B7-33 Peptide for Sale | The Next-Generation Relaxin Mimetic for Research

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• • Alternative Designations: (B7-33)H2, GTPL9321, Biased RXFP1 Agonist
  • Amino Acid Sequence: VIKLSGRELVRAQIAISGMSTWSKRSL
  • PubChem Identifier: CID 118164840

• • Functionally Selective RXFP1 Receptor Activation: Relaxin family signaling typically targets four native receptors (RXFP1/2 and RXFP3/4). B7-33 is documented as the first functionally selective, small-molecule agonist of the RXFP1 receptor. Unlike native H2-relaxin, which generates widespread spikes in intracellular cAMP across both RXFP1 and RXFP2 cell lines, B7-33 bypasses cAMP generation entirely. It remains largely unstructured in a resting state, assuming its precise functional confirmation exclusively upon direct physical interaction with the target RXFP1 binding pocket.
  • Preferential pERK1/2 Signaling over cAMP: In preclinical fibroblast models, B7-33 selectively initiates intracellular signal coupling via the phosphorylated extracellular signal-regulated kinase (pERK1/2) pathway. Because the pERK cascade regulates vital cell-cycle checkpoints, researchers use this peptide to observe localized cell cycle arrest at the G1 phase. This focused pathway activation provides an exceptional framework for investigating neurodegenerative conditions, metabolic cellular behaviors, and ligand-directed receptor trafficking behavior.
  • Heterodimer Coupling and MMP-2 Collagen Degradation: To execute its anti-fibrotic potential, B7-33 prompts RXFP1 to bind with angiotensin II type 2 receptors, forming constitutive RXFP1–AT2R heterodimers. This specific structural coupling drives an intense upregulation of matrix metalloproteinase-2 (MMP-2)—the primary enzyme responsible for breaking down extracellular collagen matrices. Preclinical cardiac and renal myofibroblast cultures confirm that B7-33 matches full-length relaxin’s potency in stimulating MMP-2 to cleave excess structural collagen tissue.
  • Nitric Oxide (NO) Synthesis and Anti-Remodeling Models: Investigators utilize B7-33 across animal models of chronic allergic reactions and acute cardiovascular damage to study the prevention of pathological tissue scarring. The peptide’s interaction with RXFP1 triggers a distinct pERK1/2–neuronal nitric oxide synthase (nNOS)–NO–cGMP-dependent cascade. This multi-tiered pathway successfully blocks downstream myofibroblast differentiation and halts excessive extracellular matrix deposition. Crucially for oncology models, literature notes that unlike native relaxin, B7-33 demonstrates no trend toward promoting tumor cell growth.

• • Verified Purity: ≥ 99% purity guaranteed through mass spectrometry and HPLC profiling.
  • USA Vetted: Independent laboratory confirmation ensures absolute consistency, proper amino acid sequence replication, and complete freedom from structural cross-contaminants.
  • Research Use Only: This compound is synthesized exclusively for in vitro laboratory experimentation and preclinical evaluation. Make sure to double-check the physical label to confirm this information.

What is B7-33 Peptide?

B7-33 Peptide is a 27-amino acid peptide derived from the B-chain of human relaxin-2. Unlike native relaxin, which is a complex two-chain peptide with three disulfide bonds, B7-33 is a linear, single-chain peptide that is easier and more cost-effective to synthesize. The sequence of B7-33 is Val-Ile-Lys-Leu-Ser-Gly-Arg-Glu-Leu-Val-Arg-Ala-Gln-Ile-Ala-Ile-Ser-Gly-Met-Ser-Thr-Trp-Ser-Lys-Arg-Ser-Leu-NH₂ . This B7-33 Peptide has a molecular weight of approximately 2987.5 g/mol and a molecular formula of C₁₃₁H₂₂₈N₄₀O₃₇S. When you Buy B7-33 Peptide, you are acquiring a compound that represents a significant advancement in the field of relaxin research.

How Does B7-33 Work?

