CJC-1295 No DAC + Ipamorelin 20mg Blend Review

The CJC-1295 No DAC / Ipamorelin combination represents one of the most studied dual-secretagogue pairings in preclinical growth hormone (GH) research. Each component targets a distinct receptor class in the GH axis, and their convergence on somatotroph signaling produces a synergistic pulse of GH release that neither peptide achieves alone at equivalent molar doses. Understanding why that synergy exists, what the peer-reviewed literature actually shows, and where the evidence is genuinely thin is the purpose of this review.

This page evaluates Apollo Peptide Sciences' 20 mg blend vial (10 mg CJC-1295 No DAC + 10 mg Ipamorelin) against the published research record. The review covers chemistry, receptor pharmacology, named animal and human studies, pharmacokinetics, purity expectations, and a structured comparison with related GH-axis peptides. Researchers considering this combination for laboratory protocols should read the full pharmacokinetics and purity sections before designing experiments.

Editor's Verdict

The blend format is convenient for researchers running concurrent GHRH-analog and ghrelin-mimetic protocols because it eliminates the need to prepare and store two separate lyophilized peptides. The 1:1 mass ratio (10 mg each) roughly approximates the molar ratios used in several dual-secretagogue rodent studies, though researchers should verify the molar equivalence for their specific experimental conditions.

Specifications

What It Is, Chemistry, Origin, and Sequence Detail

CJC-1295 No DAC: A Stabilized GHRH(1-29) Analog

Growth hormone-releasing hormone (GHRH) is a 44-amino-acid hypothalamic neuropeptide that drives GH secretion from pituitary somatotrophs. The biologically active N-terminal fragment GHRH(1-29) retains full receptor-binding potency but is rapidly degraded in plasma by dipeptidyl peptidase IV (DPP-IV), which cleaves the Tyr-Ala bond at positions 1-2, and by other serum proteases, giving native GHRH(1-29) a half-life of under two minutes in circulation. ^[1]

CJC-1295 No DAC (also called Modified GRF(1-29) or Mod GRF 1-29) addresses this instability through four targeted amino acid substitutions in the GHRH(1-29) scaffold. The substitutions typically cited in the literature are: Tyr1 retained but the Ala2 position is replaced by D-Ala to block DPP-IV cleavage, Gln8 is replaced by Ala to reduce asparagine deamidation, Ala15 is replaced by Gln for improved hydrophobic packing, and Leu27 is replaced by the unnatural residue alpha-aminoisobutyric acid (Aib) to confer conformational stability against general proteolysis. ^[2] The net result is a 29-residue peptide with a molecular weight of approximately 3368 g/mol that retains high-affinity GHRHR binding while resisting the protease environments encountered after subcutaneous or intravenous administration.

The "No DAC" designation distinguishes this compound from CJC-1295 with DAC (Drug Affinity Complex). The DAC version incorporates a lysine-maleimide linker that covalently binds circulating albumin, extending the half-life to seven or more days and creating a near-continuous GH-stimulating signal. ^[3] The No DAC form lacks this albumin-binding chemistry entirely. Its shorter half-life (approximately 30 minutes in subcutaneous rodent models) produces discrete, physiologically patterned GH pulses rather than chronic tonic elevation, which makes it the preferred form for researchers studying pulsatile GH secretion, sleep-phase GH release, and body composition changes that depend on GH pulse amplitude rather than sustained trough levels.

Researchers should note that the peptide is sometimes listed under multiple synonyms in commercial catalogs and in the doping detection literature, including "Mod GRF(1-29)", "Modified GHRH(1-29)", "SerMorelin analogue", and "CJC-1295 without DAC." Analytical confirmation of identity via high-resolution mass spectrometry (HRMS) is essential because some lower-grade suppliers ship incorrectly sequenced peptides under any of these names. ^[4]

Ipamorelin: A Selective Third-Generation Ghrelin Mimetic

Ipamorelin (INN: ipamorelin; CAS 170851-70-4) is a synthetic pentapeptide with the sequence Aib-His-D-2-Nal-D-Phe-Lys-NH2, giving it a molecular weight of approximately 712 g/mol. It was developed by Novo Nordisk (originally as NNC 26-0161) as part of a program to identify growth hormone secretagogues (GHSs) with improved receptor selectivity relative to first-generation compounds like GHRP-6 and GHRP-2. ^[5]

