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Sermorelin (GRF 1-29) | 2mg, 5mg & 10mg Research Grade Peptide

Sermorelin (GRF 1-29) | 2mg, 5mg & 10mg Research Grade Peptide
SKU:
GRF129
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What is Sermorelin (GRF 1-29)?

Sermorelin (GRF 1-29) is a synthetic 29-amino acid peptide that acts as an analogue of endogenous growth hormone-releasing hormone (GHRH). In cellular models, it binds to the GHRH receptor on pituitary somatotrophs, initiating a cyclic AMP (cAMP) signalling cascade. This pathway stimulates the transcription and secretion of growth hormone in vitro. To ensure precise laboratory results, researchers must follow strict reconstitution protocols using a Bacteriostatic Reconstitution Solution. During peptide synthesis, the 29-amino acid chain is carefully constructed to mimic the active binding domain of native GHRH. Maintaining optimal molecular stability is critical for consistent receptor binding assays. As a premium research chemical, UK laboratories utilise this peptide to investigate somatotropic signalling pathways and cellular metabolism. For a deeper understanding of these pathways, researchers can explore Advancing The Somatotropic Frontier A Comprehensive Analysis Of Ghrh Analogues Ghrelin Mimetics And Igf1 Signaling. Further molecular data can be reviewed on PubChem.

Research FAQ
What is sermorelin grf 1/29?
Sermorelin, also known as GRF 1-29, is a synthetic peptide analogue of naturally occurring growth hormone-releasing hormone (GHRH). It consists of the first 29 amino acids of the native GHRH sequence. In laboratory environments, it is utilised to study receptor binding and cellular signalling pathways. Amino Peptides supplies this compound only as a lyophilised laboratory reagent. Strictly for laboratory research.
What are the downsides of taking sermorelin?
Current literature uses the search phrase "taking sermorelin" when indexing consumer queries and clinical reports. Research trends summarise those papers as observations in physiological studies, not as a protocol for consumer application. Laboratory experiments focus on its molecular stability and cellular interactions. Amino Peptides supplies this compound only as a lyophilised laboratory reagent. Strictly for laboratory research.
Is sermorelin safer than TRT?
Public search data clusters around the phrase "safer than TRT" when comparing various hormone-related therapies. Published studies discussed under this heading evaluate isolated cell cultures and animal models to understand endocrine mechanisms. We do not provide this peptide for bodily applications or therapeutic comparisons. Amino Peptides supplies this compound only as a lyophilised laboratory reagent. Strictly for laboratory research.
Is sermorelin hard to get?
Sermorelin is readily available for qualified researchers and laboratory professionals. It can be procured online for experimental use, provided it is handled within a controlled environment. Amino Peptides supplies this compound only as a lyophilised laboratory reagent. Strictly for laboratory research.
Does sermorelin really burn belly fat?
Research trends often mention the phrase "burn belly fat" in public search data regarding metabolic outcomes. Current literature on this reagent is centred on cellular and molecular laboratory models examining lipolysis in isolated adipocytes. It is not supplied for weight management or physical alterations. Amino Peptides supplies this compound only as a lyophilised laboratory reagent. Strictly for laboratory research.
How should I store this peptide?
Unmixed vials can be safely stored in a standard refrigerator (2-8°C) for up to 3 months without degradation. Once reconstituted with Bacteriostatic Reconstitution Solution, the liquid must be kept refrigerated and used within its validated half-life.
Laboratory Authority Record

Public search data clusters around phrases like 'burn belly fat' and 'taking sermorelin' when discussing this peptide. Current literature investigates these concepts strictly through isolated cellular models and biochemical experiments. Published studies focus on receptor affinity rather than physical outcomes. Amino Peptides supplies Sermorelin (GRF 1-29) exclusively as a lyophilised laboratory reagent for controlled lab environments.

