CJC-1295

CJC-1295 refers in the literature to a modified GHRH (1-29) analogue. Two distinct materials circulate under this name: the analogue bearing a maleimidoproprionic acid linker designed to bind covalently to serum albumin, and the unconjugated tetrasubstituted analogue often labelled "without DAC", which is chemically a modified sermorelin-type peptide. These are different compounds with very different exposure profiles, and conflating them is the single most common error in the secondary literature. Identity of laboratory material is confirmed by mass spectrometry; purity by reversed-phase HPLC with a stated method. Values on this record are transcribed from supplier documentation.

The drug-affinity-complex approach was developed in the 2000s as a way to extend the very short circulating half-life of native GHRH fragments by covalent attachment to albumin in vivo. Early-phase human studies were conducted and published. Development did not reach a marketing authorisation, and no approved product exists.

Published work examines GHRH receptor agonism at the anterior pituitary, sustained elevation of growth hormone and IGF-1 following covalent albumin binding, and the pharmacokinetic consequences of that binding strategy. Studies report hormone concentration time courses, half-life estimates in humans and animals, and, in the early-phase work, tolerability observations.

The albumin-conjugation mechanism is well demonstrated: published human pharmacokinetic data show a markedly extended half-life relative to unmodified GHRH fragments, and sustained elevations of growth hormone and IGF-1 were measured directly rather than inferred. GHRH receptor pharmacology itself is textbook material. These pharmacodynamic findings are among the better-documented in this catalogue.

There are no completed randomised controlled trials demonstrating clinical benefit for any indication. Human data consist of small early-phase studies with limited participant numbers and short follow-up. Sustained rather than pulsatile elevation of growth hormone is a physiologically distinct exposure pattern whose long-term consequences are not characterised in the published record. Almost all circulating information about the unconjugated variant is preclinical or absent entirely; its pharmacokinetics in humans are not established, and much of what is claimed about it is transferred without justification from data on the conjugated compound. Independent replication of the original pharmacokinetic work is limited.

The naming problem is itself an evidentiary issue rather than a pedantic one. A reader searching the literature will find pharmacokinetic and hormone data for the albumin-binding conjugate, then encounter secondary sources applying those numbers to the unconjugated analogue, which has neither the linker nor the resulting exposure profile. Half-life figures in particular do not transfer between the two. Any summary that quotes an extended half-life without specifying which molecule it describes should be discounted entirely.

Store the lyophilised solid per the storage conditions on this record, protected from light and moisture, equilibrating the sealed vial before opening. Materials bearing reactive linker chemistry are particularly sensitive to moisture and to prolonged solution storage, and analytical re-verification after extended storage is prudent. This section covers laboratory handling of the material as supplied and provides no preparation or administration procedure.

Certificates for materials in this family should state which variant was analysed, and the calculated mass on the identity result is the practical way to tell them apart. Where a supplier's documentation uses the bare trade-style name without a mass, identity has not been established for the buyer, whatever the purity figure says.

Indexed citations appear below, each verified by PMID. See testing methodology for how identity and purity values are produced and sourcing standards for the documentation required with each batch.