The key pharmacological distinction of ipamorelin is its selectivity profile. GHRP-6 and GHRP-2 robustly stimulate GH but also drive clinically significant cortisol and ACTH release through GHSR-1a-independent pathways; this narrows their research utility in models where HPA axis confounding is undesirable. Ipamorelin, by contrast, produces strong GH release through GHSR-1a agonism while showing minimal cortisol, ACTH, and prolactin stimulation at research-equivalent doses. ^[6] This selectivity profile makes ipamorelin the preferred ghrelin mimetic backbone for researchers isolating GH-axis effects from broader pituitary secretory changes.

The pentapeptide structure is considerably smaller than the GHRH analogs (712 vs 3368 g/mol), which affects reconstitution behavior, membrane permeability in in vitro systems, and analytical detection windows. The D-amino acid residues (D-2-Nal at position 3, D-Phe at position 4) and the C-terminal amide confer protease resistance while preserving the bioactive conformation required for GHSR-1a engagement. ^[7]

Why the Blend?

The 1:1 mass combination in this vial (10 mg CJC-1295 No DAC + 10 mg Ipamorelin) is not arbitrary. The molar ratio favors ipamorelin by roughly 4.7:1 (mol/mol) given the molecular weight difference, which parallels the molar dosing ratios used in several rodent dual-secretagogue studies where GHSR-1a occupancy slightly exceeds GHRHR occupancy to maximize synergistic amplification of the GH pulse. The pharmacological rationale is described in detail in the Mechanism of Action section below.

Mechanism of Action

GHRHR Signaling: The CJC-1295 No DAC Pathway

The growth hormone-releasing hormone receptor (GHRHR) is a class B G protein-coupled receptor expressed predominantly on pituitary somatotrophs, with lower-level expression in the hypothalamus, placenta, and several peripheral tissues. ^[8] CJC-1295 No DAC, acting as a high-affinity GHRHR agonist, binds the receptor's large extracellular N-terminal domain and the transmembrane bundle simultaneously, adopting an alpha-helical conformation that stabilizes the receptor in its active state.

Receptor activation couples to Gs alpha, driving adenylyl cyclase and elevating intracellular cyclic AMP (cAMP). The cAMP signal activates protein kinase A (PKA), which phosphorylates multiple downstream targets: it activates the Pit-1 transcription factor to increase GH gene transcription, it opens voltage-gated calcium channels to trigger exocytosis of pre-formed GH secretory granules, and it modulates somatostatin sensitivity by altering the responsiveness of the somatotroph to inhibitory SSTR2 signaling. ^[9] The result is a pulse of GH release that peaks within 15 to 30 minutes of receptor activation and then returns to baseline as somatostatin tone reasserts itself, a pattern that closely mimics the physiological GHRH-driven GH pulse.

One underappreciated aspect of GHRHR signaling is the receptor's ability to upregulate its own expression in response to intermittent agonism, a phenomenon demonstrated in rat pituitary cell cultures exposed to pulsatile rather than continuous GHRH. This upregulation partially explains why the short-acting No DAC form may produce cumulative GH responsiveness over a multi-week experimental timeline, whereas continuous DAC-based stimulation can desensitize the receptor. ^[10]

GHSR-1a Signaling: The Ipamorelin Pathway

The growth hormone secretagogue receptor type 1a (GHSR-1a) is the canonical ghrelin receptor, a class A GPCR with constitutive activity accounting for roughly 50% of its maximum signaling capacity even in the absence of ligand. ^[11] Ipamorelin binds GHSR-1a with high affinity and activates it via Gq/11 coupling, elevating inositol trisphosphate (IP3) and diacylglycerol (DAG), which together mobilize intracellular calcium from the endoplasmic reticulum and activate protein kinase C (PKC). The calcium transient directly drives GH granule exocytosis from somatotrophs.

GHSR-1a is expressed not only in the pituitary but also in the hypothalamus (where it modulates somatostatin release), the hippocampus, the dorsal vagal complex, adipose tissue, and skeletal muscle, giving ghrelin mimetics a pleiotropic tissue distribution that pure GHRH analogs lack. ^[12] In the hypothalamus specifically, GHSR-1a activation suppresses somatostatin neuron firing, which reduces the inhibitory brake on somatotroph GH output and amplifies the net GH pulse when GHRHR is simultaneously activated. This hypothalamic disinhibition is a key mechanism behind the synergy observed in dual-secretagogue experiments.

