Recombinant Human FGFa Protein (140AA)

Name: Recombinant Human FGFa Protein (140AA)
Brand: Beta LifeScience
SKU: BL-2890NP
Availability: InStock

BL-2890NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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

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Product Overview

Description	Recombinant Human Fibroblast Growth Factor 1/Fibroblast Growth Factor Acidic is produced by our E.coli expression system and the target gene encoding Phe16-Asp155 is expressed.
Accession	P05230
Synonym	Fibroblast Growth Factor 1; FGF-1; Acidic Fibroblast Growth Factor; aFGF; Endothelial Cell Growth Factor; ECGFHeparin-Binding Growth Factor 1; HBGF-1; FGF1; FGFA
Gene Background	FGF acidic, also known as ECGF, FGF-1and HBGF-1, is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. It is a mitogenic peptide that is produced by multiple cell types and stimulates the proliferation of cells of mesodermal, ectodermal, and endodermal origin. Its association with heparan sulfate is a prerequisite for activation of FGF receptors. Internalized FGF acidic migrates to the nucleus where it is phosphorylated by nuclear PKC delta, exported to the cytosol, dephosphorylated, and degraded. Intracellular FGF acidic inhibits p53 activity and proapoptotic signaling.
Molecular Mass	16 KDa
Apmol Mass	16 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 50mM MOPS, 100mM Na2SO4, 1mM EDTA, pH 7.9.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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	HGNC: 3665 OMIM: 131220 KEGG: hsa:2246 STRING: 9606.ENSP00000338548 UniGene: Hs.483635
Tissue Specificity	Predominantly expressed in kidney and brain. Detected at much lower levels in heart and skeletal muscle.

