The short version of CJC-1295 fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2026-05-17. Anything still debated is marked as such rather than presented as settled.
Lyophilized peptide powder is comparatively stable when kept dry, cold, and protected from light. Once dissolved, the molecule is vulnerable to deamidation, oxidation, and aggregation, with the rate depending on pH, buffer composition, and temperature. Alkaline conditions and repeated freeze-thaw cycles accelerate loss of the intact peptide. The methionine present in the native sequence is a known oxidation site, which is one reason it was replaced in the modified fragment. Suppliers typically recommend cold storage of solutions and use within a short window.
Analytical confirmation usually relies on reversed-phase high-performance liquid chromatography for purity and on liquid chromatography coupled to mass spectrometry for identity. Mass data reveal the expected molecular mass and can flag truncated or oxidized species. Amino acid analysis and peptide mapping provide sequence-level verification. Immunoassays are used in some biological matrices, but antibodies raised against one releasing-hormone analog may cross-react with another. Reported purity figures depend heavily on the method used, so comparisons between suppliers require matching the analytical approach.
The two variants differ dramatically in how long they persist in circulation. The form lacking the albumin-binding group has a plasma half-life measured in tens of minutes, comparable to the natural hormone fragment. The version carrying the drug affinity complex binds albumin and shows a half-life of roughly six to eight days in human studies. That figure comes from small trials that tracked hormone levels over extended periods. The physiological consequences of sustained versus pulsatile stimulation are still debated and the literature does not settle the point.
Two forms circulate in research settings and are frequently confused. One carries the drug affinity complex and is often written as CJC-1295 with DAC; the other lacks that group and is usually called modified GRF(1-29). The two share the same core sequence but differ sharply in how long they persist in blood. Products labelled only as CJC-1295 normally refer to the version carrying the complex. Documentation that omits the distinction leaves the intended molecule ambiguous.
CJC-1295 is a synthetic peptide built as a long-acting analogue of growth hormone-releasing hormone. Its backbone matches the first twenty-nine residues of the natural human hormone, with four amino acid substitutions added to slow enzymatic breakdown. A reactive maleimide group, commonly termed the drug affinity complex, allows the peptide to attach to circulating albumin after administration. That albumin attachment keeps the molecule in the bloodstream for an extended period instead of being cleared within minutes.
| Property | Value | Notes |
|---|---|---|
| Molecular mass | Approximately 3.4 to 3.6 kDa | Depends on whether the affinity complex is attached |
| Appearance | White to off-white lyophilized powder | Freeze-dried solid, often in a sealed vial |
| Solubility | Soluble in water and aqueous buffers | Dissolution rate varies with pH and buffer salt |
| Typical storage | Below minus 20 degrees Celsius, dry and dark | Dissolved material is usually kept cold and used promptly |
| Common analytical methods | Reversed-phase HPLC and mass spectrometry | Peptide mapping and amino acid analysis add sequence detail |
Pharmacokinetic behaviour differs sharply between the two forms. The DAC-bearing peptide shows an extended circulation time measured in days, whereas the version without the complex is cleared within roughly half an hour. This gap shapes how researchers design dosing schedules in animal models. Whether the prolonged presence of the DAC form produces effects meaningfully different from the short-acting variant remains an open question, since comparative human data are scarce.
CJC-1295 is a synthetic peptide designed to mimic growth hormone-releasing hormone (GHRH), the endogenous signal that prompts the pituitary gland to release growth hormone. The compound is a modified fragment of the natural hormone, spanning the first twenty-nine amino acids of GHRH with several substitutions that slow enzymatic breakdown. Two variants circulate in research settings: one carrying a drug affinity complex (DAC) and one without it. The DAC-free form is frequently labelled Mod GRF(1-29) in catalogs and discussion forums.
