Human Fibroblast Growth Factor Receptor 2b (FGFR2b) Protein
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Description
Human Fibroblast Growth Factor Receptor 2 (FGFR2b) Protein is a recombinant protein produced in HEK293 cells.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Fibroblast Growth Factor Receptor 2b (FGFR2b) |
| Host | HEK293 cells |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 41.2 kDa Observed MW (SDS-PAGE): 80 kDa Sequence Fragment: 22-378 AA (Isoform 3). Tag: C-terminal 10 His tag |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Purification | Purified by affinity chromatography. |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Form | Liquid |
| Tested Applications | WB |
| Buffer | PBS, containing 20% glycerol. |
| Availability | Shipped within 5-7 working days. |
| Storage | Aliquot and store between -20 °C and -80 °C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P21802-3 |
| Alias | BEK,JWS,BBDS,CEK3,CFD1,ECT1,KGFR,TK14,TK25,BFR-1,CD332,K-SAM,Keratinocyte growth factor receptor,FGFR-2 |
| Background | Protein FGFR2 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
Fibroblast growth factor receptor 2 (FGFR2) FGFR2 is a transmembrane receptor tyrosine kinase that binds fibroblast growth factors (FGFs) to regulate diverse cellular processes such as proliferation, differentiation, migration, and tissue repair. FGFR2 consists of an extracellular ligand-binding domain with three immunoglobulin-like domains, a single-pass transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding induces receptor dimerization and autophosphorylation, initiating downstream signaling cascades such as the MAPK, PI3K-AKT, and PLCγ pathways. FGFR2 is crucial in embryonic development, particularly in limb and craniofacial formation, as well as in tissue homeostasis. Mutations in FGFR2 are associated with skeletal disorders like Apert syndrome and Crouzon syndrome, which result from gain-of-function mutations leading to aberrant signaling. FGFR2 dysregulation is also implicated in cancer, particularly in breast and gastric cancers, where it promotes tumor growth, survival, and angiogenesis. Its tissue-specific splicing variants further contribute to its functional diversity across different biological contexts.
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