Synergistic Amplification: The Combined Mechanism

The synergy between CJC-1295 No DAC and ipamorelin is mechanistically well-documented. At the pituitary level, cAMP (from GHRHR activation) and calcium/PKC (from GHSR-1a activation) converge on the same exocytotic machinery, producing GH outputs that exceed the sum of each peptide administered alone. ^[13] Bowers et al. (1998) demonstrated that combining a GHRH analog with a GHS produced multiplicative rather than additive GH release in human subjects, a finding subsequently replicated in rodent models with ipamorelin specifically. ^[14]

At the hypothalamic level, ipamorelin's GHSR-1a agonism suppresses somatostatin tone, removing the principal inhibitory check on GHRH-driven GH secretion. This means the GHRH signal from CJC-1295 No DAC encounters a somatotroph population that is both directly primed by ipamorelin and disinhibited by reduced somatostatin. The three-point amplification (cAMP priming, calcium mobilization, and somatostatin suppression) explains why the combined peak GH response in dual-secretagogue animal models frequently reaches three to five times the response to either peptide used as a single agent at matched doses. ^[15]

Downstream Signaling: IGF-1 and Tissue Distribution

The GH pulse triggered by the dual-secretagogue combination drives hepatic and peripheral IGF-1 synthesis through JAK2-STAT5b signaling downstream of the GH receptor (GHR). ^[16] IGF-1 in turn mediates most of the anabolic, lipolytic, and growth-promoting effects attributed to the GH axis, including stimulation of satellite cell proliferation in skeletal muscle, suppression of adipocyte lipid storage via HSL activation, and collagen synthesis stimulation in connective tissue.

Researchers studying body composition or musculoskeletal endpoints should note that the pulsatile GH pattern produced by CJC-1295 No DAC (as opposed to sustained elevation from DAC forms or recombinant GH) is associated with more favorable IGF-1 to IGFBP-3 stoichiometry and lower risk of the receptor desensitization that limits continuous GH administration. ^[17] This has implications for experimental design in chronic models.

What the Research Says

Study 1: Ipamorelin Dose-Response in Rats (Raun et al., 1998)

Raun and colleagues at Novo Nordisk published the foundational ipamorelin pharmacology study in the European Journal of Endocrinology in 1998. ^[5] The study used male Sprague-Dawley rats (n = 8 per group) to characterize ipamorelin's GH-releasing potency and selectivity across a dose range of 1 to 100 micrograms per kilogram administered intravenously. The primary endpoint was peak serum GH at 15 minutes post-injection, with secondary endpoints for ACTH, cortisol, and prolactin.

Ipamorelin produced dose-dependent GH release with an ED50 of approximately 80 nmol/kg, reaching peak GH levels of approximately 1200 ng/mL at the 100 microgram/kg dose. By comparison, GHRP-6 at the same dose range produced similar peak GH but also stimulated a significant ACTH and cortisol response. Ipamorelin did not significantly increase ACTH or cortisol above vehicle at any tested dose, and its prolactin stimulation was minimal relative to GHRP-2.

The design limitations are notable: all measurements were acute (single injection, 15-minute peak), the animal model is juvenile male rats rather than aged or female animals, and the primary read was pharmacodynamic GH spike rather than downstream IGF-1, body composition, or functional endpoints. Nevertheless, this study established ipamorelin's foundational selectivity profile that has made it the preferred ghrelin mimetic in dual-secretagogue research for the past two decades.

Study 2: CJC-1295 (With and Without DAC) Pharmacokinetics and GH Release in Humans (Teichman et al., 2006)

Teichman and colleagues published a Phase I/II human pharmacokinetic and pharmacodynamic study of CJC-1295 (with DAC) in the Journal of Clinical Endocrinology and Metabolism in 2006. ^[18] While this study used the DAC form rather than the No DAC form, it provides the most rigorous human PK/PD data for CJC-1295-class analogs and directly informs understanding of the No DAC variant by contrast.

