ARA 290 (cibinetide) is an 11-amino acid research peptide derived from the helix B domain of erythropoietin, specifically engineered to target the innate repair receptor without stimulating red blood cell production. PX1 Research provides reference-grade ARA 290 manufactured under stringent US quality controls for in vitro and preclinical research applications.
ARA 290 (cibinetide) is an 11-amino acid research peptide derived from the helix B domain of erythropoietin, specifically engineered to target the innate repair receptor without stimulating red blood cell production. PX1 Research provides reference-grade ARA 290 manufactured under stringent US quality controls for in vitro and preclinical research applications.
To execute an ARA 290 peptide buy for institutional or laboratory research, investigators must source high-purity reference reagents supported by comprehensive analytical documentation. ARA 290 (also known as cibinetide) is an 11-amino-acid peptide derived from the structural domain of erythropoietin (EPO). It selectively activates the innate repair receptor (IRR) without stimulating erythropoiesis, making it a critical tool for studying tissue protection and anti-inflammatory pathways in vitro and in preclinical animal models.
When procuring reference compounds from our all research peptides catalog, research teams require absolute certainty regarding purity, sequence identity, and batch consistency. PX1 Research supplies ARA 290 synthesized in GMP-compliant facilities within the United States. Every production lot undergoes independent verification via High-Performance Liquid Chromatography (HPLC) and Mass Spectrometry (MS) to ensure a minimum purity threshold of 98%. All orders ship directly from our fulfillment centers in California and Arizona, with same-day dispatch for orders placed before cutoff times Monday through Friday.
ARA 290 is an 11-residue synthetic peptide with the sequence Pyroglu-Glu-Gln-Leu-Glu-Arg-Ala-Leu-Asn-Ser-Ser-OH. It was designed by isolating the spatial domain of erythropoietin responsible for tissue protective signaling while discarding the classical hematopoietic binding site. Erythropoietin normally interacts with the homodimeric EPO receptor (EPOR2) to stimulate erythropoiesis. However, under conditions of cellular stress or tissue damage, an alternative heteroreceptor complex is expressed.
This heteroreceptor, termed the innate repair receptor (IRR), consists of one EPO receptor subunit and one beta common receptor subunit (EPOR-βc). Classical EPO binds to the IRR with low affinity, requiring elevated concentrations that simultaneously trigger unwanted red blood cell proliferation. ARA 290 was engineered to bind selectively to the IRR heteromer with high specificity, leaving the homodimeric EPOR2 uninfluenced. Laboratory researchers studying erythropoietin receptor mechanisms utilize ARA 290 to isolate local tissue-repair cascades from systemic hematological responses.
The primary mechanism of ARA 290 involves selective agonism of the heterodimeric innate repair receptor (EPOR-βc). Activation of the IRR triggers downstream intracellular signaling cascades that mediate tissue preservation, attenuate apoptosis, and suppress proinflammatory gene expression. Preclinical models demonstrate that IRR ligation initiates Janus kinase 2 (JAK2) phosphorylation, which subsequently recruits signal transducer and activator of transcription 3 (STAT3) and the phosphatidylinositol 3-kinase (PI3K)/Akt pathway.
In vitro assays indicate that activation of the Akt/STAT3 pathway by ARA 290 reduces the nuclear translocation of Nuclear Factor Kappa B (NF-κB). NF-κB is a master transcription factor responsible for upregulating inflammatory cytokines such as Tumor Necrosis Factor-alpha (TNF-α), Interleukin-1 beta (IL-1β), and Interleukin-6 (IL-6). By blunting NF-κB activation, ARA 290 effectively mitigates hyper-inflammatory signaling in cultured endothelial cells, macrophages, and neural tissue models. For a broader overview of these pathways, visit the PX1 research library.
In animal models of systemic inflammation and metabolic stress, ARA 290 has been evaluated for its capacity to reduce local tissue disruption and circulating cytokine levels. Preclinical studies using rodent models of metabolic dysfunction suggest that ARA 290 administration correlates with decreased macrophage infiltration into target tissues, preserving cellular architecture without altering hematocrit levels.
Furthermore, in vitro data indicate that ARA 290 modulates the polarization of macrophages from the proinflammatory M1 phenotype to the pro-resolving M2 phenotype. This shift is accompanied by a marked reduction in reactive oxygen species (ROS) production and down-regulation of inducible nitric oxide synthase (iNOS). Researchers investigating inflammatory signaling research utilize ARA 290 to analyze the precise molecular checkpoints governing macrophage phenotype transitions during sustained cellular stress.
Small-fiber neural degradation and peripheral neuropathic models represent a major area of investigation for ARA 290. The innate repair receptor is expressed at low baseline levels in peripheral nerve structures, but undergoes rapid upregulation following axonal injury, ischemia, or metabolic toxicity. Preclinical rodent models of peripheral neuropathy demonstrate that selective IRR stimulation promotes neurite outgrowth and protects Schwann cell integrity.
In cell culture models of metabolic and chemotherapy-induced cytotoxicity, exposure to ARA 290 preserved mitochondrial membrane potential within dorsal root ganglion (DRG) neurons. Preclinical evidence suggests that this mitochondrial preservation prevents the activation of caspase-3 and caspase-9, thereby blocking apoptotic cascades. These properties make ARA 290 a valuable tool for laboratories exploring neuroprotective pathways and small-fiber axonal regeneration mechanisms.
