peptide identity confirmation and mass-spectrometric characterization.

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Sermorelin Research Applications

GHRH Receptor Research

Sermorelin can be studied in controlled experimental systems investigating interactions between GHRH-derived peptide ligands and GHRH receptors.

Peptide-Receptor Interaction Studies

The defined structure makes Sermorelin suitable for research examining peptide-receptor binding characteristics and molecular interactions.

Structural Characterization

Researchers can investigate the molecular characteristics of this 29-residue GHRH-derived peptide using appropriate analytical methods.

Stability & Degradation Research

Sermorelin can be evaluated under controlled laboratory conditions to study stability and degradation behavior.

Structure-Function Research

The peptide can be incorporated into research examining relationships between peptide structure and experimentally observed molecular behavior.

Analytical Profiling

Appropriate analytical techniques can be used to evaluate peptide identity, purity, molecular mass, and other relevant characteristics.

The supplied product information similarly identifies GHRH-receptor interaction, signaling analysis, structure-function research, and stability/analytical profiling as research applications.

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Sermorelin vs. Full-Length GHRH

This is a useful SEO section because researchers may search for both Sermorelin and GHRH.

Sermorelin is not full-length human GHRH.

It is a synthetic peptide corresponding to the first 29 amino acids of the naturally occurring 44-amino-acid human GHRH sequence. PubChem describes it as the amidated GHRH(1-29) fragment.