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ARA-290

For research and laboratory use only. Not for human or animal consumption.

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Storage & handling: Store at 2–8 °C (≤ –20 °C long-term), away from light. Ships at ambient temperature.

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Research teams, laboratory coordinators, and institutional procurement departments can order ARA-290 peptide through a secure, research-use-only ordering process. This compound is supplied exclusively to laboratories and scientific institutions operating within approved research frameworks.

To buy ARA-290 peptide, select the required unit quantity and proceed through the secure checkout. Discreet and reliable delivery is standard across all orders, with packaging designed to preserve compound integrity throughout transit. To order ARA-290 peptide online, institutional purchase orders are accepted alongside standard procurement methods.

This compound is not available by prescription and is not supplied for clinical, therapeutic, veterinary, or personal use.

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Express tracked

$25 per order · delivery in 3–5 days
  • Tracked door to door, dispatched within 24–48 business hours
  • Ambient shipping, safe for lyophilized peptides
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Regular tracked

$15 per order · delivery in 5–10 days
  • Free on orders over $200
  • Tracked door to door, dispatched within 24–48 business hours
  • CAS: 1208243-50-8
  • Chemical Formula: C₅₁H₈₄N₁₆O₂₁
  • Molecular Weight: 1257.3 g/mol
  • Peptide Sequence: XEQLERALNSS
  • Synonyms: Cibinetide, PHBSP
  • Shelf life: 24 months from the manufacturing date.

 

ARA-290 is a chemically synthesized eleven-amino acid peptide corresponding to a modified sequence derived from the helix B surface region of erythropoietin — a naturally occurring signaling protein. Its sequence incorporates specific residue modifications that preserve IRR binding affinity while eliminating engagement of the classical erythropoietin receptor homodimer. A homodimer is a receptor complex formed from two identical protein subunits; the classical erythropoietin receptor assembles in this configuration, while the innate repair receptor incorporates a different subunit combination.

This receptor selectivity is achieved through targeted amino acid substitutions at positions that determine classical receptor contact geometry. The resulting compound binds the IRR complex while remaining pharmacologically inert at the classical receptor — a property that is itself a subject of investigation in comparative receptor binding and structure-activity relationship research.

Helix B surface peptides are studied in laboratory research because they represent a class of receptor-selective molecular tools that allow investigators to dissect signaling pathway contributions within complex receptor family systems with greater precision than full-length protein ligands permit.

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ARA-290

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Dispatched in 24–48 business hours.

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