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

Name: Recombinant Human Fibroblast Growth Factor 2 (FGF2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-11263P
Availability: InStock

Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) FGF2.

Collections: Cytokines, Cytokines and growth factors, Enzymes, Featured enzyme molecules, Growth factors and receptors, Kinase, Recombinant fibroblast growth factor basic (fgfb/fgf2/bfgf) proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Fibroblast Growth Factor 2 (FGF2) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P09038
Target Symbol	FGF2
Synonyms	Basic fibroblast growth factor; Basic fibroblast growth factor bFGF; BFGF; FGF 2; FGF B; FGF-2; Fgf2; FGF2 basic; FGF2_HUMAN; FGFB; Fibroblast growth factor 2 (basic); Fibroblast growth factor 2; Fibroblast growth factor; basic; HBGF 2; HBGF-2; HBGF2; HBGH 2; HBGH2; Heparin binding growth factor 2 precursor; Heparin-binding growth factor 2; Prostatropin
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS
Expression Range	143-288aa
Protein Length	Full Length of Mature Protein
Mol. Weight	17.9 kDa
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	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	HGNC: 3676 OMIM: 134920 KEGG: hsa:2247 STRING: 9606.ENSP00000264498 UniGene: Hs.284244
Tissue Specificity	Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non-cancerous liver tissue.

