PEPTIDE NOVA
SERMORELIN 2MG
$44.99 Original price was: $44.99.$34.99Current price is: $34.99.
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Description
Product Overview
Sermorelin is a synthetic peptide compound widely referenced in scientific literature and studied in peptide research related to endocrine signaling, peptide-mediated receptor interactions, and molecular regulatory pathways. Within controlled laboratory and preclinical research environments, this peptide is investigated for its interactions with receptor-mediated signaling systems, intracellular signaling cascades, and molecular communication networks.
As a laboratory peptide compound, Sermorelin is utilized in experimental research to study peptide stability, receptor binding interactions, and molecular regulatory mechanisms. Researchers focus on its peptide molecular structure and signaling properties to better understand complex peptide signaling pathways in preclinical and experimental research models.
WHAT IS SERMORELIN
Sermorelin is a synthetic peptide analog of the endogenous growth hormone-releasing hormone (GHRH) fragment. It is classified as a hormone fragment peptide analog, designed for laboratory research on receptor-mediated endocrine signaling pathways.
In peptide research contexts, Sermorelin is studied for its interaction with growth hormone-releasing hormone receptors and related intracellular signaling systems. Researchers examine Sermorelin to study molecular signaling cascades, receptor binding dynamics, and peptide-mediated communication mechanisms within controlled laboratory environments.
Key Research Areas
Scientific literature references Sermorelin in several laboratory peptide research areas, including:
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peptide signaling pathways
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endocrine signaling peptide activity
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receptor binding interactions
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intracellular signaling cascade analysis
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molecular signaling mechanisms
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peptide stability and structural activity
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peptide-receptor interaction studies
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laboratory peptide characterization
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cell signaling research
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preclinical peptide study setup
These areas are explored in preclinical and controlled laboratory research models.
Molecular Structure & Scientific Profile
Compound Name: Sermorelin
Peptide Classification: Synthetic hormone fragment peptide analog
Molecular Formula: C77H110N18O19
Molecular Weight: ~1986 g/mol
Amino Acid Sequence: H-Ala-Glu-Asp-Gly-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
CAS Number: 86168-78-7 (referenced in scientific literature)
Sermorelin is a synthetic peptide composed of 29 amino acids representing the N-terminal fragment of GHRH. Its peptide molecular structure allows researchers to study receptor interactions and intracellular signaling pathways.
Scientific Research Context
Scientific literature has explored Sermorelin in experimental and preclinical research investigating endocrine signaling pathways, growth hormone receptor interactions, and intracellular signaling mechanisms. Studies focus on peptide-mediated receptor interactions and molecular signaling networks within controlled laboratory environments.
In experimental research models, Sermorelin has been examined in studies related to receptor binding dynamics, intracellular signaling cascades, and peptide-mediated molecular communication. These investigations are conducted in preclinical and laboratory research settings to analyze peptide signaling interactions and molecular regulatory mechanisms.
Product Specifications
Compound Name: Sermorelin
Peptide Classification: Synthetic hormone fragment peptide analog
Format: Lyophilized Powder
Quantity: 2MG
Research Category: Peptide research / endocrine signaling research / molecular pathway research
Storage Recommendations: Store under refrigerated laboratory conditions in a cool, dry environment protected from light and moisture. Long-term storage under controlled laboratory conditions is recommended.
Research Disclaimer
Research Use Only. Not for human or veterinary use. Not approved by the FDA and not intended to diagnose, treat, cure, or prevent any disease.
Links To Research Studies
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