Batch-to-batch consistency depends on solid-phase peptide synthesis and subsequent purification. Coupling efficiency, resin choice, and cleavage conditions all affect the final profile. Counter-ion content and moisture can shift the apparent mass of a batch. Documentation typically includes a certificate of analysis with chromatograms and spectra. Independent verification by a second laboratory is sometimes requested. Whether a given certificate reflects the actual vial contents depends on chain of custody. Analytical methods themselves carry uncertainty that should be stated alongside results.
Lyophilized material is typically stored at minus twenty degrees Celsius or lower. Keeping the vial dry and protected from light preserves peptide integrity. Repeated freeze-thaw cycles can cause aggregation or loss of activity. Once dissolved, solutions are generally kept at two to eight degrees Celsius. Stability data for reconstituted solutions vary, and long-term behavior is not fully established. Working aliquots reduce the number of times a stock container is opened.
Reverse-phase high-performance liquid chromatography is the standard tool for purity assessment. The technique separates the target peptide from truncated or modified byproducts. Mass spectrometry confirms molecular weight and supports sequence verification. Electrospray ionization and matrix-assisted laser desorption are both used. Amino acid analysis provides an independent check on composition. Purity values are commonly reported as area percentage from the chromatogram. Residual trifluoroacetate and water content are also measured in many quality programs.
The core sequence keeps the receptor-binding region of GHRH while replacing four positions that are vulnerable to dipeptidyl peptidase-4 and other proteases. Substitutions at positions 2, 8, 15, and 27 raise metabolic stability relative to the natural hormone. The N-terminal residues remain essential for activity, so changes there generally lower potency. Molecular weight sits near 3368 daltons for the tetrasubstituted analog without the linker, while the albumin-binding form is heavier because of the added maleimide group.
CJC-1295 is a synthetic peptide modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. Its sequence corresponds to the first twenty-nine residues of human GHRH, with four substitutions that slow enzymatic breakdown. Early descriptions placed the compound in research on growth hormone deficiency and related conditions, and later literature groups it with the long-acting GHRH analogs. The name appears in both laboratory and popular fitness writing, where it sometimes labels chemically different peptides.
Two related peptides circulate under the CJC-1295 label, and they differ mainly in how long they persist in circulation. The version carrying a drug affinity complex includes a maleimidopropionic acid linker that forms a covalent bond with serum albumin. The other version, usually written as modified GRF(1-29) or tetrasubstituted GRF(1-29), lacks that linker and is cleared quickly. Mixing the two produces inconsistent readings of published half-life values, because the linker rather than the receptor-facing sequence drives most of the difference.
zum „Peruzzi-Schliff“ verbessert „Swiss-Cut“ (Sechzehnkant): Brillantvariante für kleine Steine mit jeweils 16 Facetten auf dem Ober- und Unterteil „Spirit Sun“ (auch Spirit diamond oder Spiegel der Sonne): Moderner, von Ulrich Freiesleben und Bernd Munsteiner in den 1990er Jahren entwickelter, Diamantschliff mit je 16 Facetten auf dem Ober- und Unterteil, die strahlenförmig von innen nach außen verlaufen als Sonderformen bzw. Fantasyschliffe davon abgeleitet sind unter anderem „Netzschliff“, „Kingschliff“ (King cut) mit 86 Facetten, „Swiss-Cut“, „Petal-Cut“, „Magna-Schliff“ mit 102 Facetten, „Amerikanischer Schliff“ (auch Tolkowsky-Schliff) sowie der „Wirbelschliff“ und die „Knospe“ mit spiralförmig angeordneten und nach außen gewölbten Facetten Rosenschliff (auch Einfache Rose, Holländische Rose oder Amsterdamer Rose): Schliff mit flachem Unterteil und 24 dreieckigen Facetten auf der gewölbten Oberseite „Antwerpener Rose“ (Brabanter Rose): Altschliff aus dem 16. Jahrhundert mit 12 trapezförmigen und dreieckigen Facetten Doppelrose: 32 dreieckige Facetten auf der gewölbten Oberfläche. als Sonderformen bzw. Fantasyschliffe davon abgeleitet sind unter anderem die „Recoupé-Rose“, der „Jubilee-Cut“ mit 80 rosettenförmig angeordneten Facetten, die zum Oberteil hin eine Spitze bilden, und der „Needle-Brillant“ „Oval“: Ellipsenförmiger Schliff als Brillantschliff mit zentrischer Tafel, 8 viereckigen und 24 dreieckigen Facetten auf der Oberseite „Navette“ bzw.
