Product Pathways - MAPK Signaling
Spry1 (D9V6P) Rabbit mAb #13013
|13013S||100 µl (10 western blots)||---||In Stock||---|
|13013||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat||Endogenous||35||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
Spry1 (D9V6P) Rabbit mAb recognizes endogenous levels of total Spry1 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg70 of human Spry1 protein.
Western blot analysis of extracts from various cell lines using Spry1 (D9V6P) Rabbit mAb.
Immunoprecipitation of Spry1 from 293 cell extracts using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or Spry1 (D9V6P) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using Spry1 (D9V6P) Rabbit mAb.
Spry1 is a member of the Sprouty (Spry) family proteins that was initially identified in Drosophila as an inhibitor of the FGF signaling pathway (1). There are four human Spry proteins (Spry1-4), encoded by different genes, and they all share a highly conserved carboxy-terminal cystine-rich Spry domain that is known to be essential for their receptor tyrosine kinase inhibitory function stimulated by various growth factors (1-3). Spry1 and other Spry proteins play a key role in embryonic development, tissue and organ formation, as well as growth in almost all living organisms (1-4). Spry proteins are considered tumor suppressors due to their inhibitory function in a variety of growth factor signaling pathways (2,3). Spry1 anchors itself to the membrane by palmitoylation and can translocate from the cytosol to the membrane by binding to caveolin-1 (5,6). Regulation of Spry1 protein function is thought to occur at various levels. Spry1 regulation includes transcriptional regulation by growth factors and kinases (1,4,7), post-transcriptional regulation by microRNA-21 (8), post-translational modifications including phosphorylation, dephosphorylation, ubiquitination and proteasomal degradation, and regulation by its interacting protein partners (2,3).
- Hacohen, N. et al. (1998) Cell 92, 253-63.
- Edwin, F. et al. (2009) Mol Pharmacol 76, 679-91.
- Guy, G.R. et al. (2009) J Endocrinol 203, 191-202.
- Minowada, G. et al. (1999) Development 126, 4465-75.
- Impagnatiello, M.A. et al. (2001) J Cell Biol 152, 1087-98.
- Hanafusa, H. et al. (2002) Nat Cell Biol 4, 850-8.
- Ozaki, K. et al. (2001) Biochem Biophys Res Commun 285, 1084-8.
- Thum, T. et al. (2008) Nature 456, 980-4.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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