Ara 290 For Sale

ARA-290 (Cibinetide) is available for purchase as a high-purity lyophilized research peptide specifically synthesized for in vitro and preclinical laboratory investigation. Derived from the helix B domain of erythropoietin, ARA-290 selectively targets the innate repair receptor to evaluate inflammatory signaling pathways and tissue-protection mechanisms without inducing erythropoiesis in experimental models.

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ARA-290 (Cibinetide) is available for purchase as a high-purity lyophilized research peptide specifically synthesized for in vitro and preclinical laboratory investigation. Derived from the helix B domain of erythropoietin, ARA-290 selectively targets the innate repair receptor to evaluate inflammatory signaling pathways and tissue-protection mechanisms without inducing erythropoiesis in experimental models.

Reviewed by PX1 Research scientific team

Key takeaways

  • When procurement officers and academic investigators search for [ara 290 for sale](/product/ara-290), verifying chemical purity, sequence fidelity, and analytical compliance is essential to maintaining experimental reproducibility.
  • ARA-290 is a synthetic peptide derived from the three-dimensional structure of human erythropoietin (EPO).
  • The primary mechanism of ARA-290 centers on its selective agonism of the Innate Repair Receptor (IRR).
  • Extensive academic literature documents the evaluation of ARA-290 across diverse rodent models of ischemia-reperfusion injury, neuroinflammation, and metabolic stress.

Sourcing High-Purity ARA-290 for Laboratory Research

When procurement officers and academic investigators search for ara 290 for sale, verifying chemical purity, sequence fidelity, and analytical compliance is essential to maintaining experimental reproducibility. ARA-290—also recognized in scientific literature as Cibinetide or pyroglutamate helix B surface peptide (pHBSP)—is an 11-amino-acid peptide designed to interact selectively with heteromeric receptor complexes involved in cellular stress responses.

Because structural degradation or counter-ion contamination can alter binding kinetics in receptor assays, laboratory researchers require reference-standard materials produced under rigid quality controls. PX1 Research supplies USA-manufactured ARA-290 produced in GMP-compliant facilities, ensuring each batch fulfills stringent criteria for identity, purity, and bio-burden control prior to deployment in cell culture or animal models.

Molecular Structure and Derivation from Erythropoietin

ARA-290 is a synthetic peptide derived from the three-dimensional structure of human erythropoietin (EPO). Native EPO is a 165-amino-acid glycoprotein primarily recognized for stimulating erythropoiesis via homodimeric erythropoietin receptor (EPOR2) activation. However, structural biology studies revealed that EPO's tissue-protective actions occur through a distinct, low-affinity heteromeric receptor complex.

Specifically, ARA-290 isolates the linear sequence corresponding to the aqueous-exposed helix B domain of EPO. The primary sequence—pyroglutamate-glutamate-proline-threonine-threonine-asparagine-lysine-tyrosine-phenylalanine-valine-alanine (pGlu-Glu-Pro-Thr-Thr-Asn-Lys-Tyr-Phe-Val-Ala)—is synthetically modified at the N-terminus with a pyroglutamyl residue to enhance metabolic stability against aminopeptidase degradation during in vitro research.

By isolating this aqueous-exposed domain, researchers obtain a peptide that retains the signaling characteristics associated with tissue repair and anti-inflammatory cascades while omitting the domain responsible for binding the homodimeric EPO receptor. Consequently, ARA-290 provides a specialized chemical probe to evaluate non-hematopoietic pathways without confounding hematological variables.

Mechanism of Action: Selective Innate Repair Receptor (IRR) Binding

The primary mechanism of ARA-290 centers on its selective agonism of the Innate Repair Receptor (IRR). The IRR is a heterotrimeric receptor complex consisting of two erythropoietin receptor subunits and two common beta receptor (CD131) subunits (EPOR/CD131 heterodimer). Unlike the classical homodimeric EPOR, which is constitutively expressed on erythroid progenitor cells, the IRR is expressed at low levels under basal conditions but is rapidly upregulated on endothelial cells, macrophages, cardiomyocytes, and neuronal tissue following metabolic stress or cytokine exposure.

