Anti-Annexin A1, clone ANXA1/3727

1 mg/ml in 1X PBS, BSA free, sodium azide free. The ANXA1 gene belongs to the annexin family, and contains 4 annexin repeats. A pair of annexin repeats may form one binding site for calcium and a phospholipid. ANXA1 promotes membrane fusion and is involved in exocytosis. The gene for ANXA1 is upregulated in hairy cell leukemia (HCL), and its protein expression is specific for HCL. Detection of ANXA1 provides a simple, highly sensitive and specific assay for diagnosing HCL. Annexin A1 has also been found to be protective against DNA damage induced by heat in breast cancer cells, suggesting it is involved in tumor suppressive and protective activities, and also is associated with treatment resistance. Protein function: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Promotes resolution of inflammation and wound healing (PubMed:25664854). Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades (PubMed:15187149, PubMed:25664854). Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (PubMed:15187149). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T- cells (PubMed:17008549). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration (PubMed:15187149). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions. Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton. [The UniProt Consortium]