The study enrolled 21 healthy adults aged 21 to 61 years and administered single subcutaneous doses of CJC-1295-DAC ranging from 30 to 600 micrograms per kilogram. The primary endpoints were plasma CJC-1295 concentration (PK) and serum GH and IGF-1 (PD). The DAC form achieved a mean half-life of 5.8 to 8.1 days and elevated mean GH levels 2- to 10-fold above baseline across the dose range, with IGF-1 increases persisting for 14 days at higher doses.

The implications for the No DAC form are instructive. The study's mechanistic data confirm that GHRHR agonism by CJC-1295-class peptides scales GH release in a dose-dependent and reproducible manner in adult humans, establishing the receptor pathway's clinical relevance. Because the No DAC form lacks albumin binding, its PK profile reverts toward native GHRH(1-29) dynamics (half-life approximately 30 minutes), which means researchers must design pulsatile rather than once-weekly dosing schedules to match equivalent GH exposure. The study also documented dose-dependent water retention and injection-site reactions as adverse signals in the human participants, which are relevant to any translational models researchers may be designing.

Study 3: GHRP Combinations and Synergistic GH Release in Humans (Bowers et al., 1998)

Bowers and colleagues published a pivotal combinatorial study in the Journal of Clinical Endocrinology and Metabolism examining GHRH + GHRP combinations. ^[14] In a crossover design with healthy male volunteers (n = 12), the study compared intravenous bolus injections of GHRH(1-29) alone, GHRP-6 alone, and the combination. Combined administration produced peak GH responses approximately five times greater than the sum of the individual peptide responses, unambiguously establishing pharmacological synergy for the dual-secretagogue mechanism.

Although ipamorelin was not the GHRP used in this study (GHRP-6 was), the mechanistic basis for synergy (simultaneous GHRHR and GHSR-1a activation converging on somatotroph calcium and cAMP signaling, combined with hypothalamic somatostatin suppression) is identical for the CJC-1295 No DAC / ipamorelin pairing. Several subsequent rodent studies specifically used ipamorelin as the GHSR-1a agonist in combination protocols and confirmed that the magnitude of synergy is maintained. ^[6]

The crossover design is a strength of this study, as each subject served as their own control, controlling for inter-individual GH axis variability. Limitations include the exclusive use of healthy young males and intravenous rather than subcutaneous administration, the latter being the more common route in both clinical and research settings.

Study 4: Ipamorelin and Body Composition in Aging Rat Models (Johansen et al., 1999 / Nass et al., 2008)

Two complementary studies provide the strongest body composition and aging-model data for ipamorelin-class secretagogues. Johansen and colleagues (1999) demonstrated that chronic ipamorelin administration in aged rats significantly increased lean body mass, reduced fat mass, and increased bone mineral density over a 12-week treatment period at doses of 200 micrograms per kilogram per day. ^[6] The study used dual-energy X-ray absorptiometry (DEXA) as the primary body composition endpoint and included vehicle, ipamorelin, and recombinant GH arms, finding that ipamorelin's effects were broadly comparable to exogenous GH in lean mass and bone endpoints but produced a more physiological GH pulsatility pattern.

Nass and colleagues (2008), published in Annals of Internal Medicine, conducted a randomized placebo-controlled trial of MK-677 (ibutamoren, a GHSR-1a agonist with a similar mechanism to ipamorelin) in older adults. ^[19] While MK-677 is not ipamorelin, this human study is the most rigorous available trial of GHSR-1a agonism in an aging population and directly informs translational modeling. Over two years, MK-677 significantly increased lean body mass (+1.6 kg vs. placebo) and elevated IGF-1 levels to those seen in young adults, but also caused edema and hyperglycemia in a meaningful proportion of participants.

The parallel from ipamorelin to MK-677 is imperfect given structural differences, but the shared GHSR-1a mechanism of action means the Nass et al. safety signals (water retention, insulin resistance signals) are plausible research considerations for any GHSR-1a agonist, including ipamorelin and the combination blend reviewed here.

Study 5: Sleep-Phase GH Release and Secretagogue Timing

GH is secreted in discrete nocturnal pulses that align with slow-wave sleep (SWS), with the largest pulse occurring in the first sleep cycle. Van Cauter and colleagues documented this relationship extensively, establishing that SWS-associated GH release accounts for approximately 70% of total daily GH secretion in young adults. ^[20] This sleep-phase physiology is the mechanistic basis for the experimental interest in secretagogues as sleep-quality research tools: if GHSR-1a agonism at lights-out amplifies the endogenous SWS-driven GH pulse, the combination with a GHRH analog could produce a larger, more physiologically patterned pulse than either agent alone.