„Marquise“: Ellipse, deren Übergänge im großen Durchmesser spitz zulaufen „Pendeloque“: Eiförmiger Schliff mit zentrischer Tafel, 8 viereckigen und 24 dreieckigen Facetten auf der Oberseite „Tonne“: Ovaler Treppenschliff, deren Seiten abgeschnitten wurde
=== Dreidimensionale Formen === „Kugel“: Kugelförmiger Brillantschliff „Olive“: Olivenförmiger Brillantschliff „Briolett“: Tropfenförmiger Facettenschliff mit dreieckigen, rauten- oder trapezförmigen Facetten „Pampel“: Tropfenförmiger Brillantschliff mit kegelförmig angeordneten, länglichen Facetten und abgeschnittener Kegelspitze.
=== Weitere Schliffformen === „Antikschliff“: Quadratische oder rechteckige Schliffform im Brillant- oder Treppenschliff mit abgerundeten Ecken „Ballonschliff“: Facettenschliff mit nach außen gewölbten Facetten „Barion-Schliff“: Rechteckige oder achteckige Grundform mit Treppenschliff auf der Oberseite und kegelförmiger Facettierung auf der Unterseite „Context Cut“: Moderner, von Ulrich Freiesleben und Bernd Munsteiner in den 1990er Jahren entwickelter, oktaederförmiger Schliff mit flacherem Oberteil „Flower Cuts“: Moderne Diamantschliffe in den Formen „Zinnie“ (Zinnia), „Ringelblume“ (Marigold), „Feuerrose“ (Fire Rose), „Sonnenblume“ (Sunflower) und „Dahlie“ (Dahlia). „Gabrielle-Cuts“: Spezielle, von Gabi Tolkowsky patentierte Schliffformen „Herz“ (auch Herzschliff): Herzförmiger Brillantschliff „Linsenschliff“: Treppenschliff, bei dem die Facetten des Ober- und Unterteils in eine Richtung verlaufen. „Prinzess-Schliff“ (Princess cut): Gemischter Schliff mit Kardinalsschliff auf dem Oberteil und Fächerschliff auf dem Unterteil. „Radiant“: Gemischter Diamantschliff mit Treppenschliff auf dem Oberteil, Brillantschliff auf dem Unterteil und insgesamt 70 Facetten. „Tafelschliff“, auch Siegel-, Flach-, Platten- oder Ringsteinschliff: Einfacher Facettenschliff, bei dem die Tafel auf der Oberseite und meist auch auf der Unterseite die vorherrschende Facette ist.
Sources: de.wikipedia.org
The version carrying the affinity complex bears a maleimide group that binds serum albumin, which extends its circulation time to several days. The version without it lacks this group and clears within roughly half an hour. The two are chemically related but behave very differently once in the body.
In common usage the name without the affinity complex is often equated with MOD GRF 1-29, a fragment carrying four stabilizing substitutions. Strictly speaking, the term originally referred to the albumin-binding version. The overlap in naming causes frequent ambiguity in both informal and technical writing.
Reversed-phase chromatography separates the peptide from related impurities and yields a purity estimate. Mass spectrometry confirms the molecular mass and detects modifications such as oxidation. Sequence-level checks rely on peptide mapping or amino acid analysis when stronger confirmation is needed.
It is a synthetic peptide analogue of growth hormone-releasing hormone. Four substitutions in its sequence make it more resistant to enzymatic degradation than the natural hormone. In the version carrying a drug affinity complex, the peptide binds albumin and remains in circulation for days.