epitope corresponding to amino acids 258-348 of FRS2 of human origin
Modification Notes
FRS2 (also designated SNT or p90) is a lipid-anchored docking protein that becomes tyrosine phosphorylated in response to FGF or NGF stimulation and subsequently binds to GRB2/Sos complexes (1-4). The GRB2 adapter protein links receptor tyrosine kinases to the Ras/MAPK signaling pathway but does not interact directly with FGF receptors (5,6). FRS2 thus provides a link between activation of FGF and NGF receptors and the Ras/MAPK pathway. FRS2 contains four Grb2 binding sites, a myristylation sequence and a PTP domain (1). Myristylation of FRS2 is essential for membrane localization, tyrosine phosphorylation, GRB2/Sos recruitment and MAPK activation (1). The function of FRS2 in FGF receptor signaling is analogous to that of IRS1 in response to insulin receptor stimulation (7).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
recommended for detection of FRS2 of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 258-348 of FRS2 of human origin
Tissue Specificity
epitope corresponding to amino acids 258-348 of FRS2 of human origin
Immunoperoxidase staining of formalin fixed, paraffin-embedded human pancreas tissue showing cytoplasmic staining of glandular cells.
Application
Western blot analysis of FRS2 expression in NIH/3T3 whole cell lysate.
Application Notes
recommended for detection of FRS2 of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.