B7-33 functions as a selective agonist of the Relaxin Family Peptide Receptor 1 (RXFP1). The mechanism of B7-33 involves binding to RXFP1 and preferentially activating the pERK pathway over the cAMP pathway in cells that express RXFP1. This is significant because excessive cAMP activation is associated with off-target effects and tumorigenesis. By selectively activating pERK1/2 signaling through RXFP1-AT2 receptor heterodimers, B7-33 promotes the production of collagen-degrading matrix metalloproteinase-2 (MMP-2). This selective signaling mechanism allows B7-33 to retain the anti-fibrotic effects of native relaxin without its tumor-promoting actions.

B7 33 Peptide Benefits

The b7 33 peptide benefits are well-documented in scientific literature, making it a valuable tool for researchers.

Anti-Fibrotic Effects

One of the most significant b7 33 peptide benefits is its potent anti-fibrotic activity. In a study on hypertrophic scar fibroblasts, treatment with B7-33 demonstrated greater downregulation of Collagen Type I α-1 Chain (COL1A1) gene expression than reference anti-fibrotic agents. Normal and hypertrophic scar fibroblasts maintained >70% viability after 72-hour exposure to B7-33 at concentrations of 0.03–0.3 μg/mL. In an experimental model of cardiomyopathy, B7-33 equivalently reduced left ventricular fibrosis compared to relaxin and more rapidly reduced fibrosis than the ACE inhibitor perindopril. These b7 33 peptide benefits make it a promising candidate for research into fibrosis, scarring, and tissue repair.

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B7-33 has demonstrated cardioprotective b7 33 peptide benefits in multiple studies. In a mouse model of myocardial ischemia-reperfusion injury, treatment with B7-33 reduced infarct size and preserved cardiac function. In a separate study, B7-33 normalized ISO-induced left ventricular inflammation, cardiomyocyte hypertrophy, and vascular rarefaction, while restoring blood vessel density and aortic contractility. These b7 33 peptide benefits suggest potential applications in cardiovascular research.

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B7-33 has shown efficacy in rodent models of preeclampsia, a hypertensive pregnancy disorder. In the RUPP model, treatment with B7-33 lowered mean arterial pressure, TNF-alpha, and sFlt-1 back to normal pregnancy levels. B7-33 also normalized blood pressure and proteinuria in the DOCA rat model of preeclampsia. Researchers conclude that B7-33 is an “ideal candidate for development as a novel therapeutic in preeclampsia”.

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Determining appropriate b7 33 peptide dosage is crucial for reproducible research. The b7 33 peptide dosage varies based on the research model and application.

In Vitro Dosage

For cell culture studies, b7 33 peptide dosage of 0.03–0.3 μg/mL has been shown to maintain >70% cell viability. A b7 33 peptide dosage of 298.7 ng/mL (approximately 100 nM) significantly modulated profibrotic gene expression. In human cardiac fibroblasts, b7 33 peptide dosage of 30 nM (approximately 180 ng/mL) significantly promoted MMP-2 levels.

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For in vivo studies, b7 33 peptide dosage of 0.25 mg/kg/day has been used in mouse models of cardiomyopathy. For myocardial ischemia-reperfusion injury, b7 33 peptide dosage of 10 μg/kg was administered via intraperitoneal injection at the onset of reperfusion. In preeclampsia models, b7 33 peptide dosage of 35 μg was administered intraperitoneally biweekly.

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A2: B7-33 is a 27-amino acid single-chain peptide derived from the B-chain of human relaxin-2. This B7-33 peptide is a selective agonist of the RXFP1 receptor and has potent anti-fibrotic properties.

Q3: What are the B7 33 peptide benefits in research?
A3: The b7 33 peptide benefits include anti-fibrotic effects (downregulating collagen I and modulating scar fibroblast behavior ), cardioprotective effects against ischemia-reperfusion injury, and efficacy in preeclampsia models.

Q4: What is the B7 33 peptide dosage for research?
A4: B7 33 peptide dosage in vitro studies uses 0.03–0.3 μg/mL for viability and 30 nM (≈100 ng/mL) for MMP-2 stimulation . In vivo, B7 33 peptide dosage of 0.25 mg/kg/day has been used.

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Q8: How does B7-33 work?
A8: B7-33 binds to RXFP1 and preferentially activates the pERK pathway over the cAMP pathway. This selective signaling allows it to retain the anti-fibrotic effects of relaxin without tumor-promoting effects.

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