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Fibroblast Growth Factor 21 Mouse E. coli Tag free

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:FGF-21, UNQ3115/PRO10196
  • Species:Mouse
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Cat. No. Size Price


RD272108025-B 0.025 mg
RD272108100-B 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 183 AA. MW: 20.1 kDa (calculated). UniProtKB acc.no. Q9JJN1. 182AA of the mouse FGF21 and one extra AA, N-terminal methionin (highlighted).

Amino Acid Sequence

MAYPIPDSSPLLQFGGQVRQRYLYTDDDQDTEAHLEIREDGTVVGAAHRSPESLLELKALKPGVIQILGVKASRFLCQQPDGALYGSPHFDPEACSFRELLLEDGYNVYQSEAHGLPLRLPQKDSPNQDATSWGPVRFLPMPGLLHEPQDQAGFLPPEPPDVGSSDPLSMVEPLQGRSPSYAS

Source

E. coli

Purity

>95%

SDS-PAGE Gel

12% SDS-PAGE separation of Mouse FGF21
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 5μg/lane
3. non-reduced and non-heated sample, 5μg/lane

Endotoxin

< 1.0 EU/ug

Formulation

Filtered (0,4 μm) and lyophilized in 0.5 mg/mL in 20mM TRIS, 20mM NaCl, pH 7.5

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture. Add DTT (0.2 mM ) and NaCl (0.1–0.15 M) before freezing to prevent potential aggregation.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Diabetology - Other Relevant Products, Energy metabolism and body weight regulation, Animal studies

Summary

The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.

FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, –2, –3, and –4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in β cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal β cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.

FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.

FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

References to Summary

References to Fibroblast Growth Factor 21

  • Christodoulides C, Dyson P, Sprecher D, Tsintzas K, Karpe F. Circulating fibroblast growth factor 21 is induced by peroxisome proliferator-activated receptor agonists but not ketosis in man. J Clin Endocrinol Metab. 2009 Sep;94 (9):3594-601
  • Cuevas-Ramos D, Almeda-Valdes P, Gomez-Perez FJ, Meza-Arana CE, Cruz-Bautista I, Arellano-Campos O, Navarrete-Lopez M, Aguilar-Salinas CA. Daily physical activity, fasting glucose, uric acid, and body mass index are independent factors associated with serum fibroblast growth factor 21 levels. Eur J Endocrinol. 2010 Sep;163 (3):469-77
  • Dostalova I, Haluzikova D, Haluzik M. Fibroblast growth factor 21: a novel metabolic regulator with potential therapeutic properties in obesity/type 2 diabetes mellitus. Physiol Res. 2009;58 (1):1-7
  • Dostalova I, Kavalkova P, Haluzikova D, Lacinova Z, Mraz M, Papezova H, Haluzik M. Plasma concentrations of fibroblast growth factors 19 and 21 in patients with anorexia nervosa. J Clin Endocrinol Metab. 2008 Sep;93 (9):3627-32
  • Fazeli PK, Misra M, Goldstein M, Miller KK, Klibanski A. Fibroblast growth factor-21 may mediate growth hormone resistance in anorexia nervosa. J Clin Endocrinol Metab. 2010 Jan;95 (1):369-74
  • Fisher FM, Chui PC, Antonellis PJ, Bina HA, Kharitonenkov A, Flier JS, Maratos-Flier E. Obesity is a fibroblast growth factor 21 (FGF21)-resistant state. Diabetes. 2010 Nov;59 (11):2781-9
  • Fu L, John LM, Adams SH, Yu XX, Tomlinson E, Renz M, Williams PM, Soriano R, Corpuz R, Moffat B, Vandlen R, Simmons L, Foster J, Stephan JP, Tsai SP, Stewart TA. Fibroblast growth factor 19 increases metabolic rate and reverses dietary and leptin-deficient diabetes. Endocrinology. 2004 Jun;145(6):2594-603. Epub 2004 Feb 19.
  • Han SH, Choi SH, Cho BJ, Lee Y, Lim S, Park YJ, Moon MK, Lee HK, Kang SW, Han DS, Kim YB, Jang HC, Park KS. Serum fibroblast growth factor-21 concentration is associated with residual renal function and insulin resistance in end-stage renal disease patients receiving long-term peritoneal dialysis. Metabolism. 2010 Nov;59 (11):1656-62
  • Harmer NJ, Pellegrini L, Chirgadze D, Fernandez-Recio J, Blundell TL. The crystal structure of fibroblast growth factor (FGF) 19 reveals novel features of the FGF family and offers a structural basis for its unusual receptor affinity. Biochemistry. 2004 Jan 27;43(3):629-40.
  • Hero M, Dunkel L, Vaaralahti K, Raivio T. Serum FGF21 in Boys with Idiopathic Short Stature: Relationship to Lipid Profile, Onset of Puberty and Growth*. Clin Endocrinol (Oxf). 2011 Feb 1;
  • Hojman P, Pedersen M, Nielsen AR, Krogh-Madsen R, Yfanti C, Akerstrom T, Nielsen S, Pedersen BK. Fibroblast growth factor-21 is induced in human skeletal muscles by hyperinsulinemia. Diabetes. 2009 Dec;58 (12):2797-801
  • Holt JA, Luo G, Billin AN, Bisi J, McNeill YY, Kozarsky KF, Donahee M, Wang da Y, Mansfield TA, Kliewer SA, Goodwin B, Jones SA. Definition of a novel growth factor-dependent signal cascade for the suppression of bile acid biosynthesis. Genes Dev. 2003 Jul 1;17(13):1581-91. Epub 2003 Jun 18.
  • Jian WX, Peng WH, Jin J, Chen XR, Fang WJ, Wang WX, Qin L, Dong Y, Su Q. Association between serum fibroblast growth factor 21 and diabetic nephropathy. Metabolism. 2012 Jun;61 (6):853-9
  • Kharitonenkov A, Shiyanova TL, Koester A, Ford AM, Micanovic R, Galbreath EJ, Sandusky GE, Hammond LJ, Moyers JS, Owens RA, Gromada J, Brozinick JT, Hawkins ED, Wroblewski VJ, Li DS, Mehrbod F, Jaskunas SR, Shanafelt AB. FGF-21 as a novel metabolic regulator. J Clin Invest. 2005 Jun;115(6):1627-35. Epub 2005 May 2.
  • Kotulak T, Drapalova J, Kopecky P, Lacinova Z, Kramar P, Riha H, Netuka I, Maly J, Housa D, Blaha J, Svacina S, Haluzik M. Increased circulating and epicardial adipose tissue mRNA expression of fibroblast growth factor-21 after cardiac surgery: possible role in postoperative inflammatory response and insulin resistance. Physiol Res. 2011;60 (5):757-67
  • Li H, Bao Y, Xu A, Pan X, Lu J, Wu H, Lu H, Xiang K, Jia W. Serum fibrobl
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