Human FGF2b Recombinant Protein

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Product nameHuman FGF2b Recombinant Protein
Uniprot IDP09038
Uniprot linkhttp://www.uniprot.org/uniprot/P09038
Origin speciesHomo sapiens (Human)
Expression systemProkaryotic expression
SequenceMAHNHRHKHKLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVC ANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS
Molecular weight17,76 kDa
Protein delivered with Tag?Yes
Purity estimated90%
BufferPBS, Urea 8M
Formliquid
Delivery conditionDry Ice
Delivery lead time in business days10-25
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
Fragment TypePartial
Protein AccessionAAA52534.1
Spec:Entrez GeneID2247
Spec:NCBI Gene AliasesFGFB, HBGF-2, FGF-2, BFGF
Spec:SwissProtIDP09038
NCBI ReferenceAAA52534.1
Aliases /SynonymsFGF2b, basic fibroblast Growth Factor proteins, FGF2, Fibroblast Growth Factor proteins 2, FGF-2, bFGF, Heparin-binding Growth Factor proteins 2, HBGF-2
ReferencePX-P1089
NoteFor research use only

Description of Human FGF2b Recombinant Protein

The Structure of Human FGF2b Recombinant Protein

Human FGF2b (Fibroblast Growth Factor 2b) is a recombinant protein that belongs to the fibroblast growth factor family. It is a small, highly conserved protein consisting of 146 amino acids with a molecular weight of approximately 17 kDa. The structure of FGF2b is characterized by a central beta-sheet surrounded by three alpha-helices, forming a compact globular structure. This structure is stabilized by disulfide bonds between cysteine residues.

The Activity of Human FGF2b Recombinant Protein

Human FGF2b is a potent mitogen, meaning it stimulates cell division and proliferation. It exerts its activity by binding to and activating specific cell surface receptors, known as FGF receptors (FGFRs). FGF2b can bind to all four known FGFRs (FGFR1-4), but it has a higher affinity for FGFR1 and FGFR2. Upon binding, FGF2b induces a conformational change in the receptor, leading to the activation of downstream signaling pathways, such as the MAPK and PI3K/AKT pathways.

The main role of FGF2b is to promote cell growth and survival. It is involved in various physiological processes, including embryonic development, tissue repair, and angiogenesis. FGF2b is also known to have neurotrophic and neuroprotective effects, making it a potential therapeutic target for neurological disorders.

The Application of Human FGF2b Recombinant Protein

Due to its potent mitogenic and pro-survival activity, human FGF2b recombinant protein has been extensively studied for its potential therapeutic applications. One of the most promising uses of FGF2b is in tissue repair and regeneration. FGF2b has been shown to promote the proliferation and migration of various cell types, including fibroblasts, endothelial cells, and mesenchymal stem cells, which are essential for tissue repair and wound healing.

In addition, FGF2b has been investigated as a potential treatment for various diseases and conditions, including cardiovascular diseases, bone disorders, and neurological disorders. In cardiovascular diseases, FGF2b has been shown to promote angiogenesis and improve blood flow, making it a potential therapy for conditions such as coronary artery disease and peripheral arterial disease.

In bone disorders, FGF2b has been studied for its ability to enhance bone healing and regeneration. FGF2b has been shown to stimulate the proliferation and differentiation of osteoblasts, the cells responsible for bone formation, and has been investigated as a potential treatment for conditions such as osteoporosis and bone fractures.

In neurological disorders, FGF2b has shown promising results in promoting nerve cell growth and survival. It has been studied as a potential treatment for conditions such as spinal cord injury, stroke, and Parkinson’s disease.

Targeting FGF2b as a Drug Target

The potent mitogenic and pro-survival activity of FGF2b makes it an attractive drug target for various diseases and conditions. However, targeting FGF2b directly has proven to be challenging due to its ability to bind to multiple receptors and its role in various physiological processes.

Instead, researchers have focused on developing small molecule inhibitors that can block the activity of FGF2b by binding to its receptors. These inhibitors have shown promising results in preclinical studies for the treatment of various diseases, including cancer and cardiovascular diseases.

Another approach to targeting FGF2b is through the use of monoclonal antibodies. These antibodies can specifically bind to FGF2b and block its activity, making them potential therapeutics for diseases such as cancer and autoimmune disorders.

In conclusion, human FGF2b recombinant protein is a small but powerful protein with diverse biological activities. Its structure and activity make it a potential therapeutic target for various diseases and conditions, and ongoing research is focused on developing effective treatments targeting FGF2b.