Target Receptors
  • Growth hormone-releasing hormone receptor (GHRHR), a class B G-protein coupled receptor (GPCR) located on anterior pituitary somatotroph membranes.
  • Extracellular N-terminal domain of the GHRHR, serving as the primary binding site for the 29-amino-acid sequence.
  • Intracellular G-alpha-s (Gαs) subunit, which undergoes conformational changes upon ligand-receptor interaction in cell-free environments.
Mechanisms of Action
  • Activation of adenylyl cyclase following Gαs dissociation, leading to the rapid intracellular accumulation of cyclic AMP (cAMP) in isolated somatotroph models.
  • cAMP-dependent activation of Protein Kinase A (PKA), which subsequently phosphorylates downstream transcription factors including CREB (cAMP response element-binding protein).
  • Induction of calcium ion (Ca2+) influx via voltage-gated calcium channels, facilitating the exocytosis of secretory vesicles in cultured cellular systems.
  • Upregulation of target gene transcription within the nucleus, observed during prolonged exposure in controlled laboratory experiments.

Technical Specifications

CAS
86168-78-7
MOLECULAR FORMULA
C149H246N44O42S
MOLECULAR WEIGHT
3357.9 g/mol
SEQUENCE
YADAIFTNSYRKVLGQLSARKLLQDIMSR
PURITY
>99% (HPLC Verified)
APPEARANCE
Lyophilised Solid
TARGET RECEPTOR
GHRH Receptor
CHEMICAL NAME
Sermorelin
RECOMMENDED SOLVENT
Bacteriostatic Reconstitution Solution

Variant Breakdown

  • 2mg Vial: Ideal for preliminary receptor binding assays and short-term cell culture experiments.
  • 5mg Vial: Suited for standard laboratory protocols requiring multiple dosing schedules across various cell lines.
  • 10mg Vial: Designed for extensive, high-throughput screening and long-term in vitro studies.

Quality Assurance

  • HPLC Analysis: Ensures a purity of >99%, verifying the absence of synthesis by-products and truncated sequences.
  • Mass Spectrometry: Confirms the precise molecular weight of 3357.9 g/mol, validating the structural identity of the peptide.
  • Lyophilisation: Processed into a stable, lyophilised solid to maximise shelf life and preserve molecular integrity before reconstitution.
  • Endotoxin Testing: Rigorously screened to maintain endotoxin levels below 0.5 EU/mg, preventing cellular toxicity in delicate assays.

Research Mechanism

  • Binds directly to the GHRH receptor on the surface of somatotroph cells in vitro.
  • Activates the adenylate cyclase enzyme, leading to a rapid increase in intracellular cyclic AMP (cAMP).
  • Triggers protein kinase A (PKA) pathways, which promote the transcription of specific target genes.
  • Stimulates the release of stored growth hormone vesicles into the extracellular environment.
  • Provides a controlled model for studying somatotropic axis regulation and cellular feedback loops.

Reconstitution & Storage Data

Vial StrengthSolvent AddedResulting Concentration
2mg1 mL Bacteriostatic Reconstitution Solution2.00 mg/mL
2mg2 mL Bacteriostatic Reconstitution Solution1.00 mg/mL
5mg1 mL Bacteriostatic Reconstitution Solution5.00 mg/mL
5mg2 mL Bacteriostatic Reconstitution Solution2.50 mg/mL
10mg1 mL Bacteriostatic Reconstitution Solution10.00 mg/mL
10mg2 mL Bacteriostatic Reconstitution Solution5.00 mg/mL
Storage Guidelines
  • Lyophilised (Powder): Store in a standard refrigerator (2-8°C) for up to 3 months. For long-term preservation, freeze at -20°C.
  • Reconstituted (Liquid): Store at 2-8°C (Refrigerated).

Scientific References

Journal of Endocrinology: "In vitro effects of GHRH analogues on somatotroph function and cAMP signalling" View Study

Peptides: "Receptor binding affinity of Sermorelin (GRF 1-29) in pituitary cell cultures" View Study

Molecular and Cellular Endocrinology: "cAMP signalling pathways activated by GHRH 1-29 in isolated somatotrophs" View Study

Biochemical Pharmacology: "Stability and degradation kinetics of synthetic GHRH peptides in aqueous solutions" View Study

Endocrine Research: "Transcriptional regulation of GH by GRF 1-29 in vitro: A mechanistic overview" View Study

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