A modified GRF(1-29). Substitutions resist enzymatic cleavage; an optional DAC linker adds albumin binding. Available with or without DAC. Read the CJC-1295 overview →
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Comparison
CJC-1295 vs Sermorelin
Two GH-axis GRF analogs, side by side: how they are built, how they differ, and what each is kept as a reference standard for. Both are GHRH(1-29) analogs. Sermorelin is the native GRF(1-29) fragment; CJC-1295 is a modified GRF(1-29), available with or without the DAC albumin-binding linker. The modifications, and the optional DAC, are the core difference.
Side by side
CJC-1295GH-Axis · GRF Analog
SermorelinGH-Axis · GRF Analog
Sequence / Structure
Modified GRF(1-29). Built on the same 29-residue growth-hormone-releasing fragment, with substitutions at positions known to be sites of enzymatic cleavage, and an optional DAC linker at the C-terminus.
Native GRF(1-29), 29 residues. The unmodified 1-29 region of human GHRH, the shortest fragment that retains the receptor-binding activity of the full-length hormone.
Family / Class
GH-axis GRF analog. The engineered member of the GHRH(1-29) family.
GH-axis GRF releasing peptide. The parent fragment the family is derived from.
Key modification
Stabilizing substitutions; optional DAC. Sequence changes resist enzymatic breakdown; the DAC (Drug Affinity Complex) form adds an albumin-binding linker. Offered with DAC or as the no-DAC variant.
None. Sermorelin is the unmodified reference fragment, with no stabilizing substitutions and no linker.
Synthesis
Fmoc solid-phase peptide synthesis, with added steps for the substitutions and, in the DAC form, for conjugating the albumin-binding linker.
Fmoc solid-phase peptide synthesis. A direct 29-residue assembly with no post-synthetic conjugation.
Characterization
RP-HPLC for purity profile, with identity confirmed by mass spectrometry. The DAC form is characterized for the conjugate.
RP-HPLC for purity profile, with identity confirmed by mass spectrometry on the intact 29-residue chain.
Storage
Supplied lyophilized; kept cold, dry, and dark for stability as a reference standard.
Supplied lyophilized; kept cold, dry, and dark for stability as a reference standard.
Research context
Studied as the engineered, cleavage-resistant GRF analog, and, in the DAC form, as a model for albumin-binding conjugation chemistry. RUO.
Studied as the native GHRH(1-29) reference fragment and the comparison point for analog work in the GRF family. RUO.
Characterization figures are method descriptions, not lot results. Batch documentation is available on request. For laboratory and research use only.
Common ground
What they share
CJC-1295 and Sermorelin are both GHRH(1-29) analogs, meaning both are built on the 1-29 region of growth-hormone-releasing hormone, the GRF(1-29) fragment. That fragment is the shortest stretch of the full-length hormone that still carries its receptor-binding activity, which is why it became the backbone for an entire family of GH-axis reference compounds. Sermorelin is that fragment in its native form; CJC-1295 is the same fragment engineered.
Because they share a backbone, they share a chemistry workflow. Both are assembled by Fmoc solid-phase peptide synthesis, both are purified and profiled by reversed-phase HPLC, and both have identity confirmed by mass spectrometry. Both ship lyophilized and are kept cold, dry, and dark. As reference standards, both are supplied for research use only, with batch documentation available on request.
The real distinction
How they differ
The difference is the modification. Sermorelin is the unmodified GRF(1-29) fragment, so it is, in effect, the reference point: the native sequence, assembled directly, with nothing added. CJC-1295 takes that same fragment and changes it. It carries substitutions at residues that are known sites of enzymatic cleavage, which makes the engineered chain more resistant to breakdown than the native fragment. That single design choice, stabilizing the sequence, is the core chemical distinction between the two.
CJC-1295 then introduces a second axis of difference that Sermorelin has no equivalent for: the DAC linker. DAC stands for Drug Affinity Complex, an albumin-binding group conjugated to the peptide. It is offered two ways, the DAC form and the no-DAC form, so the CJC-1295 standard is really a small set of related conjugates rather than a single molecule. The no-DAC variant is the stabilized fragment on its own; the DAC variant adds the albumin-binding chemistry on top. Sermorelin, by contrast, exists only as the one native fragment.
CJC-1295
Sermorelin
The native GRF(1-29) fragment, 29 residues, unmodified. The parent sequence and the comparison point for the family. Read the Sermorelin overview →
For the bench
Choosing a reference standard
From a chemistry standpoint, the two answer different reference questions. Sermorelin is the standard to reach for when the native GRF(1-29) sequence is the point of comparison, work that treats the unmodified fragment as the baseline against which modified analogs are read. It is the parent against which the rest of the family is measured.
CJC-1295 is the standard for work centered on the engineered analog itself, including its stabilizing substitutions and, in the DAC form, the albumin-binding conjugation chemistry. Because it is offered with or without DAC, the choice also includes which CJC-1295 variant matches the research context: the stabilized fragment alone, or the fragment plus linker. Both sit in the same GH-axis family of overviews, and identity and purity for either are established by the same methods, described under Standards & Verification.
At a glance
The key differences, in brief
Same backboneBoth are GHRH(1-29) analogs built on the GRF(1-29) fragment, the same receptor-binding region of growth-hormone-releasing hormone.
SermorelinThe native, unmodified GRF(1-29) fragment, 29 residues. The parent sequence and the family's comparison point.
CJC-1295A modified GRF(1-29). Substitutions resist enzymatic cleavage; offered with or without the DAC albumin-binding linker.
Core distinctionThe modifications and the optional DAC. Sermorelin adds nothing; CJC-1295 is the engineered, cleavage-resistant member of the same family.
Questions
Frequently asked
What is the difference between CJC-1295 and Sermorelin?
Both are GHRH(1-29) analogs built on the same growth-hormone-releasing fragment. Sermorelin is the native GRF(1-29) sequence itself. CJC-1295 is a modified GRF(1-29): it carries sequence substitutions that resist enzymatic cleavage, and it is offered with or without the DAC (Drug Affinity Complex) linker that lets the peptide bind serum albumin. The modifications, and the optional DAC, are the core chemical difference.
Are CJC-1295 and Sermorelin in the same class?
Yes. Both are GH-axis GRF analogs derived from growth-hormone-releasing hormone, specifically the 1-29 region that retains the receptor-binding activity of full-length GHRH. They sit in the same family of reference standards; CJC-1295 is the engineered member of that family and Sermorelin is the parent fragment.
How are CJC-1295 and Sermorelin synthesized?
Both are assembled by Fmoc solid-phase peptide synthesis and purified by reversed-phase HPLC, with identity confirmed by mass spectrometry. CJC-1295 adds steps for its stabilizing substitutions and, in the DAC form, for conjugating the maleimido-based albumin-binding linker. Sermorelin is the unmodified 29-residue chain, so its route is comparatively direct. The methods are described under Standards & Verification.
Are CJC-1295 and Sermorelin for research use only?
Yes. BioFusion supplies both as reference standards for laboratory and research use only. They are not for human or veterinary consumption, and buyers are responsible for compliance with all applicable laws and regulations. Batch documentation is available on request.
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