Anti-Spred-2 antibody produced in rabbit

Anti-Spred-2 is developed in rabbit using as immunogen a synthetic peptide corresponding to amino acids of mouse Spred-2, conjugated to KLH via an N terminal added cysteine residue. Spred-2, also known as sprouty protein with EVH-1 domain 2 related sequence, was isolated by similarity to Spred-1, which in turn was isolated from an osteoclast complementary DNA library by a two-hybrid system using c-Kit and c-Fms tyrosine kinase domains as bait. These proteins contain a carboxy-terminal cysteine-rich domain related to sprouty (the SPR domain), and an amino-terminal Ena/vasodilator stimulated phosphoprotein (VASP) homology (EVH-1) domain. This gene is mapped to human chromosome 2p14.

Spred proteins mainly function as inhibitors of the ERK and MAPK signaling cascades. Phosphorylation and Cbl-dependent ubiquitination regulate Spred-2 expression levels. Spred2 negatively modulates the hypothalamic-pituitary-adrenal axis . Anti-Spred-2 antibody is specific for human, rat, and mouse Spred-2 (approx. 48 kDa). Staining of the Spred-2 band in immunoblotting is specifically inhibited by the immunizing peptide.

synthetic peptide corresponding to amino acids 280-297 of mouse Spred 2. The sequence is conserved in rat and differs from human by three amino acids.

Anti-Spred-2 antibody produced in rabbit has been used in western blotting and indirect immunofluorescence.

Spred inhibits growth factor mediated activation of MAP kinase. Spred inhibits the activation of MAP kinase probably by mechanisms such as suppression of phosphorylation and activation of Raf. Spred-2 functions as a negative regulator of AGM (aorta-gonad-mesonephros) hematopoiesis by inhibiting hematopoietic cytokine signaling. Spred proteins are also regulators of Rho-mediated cell motility.

Solution in 0.01 M phoshate buffered saline, pH 7.4, 15 mM sodium azide.

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