Recombinant Mouse Fibroblast Growth Factor 2 (FGF2) Protein (His)

Name: Recombinant Mouse Fibroblast Growth Factor 2 (FGF2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06775P
Availability: InStock

Collections: Cytokines, Cytokines and growth factors, Enzymes, Featured enzyme molecules, Growth factors and receptors, Kinase, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Fibroblast Growth Factor 2 (FGF2) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P15655
Target Symbol	FGF2
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-10His
Target Protein Sequence	PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYSSWYVALKRTGQYKLGPKTGPGQKAILFLPMSAKS
Expression Range	10-155aa
Protein Length	Full Length of Mature Protein
Mol. Weight	18.9 kDa
Research Area	Others
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	Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. Also acts as an integrin ligand which is required for FGF2 signaling. Binds to integrin ITGAV:ITGB3. Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Can induce angiogenesis. Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation.
Subcellular Location	Secreted. Nucleus.
Protein Families	Heparin-binding growth factors family
Database References	KEGG: mmu:14173 STRING: 10090.ENSMUSP00000037694 UniGene: Mm.473689

Gene Functions References

expressed in tissues of the female reproductive tract; affects sperm motility and acrosomal exocytosis PMID: 29866768
present study highlights the central role for FGF-2 in the progression and maintenance of newly acquired blood and lymphatic vessels in the cornea of HSV-1-infected mice in the absence of infectious virions PMID: 28378806
NF-kappaBmiR15abFGF/VEGFA axis contributes to the impaired angiogenic capacity of bone marrowmesenchymal stem cells in high fat dietfed mice. PMID: 28944834
Knockout of the 18-kDa FGF-2 isoform significantly attenuated atherogenesis, reduced aortic plaques, reduced macrophage infiltration and suppressed oxidative stress in mice fed with a high fat diet at all-time points. PMID: 29466783
Data show that exostosin-like 2 (EXTL2) controls fibroblast growth factor 2 (FGF2) signaling through regulation of heparan sulfate biosynthesis. PMID: 29305908
FGF2 signaling can regulate osteoblastic niche cells to support HSC homeostasis in response to bone marrow damage PMID: 28662672
Dynamic changes in heparan sulfate during muscle differentiation and ageing regulate myoblast cell fate and FGF2 signaling. PMID: 27496348
altered glycosaminoglycans (GAG) distribution in mucopolysaccharidoses I (MPS I) chondrocytes, and altered GAG, FGF2 and Indian hedgehog distribution in growth plates from MPS I mice, is reported. PMID: 27105565
Data show that LOX-PP enhances adipogenesis at least partially through inhibition of FGF-2 receptor signaling. PMID: 28452589
tissue engineered periosteum can deliver FGF-2, TGF-beta1, and ASCs to a mouse critical-sized femur defect and further optimization may yield improved bone allograft healing. PMID: 27874253
Thus, FGF-2 levels in hESCs culture systems can be manipulated to generate cells with longer telomere which would be advantageous in the applications of hESCs in regenerative medicine. PMID: 27757766
Low FGF2 expression is associated with cardiac ischemia and systolic dysfunction. PMID: 28771625
Mechanical strain stimulates vasculogenesis of embryonic stem cells by the intracellular messengers ROS, NO and calcium as well as by upregulation of angiogenesis guidance molecules and the angiogenic growth factors VEGF, FGF-2 and PDGF-BB. PMID: 27725190
data suggest that FGF2 levels are critically related to anxiety behavior and hypothalamic pituitary- adrenal axis activity, likely through modulation of hippocampal glucocorticoid receptor expression, an effect that is likely receptor mediated, albeit not by FGFR1, FGFR2, and FGFR3. PMID: 27133954
The differentiation of ERF-overexpressing trophoblast stem cell lines also suggests that ERF may have an FGF2-independent effect during the commitment towards syncytiotrophoblasts. PMID: 28244611
Novel VF-Trap fusion protein on blockage of VEGF and FGF-2 activity to prevent angiogenesis. PMID: 27130666
FGF2 is an extracellular inducer of COUP-TFII expression and may suppress the osteogenic potential of mesenchymal cells by inducing COUP-TFII expression prior to the onset of osteogenic differentiation PMID: 27404388
These results support that controlling the aberrant expression of TGF-beta1 and FGF-2 via inhibition of Wnt/beta-catenin signaling could serve as a potential therapeutic strategy for pulmonary fibrosis. PMID: 27112840
(125)I-bFGF mAb inhibits growth of experimental hepatocellular carcinomas. PMID: 27275095
In vivo, GSPP treatment (200 mg/kg/d) not only inhibited the growth of colon carcinoma, but also inhibited the tumor lymphangiogenesis. Conclusion. GSPP possesses the antitumor ability by inhibiting bFGF-inducing lymphangiogenesis in vitro and in vivo, which may further inhibit tumor lymphatic metastasis. PMID: 27190997
