Peptide Schedule
Apelin-1212 residuesRPRLSHKGPMPFEach bubble = one amino acid. Size = residue mass. Color = chemical class.Apelin-12 Dosage Calculator
Apelin-12 is the shortest biologically active fragment of the 77-amino-acid preproapelin peptide, cleaved from the C-terminal region to yield the sequence RPRLSHKGPMPF (CAS 229961-08-4).
50mcg · Daily
Summary: Add 2mL BAC water to your 2mg vial. Draw to 5.0 units on a U-100 syringe for a 50mcg dose. This vial will last 40 doses.
Cycle Planner
Apelin-12 Pharmacokinetics
Pharmacokinetics — Active Dose Over Time
t½ = ~5 minutes (native peptide, rapid ACE2/neprilysin degradation in plasma)Disclaimer: This curve is a simplified first-order exponential decay model. Actual pharmacokinetics vary based on injection site, individual metabolism, body composition, and other factors. Half-life values are approximate and based on available preclinical and clinical literature. Many research peptides lack formal human pharmacokinetic studies. This is for educational purposes only — not medical advice.
Apelin-12 Dosing Protocol
| Level | Dose / Injection | Frequency |
|---|---|---|
| Beginner | 50mcg | Daily |
| Moderate | 150mcg | Daily |
| Aggressive | 300mcg | Daily |
Note: Apelin-12 is an endogenous 12-amino-acid peptide (sequence: RPRLSHKGPMPF) and the shortest active isoform of the apelin family. It is the natural ligand of the APJ receptor (APLNR), a class A GPCR expressed widely in cardiovascular tissue. All existing dosing data is derived from animal models — no human dosing protocols exist. The very short plasma half-life (~5 minutes) is a primary limitation for therapeutic use. Preclinical research compound only.
About Apelin-12
Apelin-12 is the shortest biologically active fragment of the 77-amino-acid preproapelin peptide, cleaved from the C-terminal region to yield the sequence RPRLSHKGPMPF (CAS 229961-08-4). It acts as an endogenous ligand for the APJ receptor (also called APLNR), an orphan G protein-coupled receptor first identified in 1993 and subsequently deorphanized when apelin was discovered in 1998 from bovine stomach extracts. Among the apelin isoforms (apelin-36, -17, -13, and -12), apelin-12 shows the strongest blood pressure-lowering effect in normotensive rats. In anesthetized rats, a single intravenous dose of 10 nmol/kg reduced mean arterial pressure by 26±5 mmHg — more than double the reduction seen with apelin-13 (11±4 mmHg) and five times that of apelin-36 (5±4 mmHg). This depressor response was completely abolished by co-administration of a nitric oxide synthase inhibitor, confirming an NO-dependent mechanism. At the cellular level, apelin-12 binding to APJ on vascular endothelial cells activates the PI3K/Akt cascade, which phosphorylates endothelial nitric oxide synthase (eNOS) at Ser1177. The resulting NO production activates soluble guanylyl cyclase in smooth muscle cells, increasing cyclic GMP and inducing vascular relaxation. APJ couples primarily through Gi/o and Gq alpha subunits, activating downstream ERK1/2, p70S6K, and PKC signaling pathways that promote cardiomyocyte survival and angiogenesis. In cardiac ischemia-reperfusion (I/R) injury models, apelin administration reduces infarct size, suppresses lactate dehydrogenase release, and limits cardiomyocyte apoptosis. Apelin-knockout mice show markedly worsened cardiac fibrosis and pathological remodeling when challenged with angiotensin II, indicating the apelin system acts as an endogenous counter-regulatory brake on the renin-angiotensin-aldosterone system (RAAS). Apelin also inhibits angiotensin II-induced atrial fibrosis through the TGF-beta1/Smad2/alpha-SMA pathway, reducing vulnerability to atrial fibrillation in animal models. The apelin/APJ system has attracted drug development interest, with the small-molecule APJ agonist AMG 986 (Amgen) completing a first-in-human Phase 1b trial in healthy subjects and heart failure patients (NCT03276728). AMG 986 was tolerated at doses up to 650 mg/day, though clinically meaningful pharmacodynamic effects in heart failure patients were not observed in the short-term study. Native apelin-12 itself remains limited to preclinical investigation due to its extremely short plasma half-life (~5 minutes), driven by rapid cleavage by ACE2 (angiotensin-converting enzyme 2) at the C-terminal Pro-Phe bond and by neprilysin (neutral endopeptidase 24.11). All dosing information is extrapolated from animal studies. No human clinical trials have tested apelin-12 peptide directly. This compound should be considered strictly experimental.