FGFR2 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, IHC |
---|---|
Primary Accession | P21802 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | polyclonal |
Calculated MW | 92025 Da |
Gene ID | 2263 |
---|---|
Other Names | Fibroblast growth factor receptor 2, FGFR-2, K-sam, KGFR, Keratinocyte growth factor receptor, CD332, FGFR2, BEK, KGFR, KSAM |
Dilution | WB~~ 1:1000 IHC~~1:50-1:100 |
Format | Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.09% (W/V) sodium azide and 50% glycerol. |
Storage Conditions | -20℃ |
Name | FGFR2 |
---|---|
Synonyms | BEK, KGFR, KSAM |
Function | Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. 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. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. |
Cellular Location | Cell membrane; Single-pass type I membrane protein. Golgi apparatus. Cytoplasmic vesicle. Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded [Isoform 3]: Cell membrane; Single-pass type I membrane protein. Note=After ligand binding, the activated receptor is rapidly internalized and degraded [Isoform 13]: Secreted. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. 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. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.
REFERENCES
Dionne C.A.,et al.EMBO J. 9:2685-2692(1990).
Houssaint E.,et al.Proc. Natl. Acad. Sci. U.S.A. 87:8180-8184(1990).
Seno M.,et al.Biochim. Biophys. Acta 1089:244-246(1991).
Hattori Y.,et al.Proc. Natl. Acad. Sci. U.S.A. 87:5983-5987(1990).
Katoh M.,et al.Proc. Natl. Acad. Sci. U.S.A. 89:2960-2964(1992).

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