Recombinant Mouse Fibroblast Growth Factor 1 (FGF1) Protein (His)

Name: Recombinant Mouse Fibroblast Growth Factor 1 (FGF1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10085P
Price: 549.6 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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 1 (FGF1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P61148
Target Symbol	FGF1
Synonyms	Fgf1; Fgf-1; Fgfa; Fibroblast growth factor 1; FGF-1; Acidic fibroblast growth factor; aFGF; Heparin-binding growth factor 1; HBGF-1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	FNLPLGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESAGEVYIKGTETGQYLAMDTEGLLYGSQTPNEECLFLERLEENHYNTYTSKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD
Expression Range	16-155aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.8kDa
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	Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis.
Subcellular Location	Secreted. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytosol. Nucleus.
Protein Families	Heparin-binding growth factors family
Database References	KEGG: mmu:14164 STRING: 10090.ENSMUSP00000045710 UniGene: Mm.241282

Gene Functions References

The present results provided evidence that aFGF accelerates the progression of atherosclerosis and suggested that aFGF may be a potential therapeutic target for the prevention of atherosclerosis development. PMID: 29845277
TUG1 knockdown ameliorates atherosclerosis by modulating FGF1 via miR-133a in ApoE knockout mice. PMID: 29268138
Fibroblast growth factor (FGF1 and FGF2), but not vascular endothelial growth factor (VEGF) rescued Psen1-/- cells from serum starvation induced apoptosis.In the absence of serum, FGF2 immunoreactivity was distributed diffusely in cytoplasmic and nuclear vesicles of wt and Psen1-/- cells, as levels of FGF2 in nuclear and cytosolic fractions were not significantly different. PMID: 27443835
Suboptimal FGFR activation by a weak FGF1-FGFR dimer is sufficient to evoke a metabolic response, whereas full FGFR activation by stable and sustained dimerization is required to elicit a mitogenic response. PMID: 28813681
FGF1 protects neuroblastoma cells from p53-dependent apoptosis through an intracrine pathway regulated by FGF1 phosphorylation. PMID: 29048426
the HDAC3-N-CoR corepressor complex leaves the Fgf1b promoter and a complex involving the translocated CRTC1, phosphorylated CREB, and histone acetyltransferase CBP induces transient transcription. PMID: 28076781
lncRNA-Map2k4 is the target gene of miR-199a, and its down-regulation promotes miR-199a expression in neurons. miR-199a targeted regulation of FGF1 expression in neurons. PMID: 28655615
clearly demonstrate the different specificity of FGF12-FGFR1c2 and FGF22-FGFR1c2 for well defined HS structures and suggest that it is now possible to chemoenzymatically synthesize precise HS polysaccharides that can selectively mediate growth factor signaling PMID: 28031461
The study supports a pro-adipogenic role for betaKlotho in skeletal muscle fibro/adipogenesis and calls for further research on involvement of the FGF-FGFR-betaKlotho axis in the fibro/adipogenic infiltration associated with functional deterioration of skeletal muscle in aging and muscular dystrophy. PMID: 26881702
fibroblast growth factor 1 (FGF1) to be synergistically induced by heat shock and wounding. PMID: 27638903
Data suggest that Fgf1-mediated signaling represents an important signaling cascade related to adipogenesis and visceral adiposity; expression of Fgf1 (fibroblast growth factor 1) and Fgfr1 (fibroblast growth factor receptor 1) is up-regulated in adipose tissue of obese mice (both obese mice due to high-fat diet and obese mice due to genetic deletion of leptin). PMID: 26847131
These results suggest that FGFs promote hair growth by inducing the anagen phase in resting hair follicles and might be a potential hair growth-promoting agent. PMID: 25685806
Study presents a transcript profiling of remyelinated multiple sclerosis lesions and identified FGF1 as a promoter of remyelination PMID: 25589163
Nucleolin-FGF1 interaction is critical for the intranuclear phosphorylation of FGF1 by PKCdelta and thereby the regulation of nuclear export of FGF1. PMID: 24595027
parenteral delivery of a single dose of recombinant FGF1 (rFGF1) results in potent, insulin-dependent lowering of glucose levels in diabetic mice that is dose-dependent but does not lead to hypoglycaemia PMID: 25043058
Although FGF1 transgenic mice had a normal phenotype with unperturbed kidney structure, they showed a severely inhibited kidney repair after unilateral ischemia/reperfusion. This was manifested by a strong decrease of postischemic kidney size and weight. PMID: 22606265
RA via RALDH2 has separable functions in the developing spinal cord to (i) maintain high levels of FGF and Notch signaling and (ii) drive stem cell differentiation, thus restricting both the numbers and the pluripotent character of neural stem cells PMID: 22396766
