|Detection of Human SPRY1 by Western Blot. Western blot shows lysates of 293T human embryonic kidney cell line and LNCaP human prostate cancer cell line. PVDF Membrane was probed with 0.5 µg/mL of Human SPRY1 Monoclonal Antibody (Catalog # MAB6097) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for SPRY1 at approximately 37 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
SPRY1 (sprouty homolog 1) is a 34-38 kDa 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-gamma 1, LAT, CBL, caveolin-1 and SPRY2. Human SPRY1 is 319 amino acids (aa) in length. It contains one CBL-TKB binding site (aa 51-57) that is phosphorylated at Tyr53, a Ser-rich region (aa 112-131), and a Cys-rich domain (aa 181-306) that mediates intracellular translocation. SPRY1 undergoes serine phosphorylation, ubiquitination and palmitoylation, the latter which induces SPRY1 to associate with cell membranes. Over aa 1-178, human SPRY1 shares 76% aa identity with mouse SPRY1.
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