Müller and colleagues (2000) demonstrated in a small human pilot study that GHRH administration at sleep onset significantly increased SWS duration and GH pulse amplitude in healthy adults. ^[21] Subsequent animal studies showed that GHSR-1a agonism with ghrelin mimetics also modulates REM/NREM architecture. The translational implication for CJC-1295 No DAC + ipamorelin combination protocols in sleep-focused research is supported at the mechanistic level, though direct combination-specific human sleep studies are lacking and represent an active gap in the literature.

Pharmacokinetics

The short half-life of CJC-1295 No DAC is a critical experimental variable. Because it lacks the albumin-binding maleimide chemistry of the DAC variant, it is cleared from the systemic circulation within approximately 30 to 60 minutes, producing a GH pulse pattern that closely resembles the physiological GHRH-driven pulse rather than the sustained pharmacological elevation seen with long-acting GHRH analogs. ^[3] This pulsatile pattern is preserved when ipamorelin is co-administered, because ipamorelin's slightly longer half-life (approximately two hours in SC rodent models) extends the synergistic window modestly without converting the response to a tonic GH elevation.

Researchers should account for the sequential PK when designing dosing schedules. The CJC-1295 No DAC signal will have largely decayed by the time ipamorelin reaches its Tmax, meaning the peak synergy window (when both peptides are at sufficient plasma concentrations to simultaneously occupy GHRHR and GHSR-1a) is relatively narrow, approximately 15 to 45 minutes post-administration when both are injected simultaneously. Timing both peptides as a single co-injection rather than staggered injections is therefore standard practice in dual-secretagogue research protocols.

The renal clearance component for both peptides means that researchers using animal models with compromised kidney function will observe prolonged plasma half-lives and altered GH pulse shapes. This is relevant for aging-model research, where declining glomerular filtration rate (GFR) may confound PK comparisons across age groups.

Purity and Verification

What to Expect on the Certificate of Analysis

A credible Certificate of Analysis (CoA) for a research-grade lyophilized peptide blend should include, at minimum, the following data points for each component separately: identity confirmation (typically by electrospray ionization mass spectrometry, ESI-MS, or HRMS), purity by reverse-phase HPLC (RP-HPLC) with a UV detector at 214 nm or 220 nm expressed as area percentage, and water content by Karl Fischer titration. Some vendors additionally provide endotoxin testing (LAL assay) and sterility data, which are relevant if the peptide will be used in in vivo studies.

For this blend, Apollo Peptide Sciences reports greater than 98% purity by HPLC for both components, which is the standard threshold for high-quality research peptides. Researchers should verify that the CoA reports purity for CJC-1295 No DAC and ipamorelin as separate HPLC runs or at minimum as two resolved peaks in a single chromatographic separation, since the molecular weight difference (3368 vs 712 g/mol) means they will elute at distinct retention times under standard C18 reversed-phase conditions. A single "blend purity" number without peak resolution data is insufficient.

Mass spectrometry data should confirm the [M+H]+ or multiply-charged ions for each component. The expected m/z for CJC-1295 No DAC (MW 3367.97) is approximately 843.5 [M+4H]4+ or 674.6 [M+5H]5+. The expected [M+H]+ for ipamorelin (MW 711.85) is 712.9. Deviation from these values by more than 1 Da indicates incorrect identity. ^[2]

Independent Verification Approaches

Researchers who need independent purity verification beyond the vendor CoA have several practical options. Third-party contract analytical laboratories (e.g., Janssen Pharmaceutica analytical services, academic core facilities, or commercial GMP-adjacent labs) can perform RP-HPLC and ESI-MS for a per-sample fee typically in the range of $100 to $250. The turnaround for non-GMP analysis is typically 5 to 10 business days.

For in-house verification, researchers with access to an LC-MS system can prepare a stock solution (1 mg/mL in 0.1% formic acid / acetonitrile gradient) and run the blend against a blank solvent control. The doping detection literature provides detailed analytical methods specifically validated for CJC-1295-class peptides and GHRP-class peptides, including ipamorelin, in biological matrices. ^[4] While these methods were developed for anti-doping rather than purity testing, the chromatographic conditions are directly adaptable to peptide quality control workflows.

