CJC-1295 (No DAC)

The table below records the chemical identity of CJC-1295 (No DAC) as supplied by Strand Peptide Research. These values describe the material itself — its registry number, empirical formula, primary structure and formula mass — and are provided so that laboratory staff can cross-check an incoming vial against their own records, purchase orders and analytical data before it enters an experiment. Identity data is descriptive chemistry only and says nothing about how the material behaves in any living system.

Where a sequence is shown in one-letter code, standard IUPAC single-letter amino acid abbreviations apply; three-letter notation is used where a residue is non-standard, a D-isomer, or otherwise cannot be written in one-letter form. Formula masses are average (not monoisotopic) masses and are quoted for the free base or the stated salt/complex form as indicated. Small differences between the mass shown here and the mass reported on an analytical report normally reflect counter-ion content, residual solvent or residual water rather than an identity difference.

Analytical testing for peptide material of this class is conventionally performed by reversed-phase HPLC with UV detection at 214 nm, with identity confirmed by mass spectrometry. 214 nm is the standard wavelength for the peptide bond and therefore the appropriate detector setting for quantifying peptide-related impurities. Mass spectrometry is typically electrospray ionisation (ESI-MS) or matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF), with the observed mass compared against the calculated formula mass shown in the identity table above.

The manufacturer's release specification is ≥99% purity by HPLC. Analytical documentation held for this material can be requested before you order. Because chromatographic purity is a measurement of a specific lot and not a property of the compound in general, any report should always be read alongside the material it was issued for. How we document purity.

The guidance below is laboratory material-handling information for trained personnel. It describes how to keep the supplied material chemically intact in a laboratory setting and is not instruction for use in or on any human or animal.

• Sealed lyophilised powder: store at -20 °C in the original sealed vial, protected from light and moisture. Under these conditions lyophilised material of this class is typically assigned a 24-month retest period from the date of manufacture. Short periods at 2-8 °C during transit or handling are acceptable and are accounted for in the shipping validation.
• Before opening: allow the vial to equilibrate to room temperature before breaking the seal. Opening a cold vial draws in ambient humidity, and adsorbed water is the single most common cause of premature degradation in lyophilised peptide stock.
• Reconstitution: introduce the diluent slowly down the inner wall of the vial rather than directly onto the powder cake, and swirl gently until dissolved. Do not shake or vortex — mechanical shear and the resulting air-liquid interface promote aggregation and surface denaturation.
• After reconstitution: hold the solution at 2-8 °C and protect it from light. For laboratory stock solutions of this class a working window of roughly 14-28 days at 2-8 °C is commonly applied, with aliquots stored at -20 °C or below where longer retention is required.
• Freeze-thaw: aliquot into single-use volumes before freezing. Each freeze-thaw cycle concentrates solutes at the ice front and measurably increases aggregation; more than two or three cycles should be avoided for any peptide stock.
• Labware: low-binding tubes and pipette tips reduce losses through surface adsorption, which becomes significant for dilute solutions of longer, highly charged peptides.
• Personal protection: handle as a research chemical of unknown hazard — gloves, eye protection and a laboratory coat, with weighing of powders performed in a suitable enclosure.

The four substitutions relative to native GRF(1-29) — D-Ala2, Gln8, Ala15 and Leu27 — remove the oxidisable methionine and the principal dipeptidyl cleavage site, which is why this analogue is reported as substantially more persistent in solution than sermorelin. Lyophilised peptide powders of this class are generally stable for extended periods when held at -20 °C and protected from light and moisture. In aqueous solution the dominant degradation routes reported for short peptides are hydrolysis of labile amide bonds, oxidation of methionine and tryptophan residues, and deamidation at asparagine and glutamine residues, all of which accelerate with temperature, repeated freeze-thaw cycling and exposure to light.

Published stability work on synthetic peptides consistently identifies the same set of variables as controlling: temperature, pH, ionic strength, oxygen and light exposure, adsorption to container surfaces, and the number of freeze-thaw cycles applied. Reported half-lives in biological matrices — plasma, serum, whole blood — are dominated by enzymatic proteolysis and are not transferable to a clean buffered solution held in a refrigerator, where chemical degradation routes such as hydrolysis, oxidation and deamidation set the limit instead. When comparing figures between sources, always check which matrix, temperature and analytical method were used.

Strand does not publish an internal accelerated-stability dataset for this compound. Where a laboratory requires a documented stability profile for its own quality system, the practical approach is to hold retained aliquots under the intended storage conditions and re-inject them by HPLC at defined intervals, comparing the main-peak area against a reference chromatogram for the same material. The primary literature indexed in the references section below is the appropriate starting point for compound-specific data.

CJC-1295 (No DAC) is supplied in 5mg, 10mg presentations, one unit per vial. Vials are Type I borosilicate glass, closed with a bromobutyl rubber stopper and sealed with a crimped aluminium cap, then labelled with the product name, nominal quantity, lot number and a research-use-only statement. Type I glass is used because it is the most hydrolytically resistant pharmaceutical glass grade and minimises ion leaching into the contents.

Orders are packed in rigid outer cartons with moulded inserts or foam separators so that individual vials cannot contact one another in transit. Consignments are dispatched from Melbourne, Victoria. Orders placed during the launch pre-order are dispatched together, about six weeks after pre-orders close, once stock lands in Melbourne. Tracking details are emailed when your order ships.

Lyophilised material of this class is stable at ambient temperature for the short duration of a domestic transit leg, so standard shipping is used without a cold chain unless a customer specifically arranges otherwise. On arrival, transfer the vials to their long-term storage condition promptly and inspect the contents: the powder cake should be intact and free of discolouration, and the seal should be undamaged. Report any damaged, discoloured or short-delivered item to us before use so the lot can be traced.

Other research compounds in our catalogue that share a category or handling profile with CJC-1295 (No DAC):

• CJC-1295 with DACC165H269N47O46 · 3647.23 g/mol
• GHRP-2C45H55N9O6 · 817.99 g/mol
• GHRP-6C46H56N12O6 · 873.01 g/mol
• IpamorelinC38H49N9O5 · 711.85 g/mol

The sources below are provided as entry points to the primary scientific and chemical literature for CJC-1295 (No DAC). They are listed for reference and identification purposes and do not constitute a claim about the material.

1. PubChem Compound Summary: Modified GRF 1-29 CJC-1295. National Center for Biotechnology Information, National Library of Medicine (US). View source
2. Indexed primary literature for Modified GRF 1-29 CJC-1295. MEDLINE/PubMed bibliographic database, National Library of Medicine (US). View source
3. Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27(4):544-575. View source