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Each peptide batch is tested and verified to meet or exceed 98โ99% purity (HPLC).
Store 2โ8 ยฐC (โคโ20 ยฐC long-term). RT exposure during transport acceptable. Protect from light.
99.2% On-Time Delivery
Tracked International Shipping
Refund Within 28 Days
Secure, Encrypted Checkout
$90.00
This product is available by prescription only
This product does not require a prescription
Each peptide batch is tested and verified to meet or exceed 98โ99% purity (HPLC).
Store 2โ8 ยฐC (โคโ20 ยฐC long-term). RT exposure during transport acceptable. Protect from light.
The product is delivered in powdered (lyophilized) form and must be properly reconstituted prior to research use.
ARA-290 peptide is sourced by research teams investigating the innate repair receptor โ a heteromeric receptor complex distinct from the classical erythropoietin receptor โ and its associated intracellular signaling cascades in controlled in vitro environments. The innate repair receptor is a tissue-protective receptor complex studied in laboratory models for its role in cellular stress response signaling, inflammatory mediator modulation, and cytoprotective pathway activation in non-haematopoietic cell systems.
ARA-290’s sequence is derived from the helix B surface of the erythropoietin molecule โ a region studied for IRR engagement โ and is modified to eliminate interaction with the classical erythropoietin receptor. This selectivity is the compound’s primary research utility: it allows investigators to study IRR-mediated signaling in isolation, without the confounding receptor crosstalk associated with full-length erythropoietin in cell-based assay systems.
Research applications include IRR binding affinity characterisation, inflammatory cytokine pathway modulation studies in cell culture models, cytoprotective signaling cascade investigation in metabolic and neuronal cell systems, and comparative receptor selectivity profiling across erythropoietin receptor family members.
ARA-290 peptide is investigated in research environments for its selective engagement of the innate repair receptor in non-haematopoietic cell model platforms. It is studied within controlled laboratory models examining downstream signaling pathway responses, including JAK2 activation โ Janus kinase 2 is an intracellular enzyme that initiates a signaling cascade following receptor engagement โ and STAT transcription factor phosphorylation. Phosphorylation is a molecular modification that activates or deactivates proteins by attaching a phosphate group; it is a primary readout in kinase signaling pathway research.
The compound is explored for experimental peptide research involving inflammatory mediator suppression in in vitro systems, where investigators examine how IRR activation influences cytokine expression profiles โ the pattern of inflammatory signaling proteins produced by stimulated cells โ under defined experimental conditions. Its receptor selectivity profile also makes it applicable to comparative receptor pharmacology studies examining the structural determinants of erythropoietin receptor family member differentiation.
ARA-290 peptide is supplied as a lyophilised powder. Lyophilisation is a freeze-drying process that stabilises the compound in solid form for laboratory storage and maintains peptide integrity prior to experimental use.
Recommended handling conditions:
This compound is not intended for use outside approved laboratory environments.
Each unit of ARA-290 peptide undergoes quality control testing prior to dispatch. Peptide purity is verified through high-performance liquid chromatography (HPLC), confirming compound concentration and the absence of significant impurities. Mass spectrometry is applied to validate the eleven-amino acid sequence and confirm the integrity of residue modifications at receptor selectivity-determining positions.
Batch-to-batch consistency is maintained through internal quality assurance standards across all production runs. Each pack size is accompanied by analytical documentation providing peptide purity data, sequence confirmation, and batch identifiers. This supports reproducible research peptide supply to institutions and laboratories in the United States and internationally, and meets the documentation requirements of structured receptor signaling research programme
ARA-290 is a chemically synthesised eleven-amino acid peptide corresponding to a modified sequence derived from the helix B surface region of erythropoietin โ 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 โ 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.
Novera Research delivers high-quality research peptides developed under strict manufacturing and quality-control standards. Each product is carefully synthesized, tested, and handled to ensure consistency, reliability, and transparency for advanced research applications.
High-purity, research-grade peptide synthesis
Analytical testing to verify quality and composition
Consistent batch-to-batch performance
Batch identification on every vial for traceability
Stored and shipped under controlled conditions
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