ARA-290
Also known as Cibinetide, Helix B surface peptide, pHBSP
ARA-290 (cibinetide) is a short, non-erythropoietic peptide modeled on erythropoietin's helix B surface. A research-use profile: its EPO-derived design, why 'non-erythropoietic' matters, and handling.
ARA-290 is an object lesson in how to take a large signaling protein and keep only the part you want. Its parent is erythropoietin — EPO — the hormone best known for driving red-blood-cell production. ARA-290 is designed to descend from EPO's structure while leaving that red-cell-stimulating activity behind. The word that captures this is the one that appears in nearly every description of it: non-erythropoietic.
This page keeps to the verifiable design story — where in EPO the peptide comes from, what 'non-erythropoietic' actually means, and how it is handled — without drifting into claims about outcomes.
ARA-290 (cibinetide) is a short peptide modeled on a solvent-exposed region — the helix B surface — of erythropoietin (EPO). It is deliberately non-erythropoietic: it is derived from EPO's structure but does not carry the part of EPO responsible for red-blood-cell signaling. Its short sequence is described here rather than enumerated to avoid overstating a residue list.
Derived from EPO's helix B — but non-erythropoietic
Erythropoietin is a folded protein with several helical regions. ARA-290 is modeled on residues from one solvent-exposed stretch of EPO known as the helix B surface — hence its other name, the helix B surface peptide (pHBSP). It reproduces a small, defined patch of the parent molecule rather than the whole protein.
The design intent is captured by the term non-erythropoietic. The receptor interaction responsible for EPO's classic red-blood-cell-stimulating effect involves a different part of the molecule; by drawing only on the helix B surface, ARA-290 is built to sit apart from that erythropoietic activity. This separation — EPO-derived structure without the red-cell signaling — is the single most important thing to understand about the peptide and the reason it exists as a distinct research entity.
A designed fragment, not a natural product
Unlike a peptide simply cleaved intact from a larger protein, ARA-290 is a deliberately engineered short peptide that mimics a surface region of EPO. That makes it a designed research tool: its value lies in isolating one structural feature of a complex hormone so that feature can be studied on its own, uncoupled from the rest of EPO's biology.
Because it is a defined short sequence, characterization is straightforward in principle — a certificate of analysis should map its mass and dominant chromatographic peak onto the intended peptide, tied to a batch identifier. Every lot we list is tied to its own certificate; verify yours by its batch number.
These are research areas the compound is associated with in the literature — not medical claims or intended uses.
Handling & storage
Supplied lyophilized. Stored sealed and cold; reconstituted with bacteriostatic water only when a protocol requires it, then kept refrigerated. Handle per accepted laboratory practice.
Verify a certificate by lot →Common questions
It means the peptide is derived from erythropoietin's structure but is designed not to carry EPO's red-blood-cell-stimulating activity. That activity involves a different part of the EPO molecule than the helix B surface ARA-290 is modeled on.
No. EPO is a full folded protein hormone; ARA-290 is a short peptide modeled on just one solvent-exposed region of it (the helix B surface), engineered specifically to leave the erythropoietic signaling behind.
Yes — cibinetide is the designated name for the same peptide, which is also described as the helix B surface peptide (pHBSP).
This monograph is a research-use reference. It describes composition and the contexts in which the compound has been studied — it is not medical advice, a description of effects, or a recommendation for use. Sold strictly for laboratory and research use; not for human or animal consumption.