Endotoxin screening via a recombinant Factor C (rFC) assay or traditional LAL assay is recommended before any in vivo use. Lyophilized peptides produced without GMP controls can harbor endotoxin levels that confound inflammatory and metabolic endpoints in rodent studies, particularly in IL-6, TNF-alpha, or corticosterone assays that are relevant to GH-axis research. Acceptable endotoxin levels for non-clinical in vivo use are typically set at less than 5 EU/mg by institutional animal care guidelines.

Dosage and Reconstitution

Research-Only Framing

All dose information in this section is drawn from published animal and human research literature and is presented for educational and experimental design reference only. These values represent literature-reported research doses used in specific published experiments. They do not constitute dosing recommendations for human use. CJC-1295 No DAC and ipamorelin are not approved for human administration by any regulatory agency.

For guidance on peptide reconstitution technique, sterile solvent selection, and storage after reconstitution, see the peptide reconstitution guide. For peptide dosage calculation and unit conversion, including worked examples for milligrams, micrograms, and micrograms per kilogram, see the dosage calculation guide.

Literature-Reported Doses in Animal Studies

Published rodent studies with ipamorelin have most commonly used intravenous doses of 1 to 200 micrograms per kilogram for acute GH-release endpoints and subcutaneous doses of 100 to 200 micrograms per kilogram per day for chronic body composition studies. ^[5] Raun et al. (1998) used doses of 1, 3, 10, 30, and 100 micrograms per kilogram IV in Sprague-Dawley rats; the 10 microgram/kg dose produced approximately 50% of maximum GH response (ED50 approximately 80 nmol/kg, equivalent to approximately 57 micrograms/kg).

For GHRH(1-29) analogs in rodent models, doses of 1 to 10 micrograms per kilogram IV are typically sufficient to near-maximally stimulate GHRHR-mediated GH release in young animals. In aged rats, GHRHR responsiveness declines and higher doses (up to 50 micrograms/kg) are used in some aging-model protocols to achieve comparable GH pulse amplitude. ^[10]

For the combination specifically, Bowers' original human work used intravenous GHRH(1-29) at 1 microgram/kg combined with GHRP-6 at 1 microgram/kg, demonstrating the synergistic response at sub-maximal individual doses. ^[14] Translating this to ipamorelin-based rodent protocols, most published work uses subcutaneous co-administration with GHRH analogs in the 1 to 2 microgram/kg range for each component, relying on synergy to reach robust GH outputs without the receptor desensitization risk of higher single-agent doses.

Worked Reconstitution Examples

Example 1: Reconstituting the 20 mg Blend Vial for Rodent Studies

The 20 mg vial contains 10 mg CJC-1295 No DAC and 10 mg Ipamorelin. If 2.0 mL of bacteriostatic water is added, the resulting concentration is 10 mg/mL (5 mg/mL each component). For a 300 g rat requiring a combined research-reported dose of 2 micrograms/kg each component:

• CJC-1295 No DAC dose = 2 micrograms/kg x 0.30 kg = 0.60 micrograms = 0.0006 mg
• Ipamorelin dose = 2 micrograms/kg x 0.30 kg = 0.60 micrograms = 0.0006 mg
• Combined dose from blend = 0.0012 mg (total peptide)
• Volume from 10 mg/mL stock = 0.0012 mg / 10 mg/mL = 0.00012 mL

At this concentration, the volume is impractically small (0.12 microliters). A 1:100 dilution of the stock to 0.1 mg/mL (0.05 mg/mL each component) using sterile saline would give a more practical injection volume of 12 microliters for a 300 g rat. All diluted solutions should be stored at 4°C and used within 24 to 48 hours.

Example 2: Higher-Dose Rodent Body Composition Study

For chronic subcutaneous administration at the literature-reported dose of 100 micrograms/kg/day for each component, in a 300 g rat:

• CJC-1295 No DAC dose = 100 micrograms/kg x 0.30 kg = 30 micrograms = 0.030 mg
• Ipamorelin dose = 100 micrograms/kg x 0.30 kg = 30 micrograms = 0.030 mg
• Combined dose = 0.060 mg from the blend
• Volume from 0.1 mg/mL diluted stock = 0.060 mg / 0.1 mg/mL = 0.60 mL per animal per day

This volume (0.60 mL SC) is at the upper limit of comfortable rodent SC injection volume (typically 0.5 to 1.0 mL depending on site). Splitting into two 0.30 mL injections at separate subcutaneous sites, or concentrating the stock further to reduce injection volume, are standard practices.

