Recombinant Mouse Fibroblast Growth Factor 15 (FGF15) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02587P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Fibroblast Growth Factor 15 (FGF15) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02587P
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Product Overview

Description Recombinant Mouse Fibroblast Growth Factor 15 (FGF15) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O35622
Target Symbol FGF15
Synonyms FGF-15; Fgf15; FGF15_MOUSE; FGF19; Fibroblast growth factor 15
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence RPLAQQSQSVSDEDPLFLYGWGKITRLQYLYSAGPYVSNCFLRIRSDGSVDCEEDQNERNLLEFRAVALKTIAIKDVSSVRYLCMSADGKIYGLIRYSEEDCTFREEMDCLGYNQYRSMKHHLHIIFIQAKPREQLQDQKPSNFIPVFHRSFFETGDQLRSKMFSLPLESDSMDPFRMVEDVDHLVKSPSFQK
Expression Range 26-218aa
Protein Length Full Length of Mature Protein
Mol. Weight 38.5kDa
Research Area Signal Transduction
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 Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression.
Subcellular Location Secreted.
Protein Families Heparin-binding growth factors family
Database References
Tissue Specificity Expressed in the developing brain.

Gene Functions References

  1. Taken together, these results suggested that FGF19, through the anti-oxidative defense system, attenuated the development of diabetic cardiomyopathy and restored cardiac function. PMID: 29778534
  2. ileal FGF15/19 to hepatic FGFR4 axis is activated and promotes liver regeneration (LR) after partial hepatectomy (PH) in mice, supporting the potential of ileal FGF15/19 to hepatic FGFR4 axis-targeted therapy to enhance LR after PH PMID: 29468415
  3. FRS2alpha-mediated pathways are essential for the FGF15/FGF19-FGFR4 signaling axis to control bile acid homeostasis. PMID: 25056539
  4. Together, our results show that SuFu promotes cerebellar radial precursor differentiation to neurons. SuFu function is mediated in part by GLI3R and down-regulation of Fgf15 expression. PMID: 28560839
  5. Results show a reciprocal regulation of adiponectin and FGF19 gene expression in mice. PMID: 27666676
  6. Tumorigenicity was assessed in three mouse models (db/db, diet-induced obese, and multi-drug resistance 2 [Mdr2]-deficient) following continuous exposure to FGF19 or FGF15 via adeno-associated viral-mediated gene delivery. PMID: 28189755
  7. These data identify hypothalamic Fgf15 as a regulator of glucagon secretion. PMID: 27829151
  8. Intestinal sensing of highly elevated levels of conjugated bile acids in blood promotes FGF15 signaling, reducing hepatic bile acid synthesis and modulating bile acid transporters. PMID: 28498614
  9. Fgf15 is the sonic hedgehog downstream signal to control thalamic regionalization, neurogenesis, and neuronal differentiation by regulating the expression and mutual segregation of neurogenic and proneural regulatory genes. PMID: 26311466
  10. human microbiota was able to reduce the levels of tauro-beta-muricholic acid and induce expression of FXR target genes Fgf15 and Shp in ileum after long-term colonization. We show that a human microbiota can change BA composition and induce FXR signaling in colonized mice, but the levels of secondary BAs produced are lower than in mice colonized with a mouse microbiota PMID: 27956475
  11. FGF15 improves lipid homeostasis and reduces bile acid synthesis, but promotes fibrosis during the development of non-alcoholic steatohepatitis PMID: 28673684
  12. This study demonstrates that the FGF19-SHP-LSD1 axis maintains homeostasis by suppressing unnecessary autophagic breakdown of cellular components, including lipids, under nutrient-rich postprandial conditions. PMID: 28446510
  13. The elevation in circulating levels of adiponectin and Fgf15 led to normalized hepatic and serum levels of bile acids, limited hepatic accumulation of toxic bile, attenuated inflammation, and amelioration of liver injury in the ethanol-fed mNT knockout mice. PMID: 27573244
  14. This study reveals SHP as a global transcriptional partner of SREBP-2 in regulation of sterol biosynthetic gene networks and provides a potential mechanism for cholesterol-lowering action of FGF19. PMID: 26634251
  15. we suggest that considerable mechanistic differences exist between humans and mice with regard to the nuclear receptors controlling the VitA-FGF15/19 axis. PMID: 26723851
  16. Ileal Fgf15 expression is a potent inhibitor of bile acid synthesis. PMID: 26040986
  17. Protective effects of farnesoid X receptor on hepatic lipid accumulation are mediated by hepatic FXR and are independent of intestinal FGF15 signaling. PMID: 25156247
  18. In mice with humanized livers human hepatocytes do not recognize FGF-15 produced by mouse intestine, resulting in up-regulation of bile acid synthesis enlargement of the bile acid pool, affecting the hepatostat. PMID: 26028580
