CJC-1295 w/ DAC

For Laboratory Research Use Only — Not for Human or Veterinary Use.

Standard (< 1,000 vials)$380/kit

Volume (1,000+ vials)$290/kit

Quantity (kits)

= 10 vials

Minimum order: 100 vials total. Mix and match across all products.

I confirm this order is for laboratory research use only.For Laboratory Research Use Only — Not for Human or Veterinary Use. By checking this box you affirm this product will not be used for human or animal administration.

Specifications

CAS Number	446262-90-4
Molecular Formula	C165H269N47O46
Molecular Weight	3647.25 g/mol
Purity	≥98% (HPLC)
Form	Lyophilized Powder
Storage	-20°C, desiccated, protected from light
Reconstitution	Bacteriostatic water

Certificate of Analysis

Lot documentation

Every production lot is independently third-party tested. A batch-specific Certificate of Analysis — documenting HPLC purity, mass spectrometry identity confirmation, and net peptide content — is issued with every shipment. View a sample COA to see the format.

View Sample COA About our testing →

Research context

The modified GRF(1-29) sequence carrying an additional linker that forms a covalent bond to circulating albumin. Supplied lyophilised, with linker integrity verified per lot.

Structure and design rationale

This compound is the same modified GRF(1-29) backbone as the version without DAC, carrying the identical four substitutions, with one addition: a maleimidopropionic acid linker conjugated at the C-terminal lysine. That linker is the entire difference between the two compounds.

The mechanism is distinct from the reversible albumin binding used by fatty-acylated peptides such as semaglutide. A maleimide reacts with free thiols by Michael addition, and the reactive cysteine 34 of serum albumin is the abundant target. The result is a covalent bond rather than an equilibrium association, which is why the reported persistence of this molecule is measured on a very different timescale from that of the version without the linker.

Findings in the published research literature

The interesting comparison in the literature is against the same backbone without the linker, since receptor pharmacology is unchanged and any difference in observed profile is attributable to the conjugation chemistry alone. Receptor-level in-vitro work uses cAMP accumulation assays in GHRH receptor-expressing cells, as for the unconjugated analog.

Additional reported work concerns the conjugation reaction itself: rates of maleimide-thiol coupling with albumin, and the competing hydrolysis of the maleimide ring to an unreactive maleamic acid. That competition is the practical determinant of how much of a given preparation can actually conjugate, and it is the property most worth understanding before designing an experiment with this compound.

Analytical verification

Everything that applies to the unconjugated backbone applies here, with one addition that dominates: the maleimide must be intact. Maleimide hydrolyses to maleamic acid in aqueous conditions, adding 18 daltons and rendering the linker unable to conjugate. That hydrolysed species is chemically similar enough to co-elute closely, so both mass spectrometry and careful chromatography are needed to quantify it.

This is the release attribute that distinguishes a usable lot from an inert one, because a preparation of otherwise perfect peptide purity whose linker has hydrolysed will behave as the unconjugated compound. The D-alanine epimerisation risk and the C-terminal considerations of the parent backbone apply unchanged.

Handling and storage

Solubility	Soluble in water and neutral aqueous buffer.
Reconstitution	Dissolve gently and use promptly. Maleimide hydrolysis begins as soon as the peptide enters aqueous conditions, so time in solution before use directly reduces the conjugatable fraction.
Storage	Lyophilised powder at -20C, desiccated and protected from moisture. Moisture ingress into the lyophilised cake will hydrolyse the linker even without formal reconstitution.
Stability	Linker hydrolysis, not peptide degradation, is the limiting factor. Maleimide reactivity is also pH-sensitive: it is selective for thiols near neutral pH and reacts increasingly with amines as pH rises, so avoid basic buffers.