Gene Functions References

Gas5 regulated proliferation and apoptosis in growth plate by controlling FGF1 expression via miR-21 regulation. PMID: 29490650
Modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. PMID: 29016740
FGF1 protects neuroblastoma cells from p53-dependent apoptosis through an intracrine pathway regulated by FGF1 phosphorylation. PMID: 29048426
Specific heparin derivatives molecular recognition patterns by FGF1 have been reported. PMID: 27858202
Multiple stepwise linear regression analysis found serum level of FGF1 was dependent on anti-diabetic drugs, hemoglobin A1C, body mass index and sex. Serum level of FGF1 is associated with the decreased risk of obesity in human. PMID: 28303556
Our study suggests that the genetic variants of FGF1 rs34011, more so than FGF2 rs2922979, may play a role in PE pathogenesis in Tunisian women. PMID: 27324104
FGF1 and 2 strongly prevent the osteogenic commitment and differentiation of hBMSCs. PMID: 27305863
Transfected FGF1 promotes angiogenic proliferation. PMID: 28281780
These observations suggest a crucial role for cancer-associated fibroblasts and fibroblast growth factor-1/fibroblast growth factor receptor 4 signaling in the progression of ovarian cancer. the expression level of Snail1 and MMP3 was reduced, while the expression level of E-cadherin increased PMID: 28718374
Enzyme-linked immunosorbent assay was used to detect the levels of chemokine (C-X-C motif) ligand 12, chemokine (C-X-C motif) ligand 7, hepatocyte growth factor, and fibroblast growth factor 1 in the supernatants of the laryngeal squamous cell carcinoma and control cells. PMID: 28475003
fibroblast growth factor 1 (FGF1) to be synergistically induced by heat shock and wounding. PMID: 27638903
The results indicate that suramin blocks the interaction between hFGF1 and FGFR2 D2. PMID: 27387234
activation of AurA kinase through FGF1/FGFR signaling axis sustains the stem cell characteristics of glioblastoma cells. PMID: 27138904
Study showed that both aFGF and bFGF were highly expressed in cervical cancer tissues. In tumors of higher clinical stages, the expression of these factors was further enhanced, suggesting that they play a role in facilitating cervical cancer cell proliferation. PMID: 27966750
FGF1 may play a role in the pathogenesis of T2 diabetes mellitus. PMID: 26806193
anti-importin alpha1 antibody treatment suppressed the importin alpha1-FGF1 complex formation and ERK1/2 activation, resulting in decreased cell growth. This study provides novel evidence that functional importin alpha1 is located at the cell surface, where it accelerates the proliferation of cancer cells. PMID: 26887791
The mutational introduction of a novel Cys residue (Ala66Cys) that forms a stabilizing disulfide bond (i.e., cystine) with one of the extant Cys residues (Cys83) effectively eliminates one Cys while increasing overall stability. PMID: 27019961
The role of intracellular FGF1 is to protect the cell against stress conditions by providing an additional signal for cell survival, independently of receptor-activated signaling cascades. PMID: 26840910
Data suggest folding of FGF1 is critical for its nonclassical secretion via permeability of lipid bilayer; mutation of proline135 in C-terminus of FGF1 leads to partial unfolding/decrease in FGF1's ability to permeabilize phosphatidylserine bilayers. PMID: 26836284
The analysis identified a signaling axis between FGF signaling and the transcription factor Sox1, which is preferentially expressed in stem- and mesenchymal-like breast cancers. PMID: 26365194
FGF-1 synthesis and secretion by synovial fibroblasts were significantly increased in osteoarthritis. PMID: 26400350
expression of human FGF1 solely in beta-cells in fgf1(-/-) animals prevented overnutrition induced compensatory beta-cell differentiation. PMID: 26420862
Results show that stress functionally associates FGF1 with AHNAK2 and both proteins with the cytoskeleton and their co-localization in the vicinity of the cell membrane. AHNAK2 seems to be an important element of the FGF1 export pathway. PMID: 25560297
These findings suggest that the presence of FGF1 may serve as a prognostic indicator and a potential therapeutic target for non-small cell lung cancer patients, especially for lung squamous cell carcinoma. PMID: 26391572
FGF1 expression is increased in lung from idiopathic pulmonary fibrosis patients. PMID: 26138239
FGF1-FGFR1 axis promotes tongue squamous cell carcinoma metastasis through the epithelial-mesenchymal transition pathway PMID: 26362179
p120RasGAP shields Akt from deactivating phosphatases in FGF1 signaling, but loses this ability once cleaved by caspase-3. PMID: 26109071
Study presents a transcript profiling of remyelinated multiple sclerosis lesions and identified FGF1 as a promoter of remyelination PMID: 25589163
These results suggested that human FGF1B promoter was active in ependymal cells, neurons, and a portion of dopaminergic neurons PMID: 25104610
This review is focused on the role of HDGF in tumorigenesis and metastasis, and provides insight for application in clinical cancer therapy as well as its clinical implications as a prognostic marker in cancer progression. PMID: 25236340
the sulfate in position 6 of d-glucosamine was essential for the mitogenic activity but not for the interaction with FGF-1 PMID: 25015527
While results are awaited from these clinical investigations in squamous NSCLC and other disease settings, additional research is needed to elucidate the role of FGF/FGFR signaling in the biology of NSCLC of different histologies PMID: 24711160
FGF1 gene polymorphism is associated with a lower risk of developing cleft palate or cleft lip in Iranian patients. clet palatot cleft lip PMID: 24613087
precursor of the hormone Irisin (FNCD5) were abundantly expressed in all three fat depots, along with fibroblast growth factors (FGF) FGF1, FGF7 and FGF10, whereas, FGF19 and FGF21 were undetectable. PMID: 23949615
Nucleolin-FGF1 interaction is critical for the intranuclear phosphorylation of FGF1 by PKCdelta and thereby the regulation of nuclear export of FGF1. PMID: 24595027
the genotype distribution of rs34011 within fibroblast growth factor 1 was significantly different between Alzheimer's disease and control group PMID: 24464990
discovery of unexpected, neomorphic insulin-sensitizing action for exogenous non-mitogenic human FGF1 with therapeutic potential for the treatment of insulin resistance and type 2 diabetes PMID: 25043058
By introducing two stabilizing mutations in the C-terminal part of the protein, obtained are variants highly resistant proteolytically with prolonged half-life and enhanced mitogenic activity. PMID: 24304385
Data suggest that the enhanced cell growth was likely due to the electrical stimulation up-regulated secretion of FGF-1 and FGF-2. PMID: 23990967
Both FGF1 and ERBB2 significantly influenced overall survival in breast cancer patients, especially among women with low levels of Native American ancestry. PMID: 23912956
We demonstrate that mesenchymal stromal cells increase FGF-1 secretion on co-culture with Human primary chondrocytes, which, in turn, is responsible for increased Human primary chondrocytes proliferation in pellet co-cultures. PMID: 23557133
FGF1 polymorphism is associated with breast cancer. PMID: 23143756
R50E suppresses angiogenesis induced by FGF1 or FGF2, and thereby indirectly suppresses tumorigenesis, in addition to its possible direct effect on tumor cell proliferation in vivo PMID: 23469107
studied the functional consequences of HSulf-2 activity on fibroblast growth factor (FGF)-induced mitogenesis and found that the enzyme could differentially regulate FGF1 and FGF2 activities PMID: 23457216
The expression of FGF-1 in the in vitro fertilization (IVF) implantation failure group is less than in the fertile group, which suggests that growth factors such as FGF-1 are important maternal factors effecting implantation PMID: 23426545
forms of FGF-1 that enhance thermostability or eliminate buried reactive thiols demonstrate a shorter distribution half-life, a longer elimination half-life, and a longer mean residence time (MRT) in comparison to wild-type FGF-1 PMID: 23133616
The folding transition state of FGF-1 is shown to be highly polarized, with the majority of turns adopting either native-like or denatured-like structure in the folding transition state. PMID: 23047594
LRRC59 facilitates transport of cytosolic FGF1 through nuclear pores by interaction with Kpns and movement of LRRC59 along the ER and NE membranes PMID: 22321063
[review] In this review, the authors discuss recent and ongoing research into the role of fibroblast growth factor and transforming growth factor-beta in the etiopathogenesis of craniosynostosis. PMID: 21806346
Plasticity in interactions of fibroblast growth factor 1 (FGF1) N terminus with FGF receptors underlies promiscuity of FGF1. PMID: 22057274

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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.