Recombinant Proteins

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RLN2 Human

Relaxin-2 Human Recombinant

Recombinant human RLN2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 184 amino acids (25-185 a.a). With a molecular mass of 20.7 kDa, this protein is fused to a 23 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13377
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution.

RLN2 Human, Sf9

Relaxin-2 Human Recombinant, Sf9

Recombinant Human RLN2, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 170 amino acids (25-185a.a.). Its molecular weight is 19.3kDa, but it may appear as approximately 18-28kDa on SDS-PAGE. This RLN2 variant includes a 6-amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13467
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

RLN3 Human

Relaxin-3 Human Recombinant

Recombinant Human Relaxin-3, produced in E. coli, is a non-glycosylated polypeptide characterized by a disulfide-linked heterodimeric structure. It comprises a 24-amino acid A chain with a molecular mass of 2.5 kDa and a 27-amino acid B chain with a molecular mass of 3 kDa. The purification of Relaxin-3 is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13506
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

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 .

Biological Properties

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 .
Biological Functions

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 .
Modes of Action

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 .
Regulatory Mechanisms

The expression and activity of relaxin are controlled by various regulatory mechanisms:

  • Transcriptional Regulation: Relaxin gene expression is regulated by hormonal signals, including steroid hormones .
  • Post-Translational Modifications: Relaxin is produced from its prohormone, prorelaxin, by post-translational proteolytic cleavage .
Applications

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 .
Role in the Life Cycle

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 .
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