|Human, Mouse, Rat|
Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting
Background: Neuropeptide Y (NPY) is a 36 amino acid peptide that belongs to the pancreatic polypeptide (PP) family, which also includes peptide YY (PYY) (1). The mature 36-residue NPY is produced from a larger pre-pro 97-residue NPY precursor through a series of cleavage reactions at dibasic sites and C-terminal amidation of the peptide product (2). NPY is widely expressed in the central nervous system (3) and exerts its action through stimulation of 5 different receptors (Y1-Y5) that belong to the G protein-coupled receptor family (4). NPY in the hypothalamus exhibits orexigenic activity through activation of Y1 and Y5 receptors (5). NPY is involved in the control of bone homeostasis, through the regulation of osteoblast activity by Y1 and Y2 receptors (6), and the regulation of testosterone secretion by activating Y1 receptor in testicular vessels (7). Research studies suggest that modulation of NPY activity and signaling represents a potential strategy for the development of appetite control and antiobesity agents (8).
|Human, Monkey, Mouse, Rat|
Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting
Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).