Recombinant Mouse Fibronectin Type Iii Domain-Containing Protein 5 (FNDC5) Protein (His)

Name: Recombinant Mouse Fibronectin Type Iii Domain-Containing Protein 5 (FNDC5) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07256P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Fibronectin Type Iii Domain-Containing Protein 5 (FNDC5) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8K4Z2
Target Symbol	FNDC5
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DSPSAPVNVTVRHLKANSAVVSWDVLEDEVVIGFAISQQKKDVRMLRFIQEVNTTTRSCALWDLEEDTEYIVHVQAISIQGQSPASEPVLFKTPREAEKMASKNKDEVTMKE
Expression Range	29-140aa
Protein Length	Partial
Mol. Weight	18.6 kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	mediates beneficial effects of muscular exercise. Induces browning of white adipose tissue by stimulating UCP1 expression, at least in part, via the nuclear receptor PPARA.
Subcellular Location	Cell membrane; Single-pass type I membrane protein. Peroxisome membrane; Single-pass type I membrane protein. Secreted. Note=Imported in peroxisomes through the PEX5 receptor pathway.; [Irisin]: Secreted. Note=Detected in the blood of individuals subjected to endurance exercise.
Database References	KEGG: mmu:384061 STRING: 10090.ENSMUSP00000099660 UniGene: Mm.44075
Tissue Specificity	In adult, it is highly expressed in skeletal muscle, heart and brain.

