RLN3 Human

Relaxin-3 Human Recombinant
Cat. No.
BT13506
Source
Escherichia Coli.
Synonyms

Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Relaxin-3 Human Recombinant produced in E.Coli is a disulfide-linked heterodimeric, non-glycosylated, polypeptide chain containing 24 amino acids for A chain and 27 amino acids for B chain and having a molecular mass of 2.5kDa for A chain and 3kDa for B chain.
The Relaxin-3 is purified by proprietary chromatographic techniques.

Product Specs

Introduction

Relaxin-3 (RLN3), a member of the relaxin hormone family, exhibits both endocrine and autocrine/paracrine functions. Primarily recognized for its role in the reproductive system, relaxin, produced by the ovary, facilitates cervical ripening, pubic symphysis elongation, and uterine contraction inhibition in mammals. Deviating from Relaxins 1 and 2 in humans, RLN3 appears to have limited reproductive involvement but plays a crucial role in stress response within the brain stem. It specifically binds to the G-protein-coupled receptor GPCR135 (RXFP3) as its only known ligand. Although RLN3 exhibits binding affinity to the LGR7 (RXFP1) receptor, it is weaker compared to Relaxin-2. While RLN3 binding to LGR7 triggers intracellular cAMP increase, its interaction with GPCR135 suppresses cAMP accumulation, suggesting coupling to Gi, Go, or Gz by the receptor.

Description
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.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2 µm filtered solution in Acetonitrile and TFA.
Solubility
To reconstitute the lyophilized RLN3, it is recommended to dissolve it in sterile 18M-cm H₂O at a concentration not less than 100 µg/ml. Further dilutions can be made in other aqueous solutions.
Stability
Lyophilized RLN3 remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. Once reconstituted, Relaxin-3 should be stored at 4°C for 2-7 days. For extended storage, it is advisable to store it below -18°C. To ensure long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Biological Activity
The ED₅₀, determined by cAMP accumulation in human THP-1 cells, is less than 17.5 ng/ml.
Synonyms

Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

Source
Escherichia Coli.
Amino Acid Sequence
A chain: DVLAGLSSSC CKWGCSKSEI SSLC.
B chain: RAAPYGVRLCG REFIRAVIFT CGGSRW.

Product Science Overview

Introduction

Relaxin-3, also known as H3 relaxin or INSL7, is a member of the relaxin family of peptides, which are part of the insulin superfamily . Unlike human relaxins 1 and 2, which are primarily involved in reproductive processes, Relaxin-3 functions as a neuropeptide and plays a significant role in the central nervous system .

Discovery and Structure

Relaxin-3 was discovered through homology searching of the human genome approximately 20 years ago . It is a disulfide-linked heterodimer composed of two chains: the A chain (Asp119-Cys142) and the B chain (Ala27-Arg53) . The predicted molecular masses of the A and B chains are 2.46 kDa and 3.04 kDa, respectively .

Biological Function

Relaxin-3 is primarily expressed in the brainstem and has been shown to modulate neuronal activity in multiple brain circuits . It interacts with its cognate G-protein-coupled receptor, relaxin-family peptide receptor 3 (RXFP3), to influence various neuroendocrine functions . This peptide is involved in stress response, feeding behavior, and arousal .

Recombinant Production

Recombinant human Relaxin-3 is produced using Escherichia coli (E. coli) expression systems . The protein is typically purified to a high degree of purity (>95%) and is free from endotoxins (<0.10 EU per 1 μg of protein) . The recombinant protein is often lyophilized and can be reconstituted in sterile phosphate-buffered saline (PBS) for use in various research applications .

Applications

Recombinant Relaxin-3 is used in research to study its effects on cAMP accumulation in THP-1 human acute monocytic leukemia cells . It is also utilized to investigate its role in neuroendocrine functions and its potential therapeutic applications in treating stress-related disorders .

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