Cell Signaling Technology

Product Pathways - MAPK Signaling

Spry1 Antibody #8775

Applications Reactivity Sensitivity MW (kDa) Source
W IP H Endogenous 35 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Spry1 Antibody recognizes endogenous levels of total Spry1 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro144 of human Spry1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using Spry1 Antibody.

IP

IP

Immunoprecipitation of Spry1 from MOLT-4 cell extracts using Normal Rabbit IgG #2729 (lane 2) or Spry1 Antibody (lane 3). Lane 1 is 10% input. Western blot analysis was performed using Spry1 Antibody.

Background

Spry1 is a member of the Sprouty (Spry) family proteins, which 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 C-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).

  1. Hacohen, N. et al. (1998) Cell 92, 253-63.
  2. Edwin, F. et al. (2009) Mol Pharmacol 76, 679-91.
  3. Guy, G.R. et al. (2009) J Endocrinol 203, 191-202.
  4. Minowada, G. et al. (1999) Development 126, 4465-75.
  5. Impagnatiello, M.A. et al. (2001) J Cell Biol 152, 1087-98.
  6. Hanafusa, H. et al. (2002) Nat Cell Biol 4, 850-8.
  7. Ozaki, K. et al. (2001) Biochem Biophys Res Commun 285, 1084-8.
  8. Thum, T. et al. (2008) Nature 456, 980-4.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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