Gene Functions References

A high-fat diet increased Fndc5 transcript levels in the skeletal muscle, but exercise had a minimal effect on the transcript level of Fndc5, whereas endurance training increased the protein content of FNDC5 in the skeletal muscle. PMID: 29365291
These findings may lead to development of an Irisin-based therapy for elderly immobile osteoporotic and physically disable patients, and might represent a countermeasure for astronauts subjected to microgravity-induced bone and muscle losses. PMID: 28588307
Glucocorticoid receptor positively regulates transcription of FNDC5 in the liver. PMID: 28240298
Findings demonstrated that one bout of both uphill and downhill exercise trainings as well as 8 weeks of training could increase the expression of PGC-1alpha and FNDC5 genes in the muscle tissues and the UCP1 gene in the subcutaneous adipose tissue. PMID: 30218749
Our study has indicated that irisin (FNDC5) possesses important anti-oxidant and anti-inflammatory properties and may protect cells from the damage induced by ROS under inflammatory conditions by activating of the Nrf2/HO-1 pathway. PMID: 29769428
FNDC5 attenuated Oxidized low density lipoprotein-induced AMPK deactivation, hepatic stellate cells activation, connective tissue growth factor and transforming growth factor-beta upregulation and extracellular matrix deposition in mouse hepatic stellate cells. PMID: 30007970
the coordinated expression of FNDC5 and PGC-1alpha may contribute to the increased levels of plasma irisin after exercise. PMID: 29415899
Irisin(Fndc5) increases myogenic differentiation and myoblast fusion via activation of IL6 signaling. PMID: 29062100
FNDC5 is overexpressed in skeletal muscle and adipose tissue of insulin resistant high fat-fed mice. PMID: 28676551
This study for the first time showed that adipocytes are directly affected by irisin (Fndc5) and provides an evidence on anti-inflammatory action of irisin on fat cells. PMID: 28614774
Mstn regulates Fndc5/Irisin expression and secretion through a novel miR-34a-dependent post-transcriptional mechanism; loss of Mstn in mice leads to the increased Fndc5/Irisin expression, which contributes to the browning of white adipocytes PMID: 27297797
The secretion of FNDC5 from myotubes and beta-cells in response to exogenous fatty acids, the effects of recombinant FNDC5 on insulin biosynthesis and glucose-stimulated insulin secretion, and beta-cell apoptosis are reported. PMID: 28724742
Irisin is upregulated in a murine model of fibrosis, but not in experimental NAFLD without significant fibrosis. PMID: 28472477
Irisin improved endothelial function by modulating HO-1/ adiponectin axis in perivascular adipose tissue (PVAT) in HFD-induced obese mice. These findings suggest that regulating PVAT function may be a potential mechanism by which irisin improves endothelial function in obesity. PMID: 28595178
The results indicate that FNDC5 deficiency impairs autophagy and FAO and enhances lipogenesis via the AMPK/mTOR pathway. FNDC5 deficiency aggravates whereas FNDC5 overexpression prevents the HFD-induced hyperlipemia, hepatic lipid accumulation, and impaired FAO and autophagy in the liver. PMID: 27504012
This research is the first to show that irisin modulates macrophage activity by reducing reactive oxygen species (ROS) overproduction, which could suggest its potential anti-inflammatory properties. PMID: 28315350
No FNDC5 expression was detected in normal or cancerous stomach tissues. FNDC5 expression in white and brown adipose tissues in the cancer group increased compared with the control and non-cancer groups. PMID: 27256459
Report showed that irisin suppressed cholesterol synthesis in hepatocytes through the activation of 5' AMP-activated protein kinase (AMPK) and subsequent inhibition of transcription and nuclear translocation of SREBP2. PMID: 27211556
PGC1alpha regulates FNDC5 and its processed and secreted peptide Irisin, which has been proposed to play a critical role in energy expenditure and to promote neural differentiation of mouse embryonic stem cells. Review. PMID: 26611102
Irisin directly targets osteoblast, promoting osteoblast proliferation and differentiation via activating P38/ERK MAP kinase signaling cascades in vitro. PMID: 26738434
irisin does not function through inflammatory NFKB activation like other myokines (such as TNFalpha). PMID: 26399516
Muscle FNDC5 mRNA expression and irisin release are not IL-15-dependent in mice. PMID: 25920499
irisin alleviates endothelial dysfunction in type 2 diabetes partially via reducing oxidative stresses through inhibiting signaling pathways suggesting that irisin may be a promising molecule for the treatment of vascular complications of diabetes. PMID: 26225842
HFD induced obese mice showed decreased irisin secretion from adipose tissues, which might contribute to muscle insulin resistance. PMID: 26261526
Our study also suggests the existence of irisin-specific receptor on the membrane of H9C2 cells. In conclusion, irisin in a certain concentration rage increased myocardial cell metabolism, inhibited cell proliferation and promoted cell differentiation PMID: 26305684
In summary, these results suggested that the endothelium-dependent relaxation of irisin is mediated by the nitric oxide (NO)-guanosine 3', 5'-cyclic phosphate (cGMP)-dependent pathway. PMID: 26582714
Fndc5 facilitates neural differentiation. This effect might be related to increased expression of BDNF following overexpression of Fndc5. PMID: 25572300
This study used irisin radiolabeled with (125)I and small-animal SPECT/CT imaging to investigate the metabolic elimination and distribution of irisin in vivo. PMID: 25757030
High intensity exercise results in increased expression of Fndc5 in skeletal muscle. PMID: 26166638
Increase PGC-1alpha expression during cardiac precursor cells formation stage via rosiglitazone treatment increase FNDC5 and mitochondrial markers transcript levels which enhanced cardiac differentiation efficiency. PMID: 25936576
The myokine irisin increases cortical bone mass and may be the molecular entity responsible for muscle-bone connectivity. PMID: 26374841
findings shed light on the poorly understood regulation of irisin/FNDC5 by demonstrating a novel association between irisin and SMAD3 signaling in skeletal muscle PMID: 25648888
Stage dependent expression of FNDC5 is affected by neural induction method used for neural differentiation. PMID: 24706335
Data suggest that fibronectin type III domain-containing 5 protein (Fndc5) may be involved in cardiomyocyte differentiation. PMID: 25168892
exists in muscle and serum of mice independent of exercise and is increased immediately after acute exercise PMID: 24644429
FNDC5 (25 kDa) and irisin (12 kDa) were present in murine skeletal muscle and that irisin was circulating in murine serum. PMID: 24498244
These findings link endurance exercise and the important metabolic mediators, PGC-1alpha and FNDC5, with BDNF expression in the brain. PMID: 24120943
This immunohistochemical results demonstrate the expression of irisin immunoreactivity in three types of cells: skeletal, cardiac muscle, and Purkinje cells of the cerebellum. PMID: 23470775
Fndc5 expression is required for the appropriate neural differentiation of mESCs. These data confirm the importance of Fndc5 in the generation and development of the nervous system. PMID: 23219938
Within the muscle, Mstn(-/-) leads to increased expression of AMPK and its phosphorylation, which subsequently activates PGC1alpha and Fndc5. PMID: 23362117

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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