Gene Functions References

The Novel Short Isoform of Securin Stimulates the Expression of Cyclin D3 and Angiogenesis Factors VEGFA and FGF2, but Does Not Affect the Expression of MYC Transcription Factor PMID: 29989583
miR-155 and FGF2 is associated with esophageal cancer progression. miR-155 in Tumor-associated macrophages suppressed ECA109cell proliferation, migration and invasion, as well as reduction in angiogenesis. miR-155-reduced cell growth, migration and invasion of ECA109cells is associated with FGF2 suppression. PMID: 29660336
the dual warhead-FGF2 conjugate may overcome the potential acquired resistance of FGFR1-overproducing cancer cells towards single cytotoxic drugs. PMID: 30029518
widely stained in sclerosing stromal tumours of the ovary PMID: 29433373
FGF2 initiates CYGB transcription via the JNK pathway. PMID: 28916723
A strong stromal FGF-2 expression was associated with a significantly higher clinical stage and higher biochemical recurrence rate. Patients with strong stromal FGF-2 expression also had a significantly worse biochemical recurrence-free survival. PMID: 29887238
levels of the angiogenesis mediators endoglin, HB-EGF, BMP-9 and FGF-2 in patients with severe sepsis and septic shock PMID: 28746898
Our results suggest photodynamic therapy is effective in increasing the expression of bFGF gene, an important factor in periodontal tissue regeneration and could indicate periodontal tissue regeneration PMID: 28935533
High FGF2 expression is associated with gastric cancer. PMID: 28500362
Regulation of vascular smooth muscle cell calcification by syndecan-4/FGF-2/PKCalpha signalling and cross-talk with TGF-beta1. PMID: 29016732
evaluation of the presence and localization of FGF2 in human sperm cells, and determination of FGF2 levels in semen samples and its relationship with conventional semen parameters PMID: 28732140
We have presented evidence that FGF2 promotes myofibroblast apoptosis in vivo, antagonizes pro-fibrotic TGF-beta signaling, inhibits fibroblast activation and prevents transdifferentiation of non-fibroblasts into myofibroblasts, and promotes a less fibrotic gene expression paradigm [Review] PMID: 28967471
These results demonstrate that FGF-TGFbeta signaling antagonism is the primary regulator of the smooth muscle cell phenotype switch. PMID: 27634335
Results describe a novel role of FGF2 as a modulator of osteoblast and mesenchymal stromal cell function, and provide evidence for involvement of FGF2 in leukemia pathogenesis and chemo-resistance. PMID: 27481339
Under specific experimental conditions, secretion of IL-1beta and FGF2 is triggered by phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]-dependent formation of pores across the plasma membrane. PMID: 28871048
HDAC1 depletion activates cardiac mesenchymal stromal cells proangiogenic paracrine signaling in a basic fibroblast growth factor-dependent manner. PMID: 28679560
The results suggest that FGF2/rs1048201, FGF5/rs3733336 and FGF9/rs546782 are associated with the risk of non-syndromic orofacial cleft and that these miRNA-FGF interactions may affect non-syndromic orofacial cleft development. PMID: 27511275
TEC is yet another regulator of FGF2-mediated Human pluripotent stem cells pluripotency and differentiation. PMID: 28631381
bFGF in primary tumor tissue associated with favorable breast cancer outcome and its levels significantly and positively correlated with ER levels. PMID: 28869446
Serum FGF-2 levels were statistically significantly lower in the autism spectrum patient group compared to healthy controls. PMID: 28734240
Dysregulation of the FGF2 gene represents an opportunity to understand further, and possibly intervene upon, mechanisms of wound healing in diabetics with CKD. PMID: 27237708
Out of five FGF-2 Gene Polymorphism loci, the TA genotype of rs308442 in the osteoporosis group (40.2%) was higher than in the control group (29.5%) (p < 0.05). The rs308442 locus of FGF-2 gene is closely correlated to osteoporosis in this Zhuang ethnic Chinese cohort, and the TA may be the risk genotype of osteoporosis. PMID: 28653999
Up-regulation of FGF2 and down-regulation FAM201A were correlated with the development of osteonecrosis of the femoral head after femoral neck fracture. PMID: 29382571
over-expression, isolation, and biological activity of all recombinant human FGF2 isoforms, are reported. PMID: 28433654
We found that hsa-miR-196a-3p affected expression on both mRNA and protein levels of FGF2. our study provided evidence that a functional SNP rs1048201 was associated with bone mineral density (BMD), and SNP rs1048201 variant may act by affecting binding of hsa-miR-196a-3p PMID: 28317323
Data show that mutant soluble ectodomain of FGFR2IIIc (msFGFR2c) but not wild-type soluble ectodomain of FGFR2IIIc (wsFGFR2c) could selectively bind to c subtype of FGFRs in the presence of FGF-2. PMID: 28049184
Furthermore, MERS coronavirus induced apoptosis through upregulation of Smad7 and fibroblast growth factor 2 (FGF2) expression in both kidney and lung cells. PMID: 27572168
The present work aims to investigate the relationship between the expression of AEG-1(astrocyte elevated gene-1), b-FGF(basic-fibroblast growth factor), beta-catenin, Ki-67, TNF-alpha (tumor necrosis factor-alfa) other prognostic parameters in DC (Ductal Carcinomas) and ductal intraepithelial neoplasm. We found a relationship between these factors. PMID: 26096243
Studies indicate that therapeutically targeting FGF2 and FGFR has been extensively assessed in multiple preclinical studies and numerous drugs and treatment options have been tested in clinical trials. PMID: 27007053
FGF2 is involved in melanoma development and progression. HMW FGF2 isoforms enhance in vitro motility of melanoma cells. LMW FGF2 confers stem-like features and increases in vivo metastasization. LMW FGF2 promotes angiogenesis while HMW FGF2 induces vasculogenic mimicry. PMID: 27558498
miR-105/Runx2 axis mediates FGF2-induced ADAMTS expression in osteoarthritis cartilage. PMID: 26816250
results suggest that MALAT1-mediated FGF2 protein secretion from Tumor-associated macrophages inhibits inflammatory cytokines release, promotes proliferation, migration, and invasion of FTC133 cells and induces vasculature formation. PMID: 28543663
This study reveals that Adv ECM hydrogels recapitulate matrix fiber microarchitecture of native adventitia, and retain angiogenesis-related actors and bioactive properties such as FGF2 signaling capable of influencing processes important for angiogenesis. PMID: 28167392
Data show that FGF2 mutants have potential as anti-angiogenic agents and useful tools for studying the role of integrin alphavbeta3 in FGF2 signalling. PMID: 28302677
Expression of these mediators was confirmed in end-stage COPD. Thus, accumulation of mast cells in COPD may contribute to vascular remodeling. PMID: 28298222
Results provide evidence that bFGF regulates stemness maintenance in stem cells isolated from human exfoliated deciduous teeth (SHEDs) by enhancing REX-1 mRNA expression via the FGFR and Akt signaling pathways. Moreover, IL-6 is also involved in the bFGF-induced REX1 expression. PMID: 27883224
Facial nerve regeneration using basic fibroblast growth factor-impregnated gelatin microspheres PMID: 24737684
These results indicated that FGF-2, but not FGF-10, may be supplemented during stem cell expansion to prime cells for successful chondrogenesis and osteogenesis. PMID: 27411850
the data suggest that endothelial cells regulate beta-catenin activity in adrenocortical cells also via secretion of basic fibroblast growth factor. PMID: 27889473
In an in vitro assay of vascular smooth muscle cells, circRNA WDR77 silencing significantly inhibited cell proliferation and migration. Bioinformatics methods revealed that miR-124 and fibroblast growth factor 2 (FGF-2) were downstream targets of circRNA WDR77. PMID: 29042195
FGF2 protects the tumor cells from the antiproliferative effect of Gefitinib and largely prevents reprogramming of the proteome and phosphoproteome PMID: 27794612
High FGF2 expression is associated with colon cancer metastasis. PMID: 28629469
These observations identify airway smooth muscle cells -derived FGF2b as a factor needed for LMC formation by CD4 T cells, affecting intercellular communication. PMID: 28924004
Report no relationship between serum bFGF levels and ovarian cancer microvessel density and tumor bFGF expression. PMID: 27312585
High FGF2 expression is associated with ovarian cancer. PMID: 28481872
The antitumor activity of scopoletin may be due to its strong anti-angiogenic effect, which may be mediated by its effective inhibition of ERK1, VEGF-A, and FGF-2. PMID: 27133199
TGF-beta, bFGF and epimorphin in the extracellular microenvironment cooperatively affect HSF behaviors under the control of a highly sulfated chondroitin sulfate PMID: 28209294
High FGF2 expression is associated with lung cancer. PMID: 28423625
miR-205 enhances chemosensitivity of breast cancer cells to TAC docetaxol, doxorubicin plus cyclophosphamide) by suppressing both VEGFA and FGF2, leading to evasion of apoptosis. PMID: 27362808
analyses identified a new bFGF-regulating mechanism by which hedgehog signaling regulates human fibroblast migration; this data opens a new avenue for the wound healing therapy PMID: 28363830

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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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