Publication

  • 1: Wróbel T, Butrym A, Łacina P, Rybka J, Gębura K, Mazur G, Bogunia-Kubik K. bFGF Polymorphism Is Associated with Disease Progression and Response to Chemotherapy in Multiple Myeloma Patients. Anticancer Res. 2017 Apr;37(4):1799-1803. PubMed PMID: 28373444.
  • 2: Neutralizing Monoclonal Antibody 3B1 Against Human Basic Fibroblast Growth Factor. Monoclon Antib Immunodiagn Immunother. 2016 Apr;35(2):122. doi: 10.1089/mab.2015.0080. PubMed PMID: 27097071.
  • 3: Hao RH, Guo Y, Dong SS, Weng GZ, Yan H, Zhu DL, Chen XF, Chen JB, Yang TL. Associations of Plasma FGF2 Levels and Polymorphisms in the FGF2 Gene with Obesity Phenotypes in Han Chinese Population. Sci Rep. 2016 Feb 16;6:19868. doi: 10.1038/srep19868. PubMed PMID: 26879180; PubMed Central PMCID: PMC4754629.
  • 4: Shi H, Xu J, Zhao R, Wu H, Gu L, Chen Y. FGF2 regulates proliferation, migration, and invasion of ECA109 cells through PI3K/Akt signalling pathway in vitro. Cell Biol Int. 2016 May;40(5):524-33. doi: 10.1002/cbin.10588. Epub 2016 Mar 9. PubMed PMID: 26833879.
  • 5: Hu M, Hu Y, He J, Li B. Prognostic Value of Basic Fibroblast Growth Factor proteins (bFGF) in Lung Cancer: A Systematic Review with Meta-Analysis. PLoS One. 2016 Jan 29;11(1):e0147374. doi: 10.1371/journal.pone.0147374. eCollection 2016. Review. PubMed PMID: 26824699; PubMed Central PMCID: PMC4732945.
  • 6: Ye L, Yang Y, Zhang X, Cai P, Li R, Chen D, Wei X, Zhang X, Xu H, Xiao J, Li X, Lin L, Zhang H. The Role of bFGF in the Excessive Activation of Astrocytes Is Related to the Inhibition of TLR4/NFκB Signals. Int J Mol Sci. 2015 Dec 28;17(1). pii: E37. doi: 10.3390/ijms17010037. PubMed PMID: 26729092; PubMed Central PMCID: PMC4730282.
  • 7: Twaroski K, Mallanna SK, Jing R, DiFurio F, Urick A, Duncan SA. FGF2 mediates hepatic progenitor cell formation during human pluripotent stem cell differentiation by inducing the WNT antagonist NKD1. Genes Dev. 2015 Dec 1;29(23):2463-74. doi: 10.1101/gad.268961.115. PubMed PMID: 26637527; PubMed Central PMCID: PMC4691950.
  • 8: Lim S, Cho H, Lee E, Won Y, Kim C, Ahn W, Lee E, Son Y. Osteogenic stimulation of human adipose-derived stem cells by pre-treatment with fibroblast growth factor 2. Cell Tissue Res. 2016 Apr;364(1):137-47. doi: 10.1007/s00441-015-2311-8. Epub 2015 Nov 7. PubMed PMID: 26547859.
  • 9: Chen Y, Zhu G, Wu K, Gao Y, Zeng J, Shi Q, Guo P, Wang X, Chang LS, Li L, He D. FGF2-mediated reciprocal tumor cell-endothelial cell interplay contributes to the growth of chemoresistant cells: a potential mechanism for superficial bladder cancer recurrence. Tumour Biol. 2016 Apr;37(4):4313-21. doi: 10.1007/s13277-015-4214-4. Epub 2015 Oct 22. PubMed PMID: 26493998.
  • 10: Zhao W, Yu H, Han Z, Gao N, Xue J, Wang Y. Clinical significance of joint detection of serum CEA, SCCA, and bFGF in the diagnosis of lung cancer. Int J Clin Exp Pathol. 2015 Aug 1;8(8):9506-11. eCollection 2015. PubMed PMID: 26464712; PubMed Central PMCID: PMC4583944.
  • 11: Litwin M, Radwańska A, Paprocka M, Kieda C, Dobosz T, Witkiewicz W, Baczyńska D. The role of FGF2 in migration and tubulogenesis of endothelial progenitor cells in relation to pro-angiogenic Growth Factor proteins production. Mol Cell Biochem. 2015 Dec;410(1-2):131-42. doi: 10.1007/s11010-015-2545-5. Epub 2015 Aug 28. PubMed PMID: 26314253.
  • 12: Fessler E, Borovski T, Medema JP. Endothelial cells induce cancer stem cell features in differentiated glioblastoma cells via bFGF. Mol Cancer. 2015 Aug 19;14:157. doi: 10.1186/s12943-015-0420-3. PubMed PMID: 26282129; PubMed Central PMCID: PMC4539660.
  • 13: Jerebtsova M, Das JR, Tang P, Wong E, Ray PE. Angiopoietin-1 prevents severe bleeding complications induced by heparin-like drugs and fibroblast growth factor-2 in mice. Am J Physiol Heart Circ Physiol. 2015 Oct;309(8):H1314-25. doi: 10.1152/ajpheart.00373.2015. Epub 2015 Aug 14. PubMed PMID: 26276817; PubMed Central PMCID: PMC4666966.
  • 14: Hurley MM, Adams DJ, Wang L, Jiang X, Burt PM, Du E, Xiao L. Accelerated fracture healing in transgenic mice overexpressing an anabolic isoform of fibroblast Growth Factor proteins 2. J Cell Biochem. 2016 Mar;117(3):599-611. doi: 10.1002/jcb.25308. PubMed PMID: 26252425.
  • 15: Li S, Payne S, Wang F, Claus P, Su Z, Groth J, Geradts J, de Ridder G, Alvarez R, Marcom PK, Pizzo SV, Bachelder RE. Nuclear basic fibroblast growth factor regulates triple-negative breast cancer chemo-resistance. Breast Cancer Res. 2015 Jul 4;17:91. doi: 10.1186/s13058-015-0590-3. PubMed PMID: 26141457; PubMed Central PMCID: PMC4491247.

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