Description
B7-33 is a synthetic single-chain peptide derived from the human H2-relaxin protein and is studied as a functionally selective agonist of the RXFP1 receptor. B7-33 peptide research focuses on how this relaxin-2–derived analogue influences extracellular matrix (ECM) remodeling pathways under controlled laboratory conditions, including signaling associated with ERK1/2 phosphorylation and regulation of matrix metalloproteinases. Compared with full-length relaxin-2, B7-33 is investigated for receptor-biased signaling profiles that can be used to probe specific downstream mechanisms.
In vitro assays and animal models commonly examine changes in collagen deposition markers, ECM turnover enzymes (e.g., MMP-2), and fibroblast activation signatures. Major research areas include fibrosis-relevant pathway biology, vascular endothelium signaling and tone regulation in preclinical systems, and biomaterials research where local tissue responses to implanted surfaces are measured. These systems matter in laboratory research because they provide measurable endpoints for studying tissue remodeling, cellular signaling, and ECM organization without implying clinical effectiveness or human use.
For research use only. Not for human consumption.
References:
Hossain MA et al., Chem Sci, 2016 7(6):3805–3813
Chan LJ et al., Br J Pharmacol, 2012 165(8):2612–2626
Bathgate RAD et al., Front Endocrinol (Lausanne), 2013 4:13




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