Recombinant Mouse Fibronectin type III domain-containing protein 5(Fndc5),partial

Code CSB-YP815686MO
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Source Yeast
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Code CSB-EP815686MO
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Source E.coli
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Code CSB-EP815686MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP815686MO
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Source Baculovirus
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Code CSB-MP815686MO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Fndc5
Uniprot No. Q8K4Z2
Alternative Names Fndc5; Frcp2; PepFibronectin type III domain-containing protein 5; Fibronectin type III repeat-containing protein 2; Peroxisomal protein; PeP) [Cleaved into: Irisin]
Species Mus musculus (Mouse)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

(From Uniprot)
Gene References into Functions
  1. 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
  2. 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
  3. Glucocorticoid receptor positively regulates transcription of FNDC5 in the liver. PMID: 28240298
  4. 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
  5. 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
  6. 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
  7. the coordinated expression of FNDC5 and PGC-1alpha may contribute to the increased levels of plasma irisin after exercise. PMID: 29415899
  8. Irisin(Fndc5) increases myogenic differentiation and myoblast fusion via activation of IL6 signaling. PMID: 29062100
  9. FNDC5 is overexpressed in skeletal muscle and adipose tissue of insulin resistant high fat-fed mice. PMID: 28676551
  10. 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
  11. 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
  12. 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
  13. Irisin is upregulated in a murine model of fibrosis, but not in experimental NAFLD without significant fibrosis. PMID: 28472477
  14. 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
  15. 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
  16. 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
  17. 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
  18. 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
  19. 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
  20. Irisin directly targets osteoblast, promoting osteoblast proliferation and differentiation via activating P38/ERK MAP kinase signaling cascades in vitro. PMID: 26738434
  21. irisin does not function through inflammatory NFKB activation like other myokines (such as TNFalpha). PMID: 26399516
  22. Muscle FNDC5 mRNA expression and irisin release are not IL-15-dependent in mice. PMID: 25920499
  23. 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
  24. HFD induced obese mice showed decreased irisin secretion from adipose tissues, which might contribute to muscle insulin resistance. PMID: 26261526
  25. 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
  26. 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
  27. Fndc5 facilitates neural differentiation. This effect might be related to increased expression of BDNF following overexpression of Fndc5. PMID: 25572300
  28. 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
  29. High intensity exercise results in increased expression of Fndc5 in skeletal muscle. PMID: 26166638
  30. 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
  31. The myokine irisin increases cortical bone mass and may be the molecular entity responsible for muscle-bone connectivity. PMID: 26374841
  32. 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
  33. Stage dependent expression of FNDC5 is affected by neural induction method used for neural differentiation. PMID: 24706335
  34. Data suggest that fibronectin type III domain-containing 5 protein (Fndc5) may be involved in cardiomyocyte differentiation. PMID: 25168892
  35. exists in muscle and serum of mice independent of exercise and is increased immediately after acute exercise PMID: 24644429
  36. FNDC5 (25 kDa) and irisin (12 kDa) were present in murine skeletal muscle and that irisin was circulating in murine serum. PMID: 24498244
  37. These findings link endurance exercise and the important metabolic mediators, PGC-1alpha and FNDC5, with BDNF expression in the brain. PMID: 24120943
  38. 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
  39. 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
  40. 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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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, SUBCELLULAR LOCATION: Irisin: Secreted
Tissue Specificity In adult, it is highly expressed in skeletal muscle, heart and brain.
Database Links

KEGG: mmu:384061

STRING: 10090.ENSMUSP00000099660

UniGene: Mm.44075


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