B7-33 10mg
(Relaxin Analogue)

Premium Grade | UK Supply | Research Peptide | COA Certified | >99% Purity | Worldwide Delivery

(Heptacosapeptide, 27 amino acids)

Brief Summary

B7-33 is a synthetic single-chain relaxin analogue studied in laboratory settings for its interaction with relaxin family peptide receptor 1, commonly abbreviated as RXFP1. Derived from the B-chain of relaxin-2, the peptide is investigated as a simplified molecular model for examining receptor-selective signalling, extracellular matrix regulation and fibrotic pathway activity. Research has focused particularly on its ability to favour ERK-associated signalling over the stronger cyclic AMP response produced by native relaxin-2 in some experimental systems. This functionally selective behaviour makes B7-33 useful for controlled studies examining biased receptor activation, fibroblast responses, collagen-associated markers and peptide-receptor communication. Within scientific research catalogues, B7-33 is valued for in vitro and preclinical investigation involving molecular signalling, extracellular matrix remodelling, receptor pharmacology and comparative relaxin analogue analysis. Its defined 27-amino-acid sequence supports structured laboratory study, analytical characterisation and reproducible peptide research within professional scientific environments.

Product Overview

B7-33 is a laboratory-grade synthetic peptide developed as a single-chain derivative of the B-chain of relaxin-2. Native relaxin-2 contains two peptide chains joined by disulphide bonds, whereas B7-33 uses a shorter single-chain design that retains key residues associated with RXFP1 receptor interaction. This simplified structure allows researchers to investigate relaxin-related signalling without using the complete two-chain hormone structure. B7-33 has been examined in cellular and preclinical models involving fibroblast activity, collagen accumulation, tissue remodelling and receptor-mediated intracellular communication. Its sequence, VIKLSGRELVRAQIAISGMSTWSKRSL, contains 27 amino acids and was designed through modification of the natural relaxin B-chain. The peptide is particularly relevant to comparative studies examining how structural changes influence receptor affinity, signalling bias and downstream molecular responses. Its defined composition and reproducible molecular characteristics support controlled investigation into peptide engineering, RXFP1 pharmacology and extracellular matrix-associated signalling pathways.

Scientific Background

From a molecular science perspective, B7-33 is studied as a functionally selective agonist of RXFP1, a G-protein-coupled receptor associated with relaxin-family peptide signalling. Experimental research indicates that B7-33 can preferentially activate phosphorylated extracellular signal-regulated kinase pathways while producing a different cyclic AMP response from native relaxin-2 in certain cell systems. This signalling profile is of interest because it allows researchers to separate individual downstream pathways and examine how receptor bias may influence cellular responses. Laboratory studies have investigated B7-33 in fibroblast models, collagen-production assays and preclinical models of cardiac, pulmonary and other forms of tissue fibrosis. Research has also examined its influence on matrix metalloproteinase-associated activity, inflammatory signalling, cellular stress responses and extracellular matrix turnover. B7-33 therefore provides a useful molecular tool for investigating how a shortened relaxin-derived sequence can preserve selected biological signalling properties while displaying different receptor pharmacology from the complete native hormone.

Research Applications

B7-33 is applied in laboratory research across peptide science, receptor biology, molecular pharmacology and extracellular matrix investigation. Researchers use the peptide to examine RXFP1 activation, biased receptor signalling, ERK-associated pathways, cyclic AMP responses and downstream cellular communication under controlled experimental conditions. Additional research applications include fibroblast-response studies, collagen-expression analysis, extracellular matrix turnover, tissue-remodelling markers and comparative evaluation against relaxin-2 or other relaxin analogues. B7-33 has also been investigated in preclinical models involving cardiac and pulmonary fibrosis, inflammatory signalling and organ-remodelling processes. Its single-chain structure supports research into peptide simplification, sequence optimisation, receptor-selective design and structure-activity relationships. These applications contribute to a broader understanding of relaxin-family receptor biology and demonstrate how modified peptide sequences may produce distinct signalling profiles. B7-33 is supplied as a research compound for analytical, in vitro and controlled preclinical investigation only.

Technical Specifications

Contents: 10mg B7-33
Form: Lyophilised powder
Purity: >99% (HPLC Verified)
Molecular Formula: C₁₃₁H₂₂₉N₄₁O₃₆S
Molecular Weight: 2986.58 g/mol
Sequence: 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
Sequence: VIKLSGRELVRAQIAISGMSTWSKRSL
Peptide Length: 27 amino acids
pH Range: Refer to batch-specific documentation and experimental protocol
Storage: Store between 2°C and 8°C in accordance with the product documentation

Note:  Reconstitute with 50% Bacteriostatic water 50% Acid Acid for best results.

Related Research Compounds

GHK-Cu 50mg
BPC-157 5mg
TB-500 10mg

Disclaimer

For research purposes only. Not for human consumption.