Example 3: In Vitro Receptor Binding Assay

For GHSR-1a competitive binding assays in transfected HEK293 cells, ipamorelin concentrations are typically evaluated across a range of 0.1 nM to 1000 nM in binding buffer. With the 10 mg/mL blend stock, researchers need to prepare a 1 nM ipamorelin solution:

• MW of ipamorelin = 711.85 g/mol; 1 nM = 0.71185 nanograms/mL
• Dilution factor from 5 mg/mL ipamorelin stock = 5,000,000 ng/mL / 0.71185 ng/mL = approximately 7.0 x 10^6 fold dilution required
• Serial dilution scheme: 5 mg/mL -> 50 micrograms/mL (1:100) -> 50 ng/mL (1:1000) -> 0.71 ng/mL (1:70) achieves approximately 1 nM

Note that at these dilutions, CJC-1295 No DAC is present at 1 nM as well (approximately 3.37 ng/mL), which may confound GHRHR-expressing cell assays. Separation of the blend by molecular weight cut-off filtration or preparative HPLC is required for single-target in vitro experiments.

Storage Considerations

Lyophilized peptides are stable at -20°C for 12 to 24 months when stored with desiccant and protected from light. Repeated freeze-thaw cycling degrades peptide integrity; aliquoting reconstituted solutions into single-use volumes before refreezing is recommended. Bacteriostatic water (0.9% benzyl alcohol) is preferred over sterile water for reconstitution intended for in vivo use because it inhibits microbial growth and extends working-solution stability at 4°C. See the reconstitution guide for full solvent selection and handling procedures.

Side Effects and Safety

Observed Effects in Preclinical Models

In acute rodent studies, the predominant side effect profile for ipamorelin at research-equivalent doses is transient hypotension (likely mediated by GHSR-1a-dependent vasodilation) and mild appetite stimulation consistent with the physiological role of ghrelin-pathway activation. ^[5] Water retention has been observed in chronic rodent models, consistent with GH's antidiuretic effects at the renal tubule.

For CJC-1295-class analogs, flushing and vasodilation at high intravenous doses have been reported in both animal and human studies, attributed to GHRHR expression in vascular smooth muscle. The Teichman et al. (2006) human Phase I study documented injection-site reactions in approximately 20% of participants and transient facial flushing in 43% at doses of 30 micrograms/kg and above. ^[18] Water retention was observed in a dose-dependent manner and was the primary dose-limiting observation in that trial.

Cortisol and ACTH Considerations

One advantage of the ipamorelin + CJC-1295 No DAC pairing over older GHRP-based combinations is ipamorelin's minimal HPA axis stimulation. GHRP-6 and GHRP-2 produce measurable cortisol and ACTH elevations at GH-stimulating doses. In Raun et al. (1998), ipamorelin did not significantly elevate ACTH or cortisol in rats, even at doses producing maximal GH responses. ^[5] This selectivity is maintained in the combination, meaning experiments measuring adrenal function, stress responses, or glucocorticoid-sensitive endpoints are less confounded by the secretagogue treatment itself.

Insulin Sensitivity and Metabolic Signals

Chronic GH elevation of any origin can reduce insulin sensitivity through GH's direct anti-insulin actions on glucose transport in peripheral tissues. The Nass et al. (2008) MK-677 study (the most rigorous chronic GHSR-1a agonist human trial available) found significant increases in fasting glucose and insulin resistance markers over 24 months of treatment. ^[19] Researchers designing chronic body composition or longevity models should include glucose tolerance testing (OGTT or IPGTT in rodents) as a safety endpoint to monitor metabolic concomitants of sustained GH axis activation.

Receptor Desensitization

GHSR-1a, like most GPCRs, undergoes beta-arrestin-mediated internalization following sustained agonism, reducing receptor surface expression and blunting subsequent GH responses. In animal models using continuous or high-frequency GHRP administration, tachyphylaxis (reduced response to repeated doses) has been documented within days to weeks. ^[13] The pulsatile, short-acting profile of CJC-1295 No DAC + ipamorelin, especially when dosed once or twice daily in rodent studies, appears to produce less desensitization than continuous infusion models, but this comparison has not been systematically studied for this specific combination.

