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CJC-1295 without DAC 2 mg

CJC-1295 without DAC is a synthetic 30-amino acid peptide analogue studied for its interactions with GHRH receptor pathways in experimental models.

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CJC-1295 without DAC is a synthetic 30-amino acid peptide analogue studied for its interactions with GHRH receptor pathways in experimental models. Also referred to as Modified GRF(1-29), the compound incorporates amino acid substitutions that confer enhanced protease resistance relative to native GHRH(1-29) while retaining GHRH receptor binding affinity.

Unlike the DAC-modified variant, CJC-1295 without DAC lacks the albumin-binding moiety, producing a shorter stability window in experimental systems that is studied for its utility in research protocols modelling pulsatile growth hormone secretagogue signalling.

Research applications include GHRH receptor pathway studies, pulsatile growth hormone signalling research, and comparative DAC versus non-DAC peptide pharmacology.

 

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3D Molecular Structure

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CJC-1295 without DAC 2 mgVial | 10 vial
Chemical Formula C152H252N44O42
Synonyms Modified GRF 1-29, Mod GRF 1-29, CJC-1295 no DAC
Molar Mass 3367.9 g/mol
CAS Number 446262-90-4
PubChem CID 91976842
Total Compound Content 2mg per vial
Shelf Life 36 months
CJC-1295 without DAC is a synthetic GHRH analogue incorporating four amino acid substitutions (D-Ala2, Gln8, Ala15, Leu27) relative to native GHRH(1-29), studied for enhanced protease resistance and selective GHRH receptor affinity in laboratory models. The absence of the Drug Affinity Complex (DAC) modification means this variant does not engage albumin-binding mechanisms, producing a shorter stability window in experimental systems compared to CJC-1295 with DAC. This characteristic is studied for its relevance to research protocols modelling pulsatile growth hormone secretagogue signalling patterns, which more closely approximate endogenous growth hormone release dynamics than the sustained signalling profile associated with the DAC-modified variant. Comparative research protocols examining both CJC-1295 variants allow investigators to characterise how the presence or absence of the albumin-binding DAC modification influences receptor engagement duration and downstream signalling profiles in GHRH pathway research. Independently third-party HPLC-tested; COA available per batch.

Results refer to the tested sample. Check the batch and date in the report.

CJC-1295 without DAC (2606-ED-CJ)
July 22, 2026
What distinguishes CJC-1295 without DAC from CJC-1295 with DAC in GHRH research models?

CJC-1295 without DAC lacks the maleimidopropionyl-lysine Drug Affinity Complex modification present in the DAC variant, meaning it does not engage albumin-binding mechanisms that extend peptide stability in biological research systems. This results in a shorter stability window studied for its utility in experimental protocols modelling pulsatile growth hormone secretagogue signalling, which more closely approximates endogenous GHRH release patterns, in contrast to the sustained signalling profile associated with the DAC-modified variant.

Why is CJC-1295 without DAC also referred to as Modified GRF(1-29) in research literature?

CJC-1295 without DAC is structurally equivalent to Modified GRF(1-29) — a tetrasubstituted analogue of the native GHRH(1-29) sequence incorporating D-Ala2, Gln8, Ala15, and Leu27 substitutions for enhanced protease resistance. The naming distinction in research literature reflects historical convention: 'CJC-1295' strictly denotes the DAC-modified form, while 'CJC-1295 without DAC' and 'Modified GRF(1-29)' both describe the unmodified tetrasubstituted sequence without the albumin-binding moiety.

How does the single vial format compare to the 10-vial KIT format for experimental protocol planning?

The single 2mg vial is suited to pilot studies, individual experimental runs, or protocols requiring a defined single-dose quantity, while the 10-vial KIT format supports larger research programs requiring multiple independent experimental replicates or extended timelines with consistent inter-vial compound quality. Researchers select format based on the total peptide quantity needed across all experimental arms and storage requirements for unused compound.

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