Rat Fibroblast Growth Factor Receptor 1 (FGFR1) Protein
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Description
FGFR1 Protein is a recombinant Rat protein expressed in E. coli.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Fibroblast Growth Factor Receptor 1 (FGFR1) |
| Host | E. coli |
| Origin | Rat |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 43.2 kDa Observed MW (SDS-PAGE): 48 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Arg22-Glu376 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 95% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in 20 mM Tris, 150 mM NaCl, pH 8.0. If a higher concentration is required, the product can be reconstituted directly in 20 mM Tris, 150 mM NaCl, pH 8.0, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 1 mM EDTA, 1 mM DTT, 0.01% Sarcosyl, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q04589 |
| Gene ID | 79114 |
| Alias | H2,H3,H4,5,CEK,FLG,BFGFR,N-SAN,CD331,FGFR-1,Proto-oncogene c-Fgr,Fms-like tyrosine kinase 2,Pfeiffer syndrome |
| Background | Protein FGFR1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
Fibroblast growth factor receptor 1 (FGFR1) FGFR1 is a transmembrane tyrosine kinase receptor that binds fibroblast growth factors (FGFs), playing a critical role in cellular proliferation, differentiation, and survival. FGFR1 consists of an extracellular ligand-binding domain composed of three immunoglobulin-like loops, a single transmembrane helix, and an intracellular tyrosine kinase domain. Upon FGF binding, FGFR1 undergoes dimerization and autophosphorylation, triggering downstream signaling pathways such as the MAPK, PI3K-AKT, and PLCγ pathways. FGFR1 is essential in embryonic development, angiogenesis, and tissue repair, and its dysregulation is implicated in various cancers, including lung and breast cancer, where aberrant FGFR1 activation promotes tumor growth and survival. FGFR1 is also involved in skeletal development, and mutations in the FGFR1 gene can lead to developmental disorders such as Pfeiffer syndrome. Its widespread expression in multiple tissues highlights its diverse biological roles.
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Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone(GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation.
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