Anti-EMAP II

0.5 mg/ml with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. EMAP II (Endothelial monocyte-activating polypeptide 2) is a pro-inflammatory cytokine and participant in apoptotic cell death. It is synthesized as a precursor (pro-EMAP II), lacking a secretion signal peptide. In apoptotic cells, the ~34 kDa pro-form of EMAP II is cleaved by Caspase-7 (and Caspase-3 to a lesser extent) at aspartate 144 to its mature, ~20 kDa form. The mature form of EMAP II has been found to have many different functions. In vivo, it recruits leukocytes to the site of apoptotic cell death. In vitro it has been shown to activate endothelial cells (and the release of von Willebrand factor, E-selectin and P-selectin), neutrophils, and induces macrophage expression of TNFa and TF (tissue factor). EMAP II is also a possible biomarker for brain injury, having been found to be differentially expressed in two types: traumatic injury shows an increase and ischemic injury shows a decrease in EMAP II expression (Dave, et al, 2014). Protein function: Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7. [The UniProt Consortium]