The present study indicates that a broad array of genes associated with functions of the cytoskeleton is significantly dysregulated in the MSC cortex of FGF-2 knockout mice PMID: 26970009
Lack of fibroblast growth factor-2 results in an increased volume of the striatal target area in mice. PMID: 26642808
Low RICTOR expression was detected in quiescent, confluent mouse aortic endothelial cells, whereas high doses of FGF2 induced high RICTOR expression that was associated with strong mTORC2-specific protein kinase Ca and AKT phosphorylation PMID: 26635098
Endogenous FGF2 secreted by trophoectoderm cells regulates protein expression and distribution in trophectoderm cells via FGFR2. PMID: 26378412
IL-1beta promotes FGF-2 expression in chondrocytes PMID: 26811540
FGF2 monoclonal antibody inhibited angiogenesis B16-F10 metastatic melanoma model. PMID: 26655277
Both cell proliferation and hair inductive activity in murine DPCs are maintained by the synergistic effect of fibroblast growth factor 2 and platelet-derived growth factor receptor alpha. PMID: 25975959
These results demonstrated that recombinant human endostatin could in-hibit tumor metastasis by inhibition of the expression of c-Myc and bFGF in gastric cancer tissue as well as by inhibition of angiogenesis PMID: 26125720
Cytosolic LMW FGF2 functions as a negative regulator in RIG-I-mediated antiviral signaling. PMID: 26466960
Data show that, depending of its concentration, FGF2 can be either a positive or negative factor of adipogenesis by regulating the ERK signaling pathway providing a mechanistic basis for FGF2 roles in adipogenesis and development of fat tissues. PMID: 25790378
Trans-regulation of oligodendrocyte myelination by neurons through Arf6-regulated secretion of fibroblast growth factor-2. PMID: 25144208
Data indicate that microbiota-driven fibroblast growth factor 2 (FGF2) and interleukin-17 (IL-17) cooperate to repair the damaged intestinal epithelium. PMID: 26320657
suggest that CD44-positive cells might be a source of cerebellar oligodendrocytes and that FGF-2 plays important roles in their development at an early postnatal stage PMID: 26079890
This study reveals a novel role for the ERK5-MEF2 cascade, linking bFGF-induced PAI-1 expression and subsequent mitogenic processes in lung fibroblasts. PMID: 26032256
Astrocyte-derived bFGF is required for regulation of dopaminergic neurons differentiation of the stem cells and may provide a strategy targeting astrocytes for treatment of Parkinson's disease. PMID: 25517983
both bone morphogenetic protein and Wnt pathways may be involved in mediating the effects of fibroblast growth factor 2 on dental pulp cells PMID: 25158181
FGF2 isoforms modulate bone and phosphate homeostasis via multiple pathways related to bone formation, osteoblast differentiation, and Wnt and Fgf2 signaling. PMID: 25389287
Endostar might exert its anti-tumor effect via suppressing b-FGF-induced angiogenesis and b-FGF-activated MAPK signaling pathway. PMID: 25597785
Basic FGF stimulated mesenchymal stem cell proliferation is NF-kappaB pathway dependent. PMID: 25065316
FGF2 acts as a protective growth factor after lung epithelial injury, and call into question the role of FGF2 as a profibrotic growth factor in vivo. PMID: 24988442
The augmentation of FGF2 expression and reduced optokinetic responses during the resolution of surface vasculopathy may indicate a role for FGF2 in the maintenance of neuroretinal function in OIR/ROP. PMID: 25525167
These studies demonstrate a feedback loop between Klotho depletion and FGF2 activation in renal fibrosis. PMID: 25130652
These findings indicate that the lens epithelium of MCT mice has increased expression of TGFbeta before cataract affection and that changes in the expression of FGF2 as well as TGFbeta may contribute to the progression of the cataract in the mice. PMID: 24279395
FGF2 regulates lymphatic endothelial cell -specific gene expression and suppresses TGFB1 signalling through Smad2. PMID: 24357720
Topical secretoneurin gene therapy accelerates diabetic wound healing by interaction between heparan-sulfate proteoglycans and basic FGF. PMID: 23918206
131 FGF2-regulated miRNAs during lens fiber cell differentiation PMID: 24142921
In this model the S-domains at the non-reducing ends of the two HS proteoglycan chains are proposed to interact with the FGF2-FGFR2 protein complex. PMID: 24563485
Data suggest that Fgf2-Fgfr2 (fibroblast growth factor 2/fibroblast growth factor receptor 2) signal cascade is involved in stimulating cell proliferation in prostate basal epithelium in absence of androgen replacement therapy following castration. PMID: 23946540
Therefore, constitutive deletion of Fgf2 or Fgfr1 knockdown in oligodendrocyte lineage cells is sufficient to overcome impairment of sensorimotor coordination after cuprizone demyelination. PMID: 23684572
expression of Mll-Ell in myeloid progenitor cells resulted in autocrine production of Fgf2 and Fgf2-dependent cytokine hypersensitivity. PMID: 24089521

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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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