When designing preclinical protocols for tissue repair and inflammation modulation, investigators frequently compare ARA 290 against other specialized research peptides. While ARA 290 operates strictly through the heterodimeric innate repair receptor (EPOR-βc), the C-terminal tripeptide KPV peptide functions predominantly via alpha-melanocyte-stimulating hormone (α-MSH) pathways to suppress NF-κB transcription.
Conversely, compounds such as BPC-157 peptide exert cytoprotective effects through growth factor up-regulation (such as VEGF) and nitric oxide pathway modulation, whereas TB-500 peptide acts via actin sequestration and cell migration signaling. While BPC-157 and TB-500 are broadly evaluated in musculoskeletal recovery models, ARA 290 is uniquely tailored for target studies demanding absolute isolation from hematopoietic activation while focusing on neural, renal, and vascular IRR signaling networks. Institutional research groups interested in compound cross-evaluations can set up bulk peptide purchasing accounts for multi-peptide comparative studies.
Proper handling and preparation are required to preserve the structural integrity of ARA 290 during in vitro and animal research protocols. ARA 290 is supplied as a lyophilized (freeze-dried) cake or powder. Prior to reconstitution, lyophilized vials should be stored in a dry environment at -20°C for short-term storage or -80°C for long-term preservation to prevent hydrolytic degradation.
For laboratory reconstitution, researchers should allow the vial to equilibrate to room temperature before adding a solvent to prevent moisture condensation. Common analytical solvents include sterile Bacteriostatic Water (0.9% benzyl alcohol) or sterile Phosphate-Buffered Saline (PBS, pH 7.4). Solvents should be gently injected against the inner glass wall of the vial, followed by gentle swirling. Gentle rotation is recommended; vigorous vortexing should be avoided as it may cause shear stress and peptide aggregation. Reconstituted solution aliquots should be stored at 2°C to 8°C and evaluated within short experimental timeframes, or sub-aliquoted and stored at -80°C to minimize freeze-thaw cycles.
Analytical rigor is paramount when acquiring peptides for research. Substandard reagents containing residual trifluoroacetic acid (TFA), truncated peptide sequences, or high bacterial endotoxin levels can invalidate experimental outcomes by inducing non-specific cellular responses or cytotoxic effects.
PX1 Research enforces strict quality control standards for every batch of ARA 290. Each lot undergoes standard reversed-phase HPLC (RP-HPLC) to confirm chemical purity exceeds 98%. Electrospray Ionization Mass Spectrometry (ESI-MS) is conducted concurrently to verify exact molecular weight (1257.37 Da theoretical). Furthermore, every batch undergoes chromogenic Limulus Amebocyte Lysate (LAL) testing to confirm endotoxin levels remain strictly below <0.01 EU/μg, ensuring that in vitro cellular assays are free from lipopolysaccharide (LPS) contamination.
Inconsistent peptide manufacturing and delayed international supply chains present significant challenges for academic and commercial laboratories. Overseas suppliers often lack traceable lot documentation, ISO 17025 accredited analytical validation, or standardized synthesis protocols, leading to batch-to-batch variation that compromises scientific reproducibility.
PX1 Research addresses these challenges by maintaining 100% US-based synthesis and analytical testing protocols within ISO 17025 certified laboratory environments. Orders are fulfilled directly from facilities in California and Arizona, providing fast shipping with thermal-controlled packaging. Qualified laboratories, universities, and contract research organizations (CROs) can access lot-specific Certificates of Analysis (COAs) directly through our verification portal prior to experimental deployment.
What primary receptor does ARA 290 target in research models?
ARA 290 selectively binds to the innate repair receptor (IRR), a heteromer composed of one erythropoietin receptor (EPOR) subunit and one beta common receptor (βc) subunit. It does not bind to the classical EPOR homodimer involved in erythropoiesis.
How does ARA 290 differ from native erythropoietin (EPO)?
Native EPO activates both the hematopoietic EPOR homodimer and the tissue-protective IRR heteromer. ARA 290 is an 11-amino acid peptide derived from helix B of EPO that exclusively targets the IRR, allowing researchers to study tissue repair without altering red blood cell counts.
What analytical purity level is guaranteed for PX1 Research ARA 290?
Every lot of ARA 290 from PX1 Research is verified via RP-HPLC and Mass Spectrometry to guarantee a minimum chemical purity of 98.0%, supported by lot-specific Certificates of Analysis.
What are the recommended storage conditions for lyophilized ARA 290?
Lyophilized ARA 290 should be stored at -20°C for standard lab storage or -80°C for long-term stability. Vials should be kept away from light and direct moisture until reconstitution.
How should ARA 290 be reconstituted for in vitro experimental use?
Reconstitute ARA 290 using sterile PBS (pH 7.4) or sterile bacteriostatic water by slowly introducing the liquid along the internal vial wall. Gently swirl the solution until fully dissolved; avoid high-speed vortexing.
What are the endotoxin limits for PX1 Research peptides?
PX1 Research conducts LAL endotoxin testing on all peptide lots, ensuring endotoxin content remains strictly below <0.01 EU/μg (<0.5 EU/mg) to prevent non-specific immune activation in laboratory assays.
Where does PX1 Research ship ARA 290 orders from?
All PX1 Research compounds are synthesized and stored in the United States, shipping directly from our primary distribution centers in California and Arizona with same-day fulfillment M–F.
Can ARA 290 be ordered in bulk or custom quantities for institutional labs?
Yes. Institutional accounts, university departments, and CROs can request bulk lot reserves and specialized packaging options through the PX1 Research wholesale portal.
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.