CJC-1295 with DAC
Also known as CJC-1295 DAC, DAC:GRF, Drug Affinity Complex GRF
CJC-1295 with DAC is a GHRH analog carrying a Drug Affinity Complex that binds serum albumin to extend circulating half-life. A research profile centered on what the DAC linker actually does.
This is the 'long' half of the CJC-1295 story. Chemically it starts from the same modified GRF(1-29) analog as the no-DAC version — same GHRH-receptor target, same four stabilizing substitutions — but it adds one thing that changes everything about its behavior in solution: the Drug Affinity Complex, or DAC.
Because that single addition is the entire reason this exists as a separate product, this page is built around it. What follows is descriptive chemistry and the research contexts the molecule appears in, not effects or protocols.
The same tetra-substituted GRF(1-29) analog as the no-DAC form, but bearing a Drug Affinity Complex — a maleimidopropionyl linker that forms a covalent bond with a cysteine on circulating serum albumin. That albumin conjugation is what distinguishes this molecule and is the reason it is described as long-acting.
The Drug Affinity Complex, in plain terms
A Drug Affinity Complex is a small reactive group — here a maleimidopropionyl linker — attached to the peptide. Once in a biological fluid, that group reacts with a free thiol on albumin, the most abundant protein in blood plasma, forming a bond between the peptide and its albumin carrier.
The consequence is a dramatic shift in longevity. Unbound GHRH is cleared in minutes; a peptide riding on albumin is shielded from the enzymes and filtration that would otherwise remove it. This is the mechanism behind CJC-1295 with DAC being characterized as a long-acting analog, and it is precisely what the no-DAC variant lacks.
Why the two CJC-1295 SKUs are studied differently
Half-life is not a cosmetic detail — it changes the shape of the signal. The body's own GHRH is pulsatile: brief spikes, then silence. A short-acting analog can be studied against that natural rhythm; a DAC-conjugated one produces a much flatter, more sustained presence. Researchers care about that difference, which is why a store lists the two forms separately rather than treating 'CJC-1295' as one thing.
On a certificate of analysis, the DAC form carries additional mass from the linker relative to the bare 29-residue peptide. A mass that matches the plain modified GRF(1-29) under a 'with DAC' label is a red flag that the lots have been mixed up.
Research contexts and common pairings
As a GHRH-receptor analog, this molecule appears in growth-hormone-axis research on the releasing-hormone side of the pathway. It is frequently discussed together with ghrelin-receptor secretagogues, since the two receptor mechanisms are studied in combination.
It sits in the same family as sermorelin and tesamorelin — all GHRH-based — but is distinguished from them by its albumin-binding half-life extension.
These are research areas the compound is associated with in the literature — not medical claims or intended uses.
Handling & storage
Supplied lyophilized. Stored sealed and cold; reconstituted with bacteriostatic water only when a protocol requires, then refrigerated. Handle per accepted laboratory practice.
Verify a certificate by lot →Common questions
The Drug Affinity Complex is a linker that covalently binds circulating albumin. By tethering the peptide to a long-lived carrier protein, it substantially extends the molecule's half-life compared with the no-DAC form.
They share the same GRF(1-29) analog core, but the DAC linker makes them behave very differently — long-acting versus short-acting — so they are handled and studied as distinct products.
A GHRH analog. It engages the GHRH receptor, unlike ghrelin-receptor secretagogues such as ipamorelin, GHRP-2 and GHRP-6.
This monograph is a research-use reference. It describes composition and the contexts in which the compound has been studied — it is not medical advice, a description of effects, or a recommendation for use. Sold strictly for laboratory and research use; not for human or animal consumption.