Upon binding to the IRR, ARA-290 initiates intracellular signaling cascades that modulate nuclear factor kappa B (NF-κB) transcription. Preclinical models indicate that IRR activation leads to the inhibition of IκB phosphorylation, thereby preventing the translocation of NF-κB to the nucleus and suppressing the downstream transcription of pro-inflammatory cytokines such as TNF-α, IL-1β, and IL-6.

Additionally, IRR signaling stimulated by ARA-290 promotes the activation of the Akt/protein kinase B pathway and endothelial nitric oxide synthase (eNOS). In cell culture models, this signaling axis promotes cell survival, reduces mitochondrial ROS production, and inhibits apoptotic cascades mediated by caspase-3 and caspase-9.

Preclinical Literature: Inflammatory Signaling and Tissue Protection

Extensive academic literature documents the evaluation of ARA-290 across diverse rodent models of ischemia-reperfusion injury, neuroinflammation, and metabolic stress. Research published in peer-reviewed journals demonstrates that administration of ARA-290 in rodent models of peripheral neuropathy mitigates mechanical allodynia and thermal hyperalgesia by attenuating microglial activation within the spinal dorsal horn.

In models of metabolic dysregulation and diabetic microvascular injury, preclinical studies suggest that ARA-290 administration preserves microvascular density, restores endothelial barrier function, and attenuates small-fiber nerve degeneration. Researchers investigating inflammatory bowel disease models have noted that IRR activation by ARA-290 reduces mucosal cytokine levels and preserves tight junction integrity in intestinal epithelial monolayers.

Furthermore, in renal and myocardial ischemia-reperfusion experiments, ARA-290 treatment demonstrated significant attenuation of tissue necrosis and neutrophil infiltration. These findings underscore the utility of ARA-290 as a standard tool for dissecting the molecular mechanisms governing innate tissue repair.

Non-Erythropoietic Profile in Experimental Designs

A major limitation of wild-type recombinant human EPO (rhEPO) in long-term tissue protection research is its potent stimulation of red blood cell production, which increases hematocrit and blood viscosity, introducing confounding hemodynamic variables. ARA-290 circumvents this experimental limitation entirely.

Structural and biophysical binding assays confirm that ARA-290 exhibits negligible affinity for the classical (EPOR)2 homodimer responsible for erythropoiesis. In preclinical rodent and non-human primate studies, repeated administration of ARA-290 at high concentrations produced no statistically significant changes in red blood cell counts, hemoglobin concentration, hematocrit levels, or reticulocyte counts.

This structural selectivity makes ARA-290 the preferred candidate for long-term experimental protocols focused exclusively on tissue preservation, anti-inflammatory signaling, and neuroprotective pathways where hematological stability is mandatory.

Comparative Analysis: ARA-290 vs. Related Research Compounds

When designing protocols evaluating cytoprotection, tissue repair, or anti-inflammatory pathways, researchers often compare ARA-290 against other characterized signal-modulating peptides in our all peptides catalog. Selecting the appropriate compound depends heavily on the specific receptor system and downstream signaling pathways under investigation.

For example, while ARA-290 operates specifically through the EPOR/CD131 innate repair receptor to suppress NF-κB signaling, compounds such as BPC-157 research peptides influence tissue repair primarily through VEGFR2 activation, FAK-Src signaling, and growth factor upregulation. Conversely, peptides like KPV target the melanocortin-1 receptor (MC1R) to inhibit inflammatory mediators. The table below highlights key functional distinctions among these common research compounds:

Comparing these distinct mechanisms allows laboratory personnel to select the precise peptide probe—or combination of probes—required to isolate target signaling pathways in cytoprotection and inflammation assays.

Analytical Quality Standards: HPLC, MS, and Endotoxin Control

To ensure high experimental reproducibility, research peptides must undergo rigorous analytical verification. PX1 Research enforces strict quality control protocols for every lot of ARA-290 produced and distributed. Every batch is evaluated in an ISO 17025 accredited laboratory using dual-spectrum analytical procedures.

Purity is verified using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC). The resulting chromatogram must demonstrate a sharp, symmetrical primary peak corresponding to ARA-290, with total integrated chemical purity exceeding 98.0%. Residual counter-ions, truncated synthetic sequences, and deletion peptides are strictly quantified and kept below rigorous baseline tolerances.