  19. Intestinal PPARalpha-UDP- Glucuronyltransferases and downstream FXR-FGF15 signalling play vital roles in control of bile acid homeostasis and the pathological development of colitis. PMID: 25183423
  20. Sstudy shows an important contribution of ileal FGF15 to hepatocarcinogenesis in a clinically relevant mouse model where lack of Fgf15 resulted in reduced tumor burden and attenuated tumor progression. PMID: 25346390
  21. results suggest that FGF15 deficiency severely impairs liver regeneration in mice after PHx. The underlying mechanism is likely the result of disrupted bile acid homeostasis and impaired priming of hepatocyte proliferation. PMID: 24699334
  22. a direct role of intestinal FGF15/19 in the regulation of SI P450 expression and may have profound implications for the prediction of drug exposure in patients with compromised hepatic P450 function PMID: 24184963
  23. findings implicate the brain in the antidiabetic action of systemic FGF19 and establish the brain's capacity to rapidly, potently, and selectively increase insulin-independent glucose disposal PMID: 24084738
  24. Total ileal FGF15 expression was elevated almost 20-fold in Ostalpha(-/-) mice as a result of increased villus epithelial cell number and ileocyte FGF15 protein expression PMID: 22542490
  25. generated a variant of FGF19, FGF19-7, that has altered receptor specificity with a strong bias toward FGFR1c PMID: 22457778
  26. Differential specificity of endocrine FGF19 and FGF21 to FGFR1 and FGFR4 in complex with KLB. PMID: 22442730
  27. Mouse Fgf15 and human FGF19 play key roles in enterohepatic signaling, regulation of liver bile acid biosynthesis, gallbladder motility and metabolic homeostasis PMID: 22396169
  28. Pregnane X receptor activation induces FGF19-dependent tumor aggressiveness in humans and mice PMID: 21747170
  29. mice lacking FGF15 (FGF19) fail to maintain blood concentrations of glucose and normal postprandial liver glycogen; FGF19 activates a physiologically important, insulin-independent endocrine pathway that regulates hepatic protein and glycogen metabolism PMID: 21436455
  30. Fgf15 is a crucial signaling molecule regulating the postmitotic transition of dorsal neural progenitors and thus the initiation and proper progression of dorsal midbrain neurogenesis in the mouse. PMID: 21172336
  31. the physiological relevance of the contribution of the intestinal FXR-Fgf15 signalling pathway in control of hepatic bile acid synthesis PMID: 20531290
  32. the structure-function relationship of FGF19/FGF21 and the structural basis underpinning the distinct proliferative feature of FGF19 compared with FGF21 PMID: 20660733
  33. activation of FGFR4 is the mechanism whereby FGF19 can increase hepatocyte proliferation and induce hepatocellular carcinoma formation. PMID: 20018895
  34. Fgf15 is expressed in the optic vesicle, a subset of progenitor cells of neural retina, and emerging ganglion and amacrine cells during retinogenesis PMID: 15465490
  35. Fgf15 is directly regulated by Shh signaling through Gli proteins in the developing diencephalon and midbrain PMID: 15614767
  36. in the mouse, loss of FG15 gene function results in high penetrant VSDs and alignment defects of the aorta and pulmonary trunk PMID: 15789410
  37. fibroblast growth factor 15 (FGF15) signals from intestine to liver to repress the gene encoding cholesterol 7alpha-hydroxylase (CYP7A1), which catalyzes the first and rate-limiting step in the classical bile acid synthetic pathway PMID: 16213224
  38. identified two enhancers: one directed lacZ expression in the hindbrain/spinal cord and the other in the posterior midbrain (pmb), rhombomere1 (r1) and pharyngeal epithelia PMID: 16930954
  39. compare the expression pattern during neural development of chick Fgf19 with mouse Fgf15. PMID: 17654705
  40. These findings suggest that the repressor form of Gli2 preferentially binds to the GliREs to control Fgf15 expression. PMID: 18279667
  41. FGF15 and FGF8 have distinct signaling properties, and opposite effects on neocortical patterning and differentiation PMID: 18625063
  42. The results of this study indicate that both beta-Klotho and FGF-15/19 repress the apical sodium-dependent bile acid transporter in enterocytes and cholangiocytes. PMID: 18772362
  43. FGF15/FGFR4 integrates growth factor signaling with hepatic bile acid metabolism and insulin action PMID: 19237543
  44. Results suggest that FGF19-regulated liver bile acid metabolism could be independent of its glucose-lowering effect, and direct FGFR activation in adipose tissue may play an important role in the regulation of glucose homeostasis. PMID: 19706524

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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