discovery of a phenotype for the FGF1 knockout mouse establishes the PPARgamma-FGF1 axis as critical for maintaining metabolic homeostasis and insulin sensitization PMID: 22522926
The results demonstrate that the FGF1/FGFR1 complex constitutes a signalling module that independently of the receptor tyrosine kinase can convey a signal that initiates a strictly timed and periodic release of endocytosed FGF1 into the cytosol/nucleus. PMID: 21223966
RFX1 may negatively regulate the self-renewal of GBM-SCs through modulating FGF-1B and FGF1 expression levels by binding the 18-bp cis-elements of the F1B promoter. PMID: 20189986
the neuroprotective effects of FGF1 involve inactivation of GSK3beta PMID: 12095987
FGF-1, FGF-2 and FGF receptor-1 levels in the cochlear nucleus following acoustic overstimulation PMID: 12121735
the depletion of FGF1 may be a key regulatory component in initial phase of branching morphogenesis of the lung bud epithelium in vitro PMID: 12128203
Agonist role for FGF1 and FGF2 in specifically insult-induced liver matrix deposition and hepatic fibrogenesis and a potential target for the prevention of hepatic fibrosis. PMID: 14507672
non-classical release is mediated by synaptotagmin 1 PMID: 14559220
High steady-state levels of ONOO(-) may induce cysteine oxidation, tyrosine nitration, and non-nreversible inactivation of FGF-1, a inhibitory feedback mechanism restoring cellular homeostatis during resolution of inflammation and repair. PMID: 14592461
Gab1 is essential for FGF1 stimulation of both PI 3-kinase and the antiapoptotic protein kinase Akt, while FGF1-induced MAPK stimulation is not affected by Gab1 deficiency. PMID: 15199124
Data show that mouse and human fibroblast growth factor 1 (FGF-1) internal ribosome entry sites show similar activity profiles, and have a conserved structural domain at both the nucleotide sequence and RNA structure levels. PMID: 15314170
Phosphorylation of Fgf1 occurs in the nucleus by pkcdelta. It is then exported to the cytosol. PMID: 15574884
Hsp90 is required for translocation of FGF-1 and FGF-2 across the endosomal membrane PMID: 16495214
FGF7- and FGF1-induced mitogenesis and downstream signaling is controlled by distinct heparin octasaccharide motifs PMID: 16728399
FGF1 and p40 synaptotagmin 1 release correlates with membrane destabilizing ability PMID: 16930531
These results identify a novel aspect of the crosstalk between FGF and thrombin signaling pathways which both play important roles in tissue repair and angiogenesis. PMID: 17027650
Shisa is antagonistic to Wnt and Fgf signalings PMID: 17481602
In apoE-deficient mouse astrocytes, FGF-1 stimulated cholesterol biosynthesis without enhancing its release, indicating a signaling pathway independent of apoE biosynthesis upregulation. PMID: 17548887
Formation of the FGF-1-exportin-1-Ran-GTP complex in vitro as well as nuclear export of FGF-1 in vivo was dependent on phosphorylation of FGF-1, and it was abolished by leptomycin B. PMID: 17616529
sphingosine kinase 1 is a component of the copper-dependent FGF1 release pathway. PMID: 17643421
A conserved, specific and stage-dependent requirement for Erk1/2 signalling downstream of FGF-induced neural specification in higher vertebrates. PMID: 17660197
FGF and PDGF have roles in cell proliferation and migration in osteoblastic cells PMID: 17852407
analysis of expression of bicistronic vector driven by the FGF-1 IRES in mouse muscle PMID: 17963525
6-O-sulfate in HS may regulate the signalings of some of HB-GFs, including FGF-1, FGF-2 and FGF-4, by inducing different interactions between ligands and their receptors PMID: 18281280
and fibroblast growth factor signaling interact to control the proximal-distal pattern of forming airways in the mammalian lung PMID: 18694942
These data demonstrate the existence of novel cross-talk between thrombin, FGF, and Notch signaling pathways, which play important roles in vascular formation and remodeling. PMID: 18784255
An interplay between retinoic acid, Fgf and Shh signalling is likely to be an important mechanism underpinning the tight regulation of caudal embryonic development. PMID: 19168680
A detailed double-label immunohistochemical investigation of the localization patterns of FGF1 and its receptors FGFR1 and FGFR2 in adult and early postnatal mouse retinas, is reported. PMID: 19408015
Results revealed a mechanism of molecular coupling of mRNA transcription and translation, involving a unique process of IRES activation by a FGF1 promoter element. PMID: 19561198
that the main role of heparin in FGF-induced signaling is to protect this naturally unstable protein against heat and/or proteolytic degradation and heparin is not essential for a direct FGF1-FGFR interaction and receptor activation PMID: 19574212

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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.