Molecular identity is unequivocally confirmed via Electrospray Ionization Mass Spectrometry (ESI-MS), verifying that the observed mass-to-charge ratio matches the theoretical molecular weight of 1257.4 Da. Crucially, because ARA-290 is frequently utilized in cell culture assays and immunological studies sensitive to bacterial contaminants, every lot undergoes chromogenic LAL testing to ensure endotoxin levels remain under strict limits (<0.01 EU/mg).

Laboratory Handling, Reconstitution, and Storage Protocols

ARA-290 is supplied as a sterile, lyophilized cake inside sealed borosilicate glass vials to maximize chemical stability during transport and storage. Proper handling protocols must be maintained in the laboratory to prevent peptide degradation or aggregation.

Upon arrival, un-reconstituted lyophilized ARA-290 should be stored in a freezer at -20°C or -80°C, protected from light and moisture. Under these conditions, the lyophilized powder maintains structural integrity for up to 24 months. Prior to opening, vials should be allowed to equilibrate to room temperature inside a desiccator to prevent atmospheric moisture condensation on the cake.

For reconstitution, laboratory grade Bacteriostatic Water or sterile 0.9% Sodium Chloride Injection, USP should be introduced slowly along the glass wall of the vial. Direct forceful jet spraying onto the lyophilized cake should be avoided to prevent mechanical shear stress. The vial should be gently swirled until complete dissolution is achieved; vigorous vortexing is strictly prohibited.

Once reconstituted, aqueous solution aliquots should be stored at 2°C to 8°C for short-term experimentation (up to 7 days) or stored in single-use working aliquots at -80°C to avoid repeated freeze-thaw cycles.

Verifying Supplier Integrity and Lot-Specific COAs

Navigating the research peptide marketplace requires strict due diligence. Academic and industrial buyers seeking wholesale research peptides must ensure that vendors provide transparent, lot-specific documentation rather than generic static images or outdated analytical certificates.

PX1 Research maintains complete lot traceability from raw amino acid synthesis through final packaging. Every shipment of ARA-290 is accompanied by a downloadable, lot-matched Certificate of Analysis (COA) detailing the exact RP-HPLC chromatogram, mass spectrometry readout, net peptide content, and endotoxin assay results. All orders ship directly from our state-of-the-art logistics hubs in California and Arizona, with same-day dispatch for orders finalized before standard cutoff times.

Frequently Asked Questions

What is the primary target receptor of ARA-290 in preclinical research?

ARA-290 targets the Innate Repair Receptor (IRR), a heterotrimeric complex composed of two erythropoietin receptor (EPOR) subunits and two common beta receptor (CD131) subunits.

Does ARA-290 stimulate erythropoiesis in animal models?

No. Preclinical evidence confirms that ARA-290 lacks affinity for the homodimeric (EPOR)2 receptor responsible for red blood cell production, demonstrating a non-erythropoietic profile.

What purity level is guaranteed for PX1 Research ARA-290?

Every lot of ARA-290 offered by PX1 Research is verified by RP-HPLC to exceed 98.0% chemical purity, backed by lot-specific ESI-MS identity verification.

How is endotoxin testing performed on ARA-290?

Endotoxin levels are measured using a validated chromogenic Limulus Amebocyte Lysate (LAL) assay to ensure levels remain below 0.01 EU/mg, preventing cell culture contamination.

What solvents are recommended for reconstituting ARA-290 for lab assays?

ARA-290 is readily soluble in standard laboratory diluents, including Bacteriostatic Water, Phosphate-Buffered Saline (PBS, pH 7.4), or sterile 0.9% saline.

How should lyophilized ARA-290 be stored upon receipt?

Lyophilized ARA-290 should be stored at -20°C or -80°C in a dry environment protected from direct light, where it remains stable for up to 24 months.

Where does PX1 Research manufacture and ship ARA-290?

PX1 Research peptides are manufactured in US-based GMP-compliant facilities and dispatched directly from facilities located in California and Arizona.

Is ARA-290 suitable for human consumption or clinical administration?

No. ARA-290 is provided strictly as a synthesized research chemical for in vitro, cell culture, and preclinical laboratory experimentation. It is not for human or veterinary use.

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All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.