Biotinylated Recombinant Human Fibroblast Growth Factor 2 (FGF2) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-01556P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Biotinylated Recombinant Human Fibroblast Growth Factor 2 (FGF2) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-01556P
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Product Overview

Description Biotinylated Recombinant Human Fibroblast Growth Factor 2 (FGF2) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P09038
Target Symbol FGF2
Synonyms Basic fibroblast growth factor;bFGFHeparin-binding growth factor 2;HBGF-2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-MBP&C-6His-Avi
Target Protein Sequence PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS
Expression Range 143-288aa
Protein Length Full Length of Mature Protein
Mol. Weight 64.2 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: 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.

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

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