SPRY1 (sprouty homolog 1) is a 34-38kD member of the sprouty family of proteins. It is widely expressed, being found in multiple embryonic and adult tissues. SPRY1 is considered a negative regulator of cellular signaling. In particular, it appears to both inhibit MAP kinase signaling following RTK activation, and block TCR signaling following antigen activation. It interacts with a number of molecules, including PLC-gama-1, LAT, CBL, caveolin-1 and SPRY2. Human SPRY1 is 319 aa in length and contains one CBL-TKB binding site (aa51-57) that is phosphorylated at Tyr53, a Ser-rich region (aa112-131), and a Cys-rich domain (aa181-306) that mediates intracellular translocation. In addition, SPRY1 undergoes serine phosphorylation, ubiquitination and palmitoylation, the latter which induces SPRY1 to associate with cell membranes.
Applications:
Suitable for use in Western Blot. Other applications not tested.
Recommended Dilutions:
Western Blot: 1ug/ml
Optimal dilutions to be determined by the researcher.
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile PBS, 0.02% NaN3. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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