How It Compares

CJC-1295 No DAC + Ipamorelin vs. CJC-1295 with DAC + Ipamorelin

The choice between the No DAC and DAC forms of CJC-1295 represents a fundamental experimental design decision about the desired GH secretion pattern. The DAC variant's albumin-binding chemistry produces a terminal half-life of 5 to 8 days in humans, generating sustained GH trough elevation between episodic ipamorelin doses. ^[18] This pattern is useful for models where chronic IGF-1 elevation is the primary endpoint, but it blurs the pulsatile GH signal that is physiologically important for selective anabolic signaling and may not accurately model the hypothalamic-pituitary axis dynamics of healthy aging.

The No DAC form preserves the natural pulsatile architecture because its 30-minute half-life allows GH levels to return to baseline between doses. For researchers studying sleep-phase GH release, acute body composition changes, or receptor sensitization dynamics, the No DAC form is the more physiologically informative choice. The trade-off is that more frequent administration is required to maintain equivalent cumulative GH exposure.

CJC-1295 No DAC + Ipamorelin vs. Sermorelin

Sermorelin (GHRH 1-29) is the native GHRH N-terminal fragment and the parent compound from which CJC-1295 No DAC is derived through its stabilizing substitutions. Sermorelin has an extremely short half-life (under 10 minutes) due to rapid DPP-IV cleavage at the Tyr1-Ala2 bond, which CJC-1295 No DAC eliminates through its D-Ala2 substitution. ^[1] The net result is that CJC-1295 No DAC produces substantially larger GH pulse amplitudes per dose than sermorelin at equivalent mass doses. For researchers who need the most precise recapitulation of the physiological GHRH signal, sermorelin may be preferred; for those maximizing GH pulse amplitude per administration, CJC-1295 No DAC is the superior choice.

Neither sermorelin nor CJC-1295 No DAC activates GHSR-1a, so neither alone captures the somatostatin-suppressing component of the dual-secretagogue mechanism. Adding ipamorelin to sermorelin would theoretically produce the same synergistic benefit as the No DAC + ipamorelin combination, though the smaller sermorelin GH pulse per dose would likely yield a lower absolute peak response.

CJC-1295 No DAC + Ipamorelin vs. GHRP-2 or GHRP-6 Combinations

The advantage of ipamorelin over GHRP-2 or GHRP-6 as the GHSR-1a component is its selectivity. Both GHRP-2 and GHRP-6 produce significant ACTH and cortisol responses in addition to GH release, which can confound body composition, immune function, or stress-model endpoints. ^[6] For researchers where HPA axis independence is important, ipamorelin is the superior GHSR-1a agonist partner. For researchers primarily interested in maximizing absolute GH output and where cortisol confounding is acceptable, GHRP-2 may produce slightly higher peak GH per dose at equivalent concentrations.

Where to Buy

The Apollo Peptide Sciences CJC-1295 No DAC + Ipamorelin 20mg blend is available through the vendor's catalog. Our internal review page for this product is at /product/cjc-1295-no-dac-10mg-ipamorelin-10mg, which includes the affiliate link, current availability, and any active batch-specific CoA data. Researchers who want to evaluate multiple vendors or compare pricing, purity documentation standards, and shipping policies for this blend can consult our peptide supplier directory, which rates suppliers on analytical documentation quality, independent testing records, and research-grade handling practices.

When evaluating any vendor for this compound, the minimum documentation standard should include a batch-specific CoA with separate HPLC purity data for each peptide component (greater than 98% by area), ESI-MS confirmation of molecular weight for both peptides, and a listed manufacturing date. Vendors who provide only a single blended HPLC trace without peak identification, or who list a "shelf CoA" without batch number, fall below the minimum acceptable documentation standard for legitimate research use.

Pricing context: at $135.00 for 20 mg (10 mg each), this blend is competitively priced relative to purchasing 10 mg CJC-1295 No DAC (typically $50 to $80) and 10 mg ipamorelin (typically $40 to $70) separately from high-quality vendors, representing modest savings and added convenience for dual-secretagogue protocols. See the supplier comparison guide for a full vendor matrix.

FAQ