Recombinant Proteins
Product List
RLN2 Human
Relaxin-2 Human Recombinant
RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
RLN2 Human, Sf9
Relaxin-2 Human Recombinant, Sf9
RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).
RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
RLN3 Human
Relaxin-3 Human Recombinant
The Relaxin-3 is purified by proprietary chromatographic techniques.
Introduction
Relaxin is a peptide hormone belonging to the insulin superfamily. It was first described in 1926 by Frederick Hisaw. The relaxin family consists of seven peptides: relaxin-1 (RLN1), relaxin-2 (RLN2), relaxin-3 (RLN3), and the insulin-like peptides INSL3, INSL4, INSL5, and INSL6 . Relaxin is structurally related to insulin and is produced from its prohormone, prorelaxin, by post-translational proteolytic cleavage .
Relaxin exhibits several key biological properties:
- Expression Patterns: In females, relaxin is produced by the corpus luteum of the ovary, the breast, and during pregnancy, by the placenta, chorion, and decidua. In males, it is produced in the prostate and is present in semen .
- Tissue Distribution: Relaxin is found in various tissues, including the reproductive organs, heart, and kidneys .
- Key Biological Properties: Relaxin has anti-inflammatory effects, promotes extracellular matrix remodeling, and has angiogenic and anti-ischemic effects .
Relaxin plays several primary biological functions:
- Reproductive System: In females, relaxin helps prepare the endometrium for implantation, mediates hemodynamic changes during pregnancy, and relaxes the uterine muscle and pelvic ligaments to facilitate childbirth . In males, it enhances sperm motility .
- Immune Responses and Pathogen Recognition: Relaxin has been reported to reduce fibrosis in the kidney, heart, lung, and liver, promote wound healing, and protect the heart from ischemia-induced injury .
Relaxin interacts with other molecules and cells through several mechanisms:
- Binding Partners: Relaxin binds to the relaxin family peptide receptors (RXFP1 and RXFP2), which are G protein-coupled receptors .
- Downstream Signaling Cascades: The binding of relaxin to its receptors activates several signaling pathways, including the nitric oxide pathway, NFκB leading to vascular endothelial growth factor (VEGF) activation, PI3K/Akt-associated signaling pathways, and matrix metalloproteinases transcription .
The expression and activity of relaxin are controlled by various regulatory mechanisms:
Relaxin has several applications in biomedical research, diagnostics, and therapeutics:
- Biomedical Research: Relaxin is studied for its potential therapeutic effects in treating heart failure, fibrosis, and other conditions .
- Diagnostic Tools: Relaxin levels can be measured to monitor pregnancy and reproductive health .
- Therapeutic Strategies: Relaxin or its recombinant form, serelaxin, is being investigated as a potential treatment for cardiovascular diseases, especially heart failure .
Relaxin plays a significant role throughout the life cycle:
- Development: During pregnancy, relaxin helps prepare the body for childbirth by relaxing the pelvic ligaments and softening the cervix .
- Aging and Disease: Relaxin’s anti-fibrotic, anti-inflammatory, and vasodilatory properties make it a potential therapeutic agent for age-related diseases and conditions such as heart failure and fibrosis .
