FNDC5 Human

Fibronectin Type III Domain Containing 5 Human Recombinant
Cat. No.
BT9059
Source
Escherichia Coli.
Synonyms
Fibronectin type III domain-containing protein 5, Fibronectin type III repeat-containing protein, Fibronectin Type III Repeat-Containing Protein 2, Irisin, FNDC5, FRCP2.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

FNDC5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 32-143) containing 122 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 13.8kDa (calculated).

Product Specs

Introduction
Fibronectin Type III Domain Containing 5 (Irisin) is a recently discovered hormone produced by muscles and released into the bloodstream. It primarily targets white fat cells, promoting their transformation into a type of fat tissue known as 'beige' or 'brite' fat, a process often referred to as 'WAT browning'. Recombinant Irisin (r-Irisin) has demonstrated the ability to decrease body weight and stimulate the production of brown-like adipocytes in living organisms. This includes the activation of thermogenic energy expenditure, which involves the utilization of a protein called uncoupling protein 1 (UCP-1). The mature Irisin protein consists of 110 amino acid residues and has two potential sites for glycosylation. Notably, Irisin levels are elevated in the heart, while its presence in the colon, pancreas, and spleen is either extremely low or undetectable.
Description
Recombinant Human FNDC5, manufactured in E. coli, is a single-chain polypeptide consisting of 122 amino acids (amino acids 32-143). It is non-glycosylated and includes a 10 amino acid His-tag at the N-terminus. The calculated molecular weight is 13.8 kDa.
Physical Appearance
White, lyophilized powder after filtration.
Formulation
FNDC5 undergoes a 0.4 μm filtration process and is subsequently lyophilized from a 0.5 mg/ml solution in phosphate-buffered saline.
Solubility
To prepare a working stock solution, add deionized water to the lyophilized pellet, aiming for a concentration of approximately 0.5 mg/ml. Allow sufficient time for the pellet to dissolve entirely. Important note: FNDC5 is not sterile. Prior to using it in cell culture, it is essential to filter the product through a sterile filter of appropriate pore size.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to prevent repeated freeze-thaw cycles. The reconstituted protein can be stored at 4°C for a limited period; no significant changes are observed after two weeks at 4°C.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Synonyms
Fibronectin type III domain-containing protein 5, Fibronectin type III repeat-containing protein, Fibronectin Type III Repeat-Containing Protein 2, Irisin, FNDC5, FRCP2.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHASDSPSAPVNVT VRHLKANSAV VSWDVLEDEV VIGFAISQQK KDVRMLRFIQ EVNTTTRSCA LWDLEEDTEY IVHVQAISIQ GQSPASEPVL FKTPREAEKM ASKNKDEVTM KE.

Product Science Overview

Discovery and Structure

FNDC5 was first characterized in 2002 as a transmembrane protein expressed in various tissues, including skeletal muscle, heart, and brain . The protein contains a fibronectin type III domain, which is a common structural motif involved in cell adhesion and receptor binding. The human FNDC5 gene is located on chromosome 1 and is known to produce multiple transcript variants through alternative splicing .

Irisin: The Cleaved Form of FNDC5

The most intriguing aspect of FNDC5 is its role as the precursor to irisin. During physical exercise, the ectodomain of FNDC5 is cleaved to release irisin, a 112-amino acid hormone . Irisin was named after the Greek messenger goddess Iris, reflecting its role in conveying signals within the body . This hormone has been shown to induce the browning of white adipose tissue, a process that increases energy expenditure and has potential implications for combating obesity and metabolic disorders .

Biological Functions and Research

Research on FNDC5 and irisin has expanded rapidly since the discovery of irisin in 2012. Studies have explored the hormone’s effects on various physiological processes:

  • Metabolism: Irisin has been linked to improved glucose homeostasis and lipid metabolism. It is believed to play a role in the beneficial effects of exercise on metabolic health .
  • Bone Remodeling: Recent studies suggest that irisin may influence bone density and strength, potentially offering new avenues for treating osteoporosis .
  • Cognitive Function: There is emerging evidence that irisin may have neuroprotective effects and could be involved in brain health, including the regulation of brain-derived neurotrophic factor (BDNF) and neurogenesis .
Challenges and Controversies

Despite the promising findings, the study of FNDC5 and irisin is not without challenges. Some researchers have questioned the accuracy of assays used to measure irisin levels in plasma, leading to discrepancies in reported data . Additionally, while animal studies have shown significant effects of irisin on adipose tissue and metabolism, similar results in humans have been less consistent .

Human Recombinant FNDC5

Human recombinant FNDC5 is produced through recombinant DNA technology, allowing for the study of this protein in various experimental settings. This recombinant form is crucial for investigating the detailed mechanisms of FNDC5 and irisin, as well as their potential therapeutic applications.

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