Fibroblast growth factor receptor 1 isoform 2, FGFR 1a, bFGF-R-1, BFGFR, CD331, CEK, ECCL, FGFBR, FGFR-1, FLG, FLT-2, FLT2, HBGFR, HH2, HRTFDS, KAL2, N-SAM, OGD.
Sterile Filtered colorless solution.
Greater than 95.0% as determined by SDS-PAGE.
FGFR1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 361 amino acids (22-374a.a.) and having a molecular mass of 40.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR1 Human is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Fibroblast growth factor receptor 1 protein, also known as FGFR1, is encoded by the FGFR1 gene. This protein belongs to a family of four related proteins called fibroblast growth factor receptors. These receptors play crucial roles in various cellular pathways and processes, including cell growth regulation, maturation, division, embryonic development, and blood vessel formation.
Human FGFR1, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain comprising 361 amino acids (22-374a.a.). It has a molecular mass of 40.1 kDa. However, on SDS-PAGE, the apparent molecular size will be approximately 40-57 kDa. This protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
The solution is colorless and sterile filtered.
The FGFR1 protein solution has a concentration of 0.5 mg/ml and is prepared in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For longer periods, it's recommended to store it frozen at -20°C. To ensure long-term stability, consider adding a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing should be avoided.
The purity is determined to be greater than 95.0% based on SDS-PAGE analysis.
Fibroblast growth factor receptor 1 isoform 2, FGFR 1a, bFGF-R-1, BFGFR, CD331, CEK, ECCL, FGFBR, FGFR-1, FLG, FLT-2, FLT2, HBGFR, HH2, HRTFDS, KAL2, N-SAM, OGD.
RPSPTLPEQA QPWGAPVEVE SFLVHPGDLL QLRCRLRDDV QSINWLRDGV QLAESNRTRI TGEEVEVQDS VPADSGLYAC VTSSPSGSDT TYFSVNVSDA LPSSEDDDDD DDSSSEEKET DNTKPNPVAP YWTSPEKMEK KLHAVPAAKT VKFKCPSSGT PNPTLRWLKN GKEFKPDHRI GGYKVRYATW SIIMDSVVPS DKGNYTCIVE NEYGSINHTY QLDVVERSPH RPILQAGLPA NKTVALGSNV EFMCKVYSDP QPHIQWLKHI EVNGSKIGPD NLPYVQILKT AGVNTTDKEM EVLHLRNVSF EDAGEYTCLA GNSIGLSHHS AWLTVLEALE ERPAVMTSPL YLELEHHHHH H
Fibroblast Growth Factor Receptor-1 (FGFR1) is a crucial receptor tyrosine kinase involved in various cellular processes, including cell growth, differentiation, and angiogenesis. The recombinant form of FGFR1, specifically the amino acid sequence from 22 to 374, is often used in research to study its function and role in different biological pathways.
FGFR1 is composed of an extracellular region, a single transmembrane span, and an intracellular tyrosine kinase domain. The extracellular region includes three immunoglobulin-like domains (D1, D2, and D3), with D2 and D3 being essential for binding to fibroblast growth factors (FGFs) . The recombinant FGFR1 (22-374 a.a.) is expressed in insect cells and is a glycosylated polypeptide chain containing 361 amino acids .
FGFR1 plays a pivotal role in several biological processes:
The binding of FGFs to the extracellular domain of FGFR1 induces receptor dimerization and activation. This leads to the autophosphorylation of tyrosine residues in the intracellular domain, triggering downstream signaling pathways such as the MAPK, PI3K-AKT, and PLCγ pathways . These pathways ultimately result in various cellular responses, including proliferation, survival, and differentiation.
Aberrant FGFR1 signaling has been implicated in several diseases, including cancer. Overexpression or mutations in FGFR1 are associated with various cancers, such as lung, breast, and head and neck cancers . Targeting FGFR1 with specific inhibitors is being explored as a therapeutic strategy for these cancers.
The recombinant form of FGFR1 (22-374 a.a.) is used in research to study its structure, function, and interactions with other proteins. It is expressed in insect cells and purified to high purity levels . This recombinant protein is valuable for investigating the molecular mechanisms of FGFR1 signaling and for developing potential therapeutic interventions.