Compound Profile
What Is HGH (Recombinant Somatropin)?
Human Growth Hormone (HGH), designated somatropin in its recombinant form, is a 191-amino acid single-chain polypeptide produced naturally by somatotroph cells located in the anterior pituitary gland. Its molecular weight is approximately 22,124 daltons with a molecular formula of C990H1529N263O299S7.
For research applications, recombinant human growth hormone (r-hGH) is synthesized using recombinant DNA technology — typically expressed in E. coli or mammalian cell systems — to produce a sequence-identical polypeptide to the endogenous molecule. This recombinant production context is the basis for its research compound classification.
Published research has examined how r-hGH interacts with the GH receptor (GHR) at the molecular level. GHR belongs to the cytokine receptor superfamily. Upon GH binding, the receptor undergoes conformational dimerization, recruiting and activating JAK2 (Janus kinase 2). JAK2 subsequently phosphorylates STAT5 (Signal Transducer and Activator of Transcription 5), which translocates to the nucleus — making the GHR/JAK2/STAT5 axis a central subject of somatotropin receptor research in preclinical models.
As a research compound, HGH is classified within the GH receptor agonist category and carries dual-use pharmaceutical context. Researchers handling this compound must comply with all applicable federal, state, and institutional regulatory frameworks.
Compound Specifications
Research Classification Notice: Recombinant HGH carries dual-use pharmaceutical context. Researchers must be aware of applicable federal regulations and institutional protocols governing GH-axis compounds in their jurisdiction. For research use only. Not for human use.
Published Research Areas
Research Background
Published research has examined recombinant somatropin across several molecular and cellular biology domains in preclinical and in vitro models. The following areas represent principal research contexts in the scientific literature.
GH Receptor Mechanism & JAK2/STAT5 Signaling Research
Published research has examined the structural basis of GH–GHR interaction, including the sequential receptor dimerization event that initiates JAK2 kinase activation and subsequent STAT5 phosphorylation. Preclinical model research in this area has clarified ligand–receptor binding kinetics and downstream transcriptional regulation.
IGF-1 Axis Production Research in Preclinical Models
Published research has examined how GHR signaling in hepatic preclinical models relates to IGF-1 (Insulin-like Growth Factor 1) gene expression. The somatotropic axis — hypothalamic GHRH → pituitary GH → hepatic IGF-1 — has been a subject of endocrinology research in rodent and cell culture models.
Skeletal Growth Plate Research in Animal Models
Published research has examined the role of GH receptor signaling in chondrocyte proliferation and differentiation at the epiphyseal growth plate in animal models. These studies have informed the mechanistic understanding of long bone growth plate biology in research contexts.
Metabolic Pathway Research in Preclinical Models
Published research has examined GHR-mediated effects on substrate metabolism in preclinical models, including research into carbohydrate and lipid pathway modulation downstream of JAK2/STAT5 signaling. These represent areas of ongoing metabolic biology research.
Adipose Tissue Research in Preclinical Models
Published research has examined GH receptor expression and GHR-mediated signaling in adipocyte preclinical models. Research into lipolytic pathway regulation via JAK2/STAT5 in adipose cell lines represents an active area of receptor biology investigation.
External resource. Published research literature on PubMed. For informational reference only.
Research Context Comparison
Direct GH vs. Secretagogue Pathway Research
In research models, direct recombinant GH (somatropin) and GHRH-pathway secretagogues engage the GH signaling cascade through distinct upstream mechanisms. Researchers select compound class based on the specific node of the somatotropic axis under investigation.
Direct GH Agonist
Recombinant HGH
(Somatropin)
- Binds GHR directly at cell surface in research models
- Initiates GHR dimerization → JAK2 activation without upstream GHRH pathway involvement
- Used in research examining GHR-distal signaling nodes and receptor saturation kinetics
- 191-AA polypeptide; MW ~22,124 Da; CAS 12629-01-5
- Research does not depend on somatotroph cell function in preclinical models
GHRH Analog (Secretagogue)
Sermorelin / CJC-1295
(GHRH-R Agonists)
- Activates GHRH receptor on somatotroph cells in preclinical research models
- Stimulates endogenous GH release from pituitary somatotrophs — upstream of GHR
- Research examines GHRH-R–mediated signaling and pulsatile GH release dynamics
- Sermorelin: 29-AA fragment; CJC-1295: DAC-modified GHRH analog
- Preclinical model function depends on intact somatotroph cell capacity
GHS-R Agonist (Ghrelin Mimetic)
Ipamorelin
(GHS-R1a Agonist)
- Activates GHS-R1a (ghrelin receptor) — distinct receptor from GHRH-R
- Research examines GHS-R pathway–mediated GH release dynamics in preclinical models
- 5-AA pentapeptide; selective GHS-R1a binding profile studied in preclinical research
- Often combined with GHRH analogs in preclinical model research examining synergistic GH release
- Upstream of GHR; does not directly bind GHR in receptor mechanism research
Sequence Labs Supply
HGH Research Compound — Available Vials
Lyophilized recombinant somatropin research compound. Each vial independently tested by Krause Analytical (HPLC + MS). Reviewed by Sabrina Runbeck, PA-C. Verified by Finnrick Pulse. For research use only.
10 IU
HGH Research Vial · Lyophilized
~$85
- Recombinant somatropin research compound
- Lyophilized powder — reconstitute with bacteriostatic water
- HPLC + Mass Spectrometry verified — Krause Analytical
- ≥99% purity verified
- COA available — batch-level transparency
- Reviewed by Sabrina Runbeck, PA-C
- For research use only. Not for human use.
15 IU
HGH Research Vial · Lyophilized
~$115
- Recombinant somatropin research compound
- Lyophilized powder — reconstitute with bacteriostatic water
- HPLC + Mass Spectrometry verified — Krause Analytical
- ≥99% purity verified
- COA available — batch-level transparency
- Reviewed by Sabrina Runbeck, PA-C
- For research use only. Not for human use.
Laboratory Reference
Reconstitution Reference for Research Use
Lyophilized HGH research compound requires solvent introduction prior to laboratory use. The following protocol describes standard laboratory reconstitution practice for research purposes only.
Prepare Solvent
Use bacteriostatic water (BAC water, 0.9% benzyl alcohol in sterile water, USP) as the reconstitution solvent. BAC water is the standard solvent for lyophilized polypeptide research samples due to its antimicrobial preservative properties.
Introduce Solvent
Introduce solvent slowly by directing it down the inside wall of the vial — not directly onto the lyophilized cake. This minimizes foam and mechanical disruption of the polypeptide chain. Do not agitate or vortex the research sample.
Gentle Rotation
After solvent introduction, gently rotate the vial between fingers to allow complete solubilization of the lyophilized powder. Avoid vigorous shaking. Allow the research sample to solubilize fully before proceeding with laboratory work.
Storage of Reconstituted Sample
Store reconstituted research sample refrigerated at 2–8°C (36–46°F). Protect from light. Lyophilized (unreconstituted) research compound may be stored at −20°C for extended research periods. Follow institutional storage protocols.
Frequently Asked Questions
HGH Research Compound FAQ
Inquire About HGH Research Compound
For research use only. HPLC + MS verified by Krause Analytical. Reviewed by Sabrina Runbeck, PA-C. 10 IU and 15 IU vials available.
For research use only. Not for human use. Not for veterinary use without appropriate licensing. These products have not been evaluated by the FDA and are not intended to diagnose, treat, cure, or prevent any disease. Researchers must comply with all applicable federal, state, and institutional regulations.