Mouse Anti-ANXA1 Recombinant Antibody (CBYC-A624) (CBMAB-A2885-YC)

Annexin A1

ANXA1 is a membrane-localized protein that binds phospholipids. This protein inhibits phospholipase A2 and has anti-inflammatory activity. Loss of function or expression of this gene has been detected in multiple tumors.

Annexin A1; Phospholipase A2 Inhibitory Protein; Chromobindin-9; Calpactin II; Calpactin-2; Annexin-1; ANX1;

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 (By similarity). 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 Ca2+ and can bind up to eight Ca2+ ions (By similarity). Displays Ca2+-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 Ca2+-dependent interaction between phagosomes and the actin cytoskeleton (By similarity).

Actin cytoskeleton reorganization Source: UniProtKB
Adaptive immune response Source: UniProtKB-KW
Alpha-beta T cell differentiation Source: BHF-UCL
Arachidonic acid secretion Source: GO_Central
Cell surface receptor signaling pathway Source: GO_Central
Cellular response to glucocorticoid stimulus Source: BHF-UCL
Cellular response to hydrogen peroxide Source: GO_Central
Cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
Cytokine-mediated signaling pathway Source: Reactome
DNA duplex unwinding Source: GO_Central
Endocrine pancreas development Source: GO_Central
Gliogenesis Source: GO_Central
G protein-coupled receptor signaling pathway Source: Reactome
G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: UniProtKB
Granulocyte chemotaxis Source: UniProtKB
Hepatocyte differentiation Source: GO_Central
Inflammatory response Source: UniProtKB
Innate immune response Source: UniProtKB-KW
Insulin secretion Source: GO_Central
Keratinocyte differentiation Source: UniProtKB
Monocyte chemotaxis Source: UniProtKB
Myoblast migration involved in skeletal muscle regeneration Source: GO_Central
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of exocytosis Source: UniProtKB
Negative regulation of interleukin-8 production Source: BHF-UCL
Negative regulation of phospholipase A2 activity Source: GO_Central
Negative regulation of protein secretion Source: Ensembl
Negative regulation of T-helper 2 cell differentiation Source: UniProtKB
Neutrophil clearance Source: BHF-UCL
Neutrophil homeostasis Source: BHF-UCL
Peptide cross-linking Source: UniProtKB
Phagocytosis Source: UniProtKB
Positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
Positive regulation of G1/S transition of mitotic cell cycle Source: GO_Central
Positive regulation of interleukin-2 production Source: UniProtKB
Positive regulation of neutrophil apoptotic process Source: GO_Central
Positive regulation of prostaglandin biosynthetic process Source: GO_Central
Positive regulation of T cell proliferation Source: UniProtKB
Positive regulation of T-helper 1 cell differentiation Source: UniProtKB
Positive regulation of vesicle fusion Source: UniProtKB
Positive regulation of wound healing Source: UniProtKB
Prolactin secretion Source: GO_Central
Prostate gland development Source: GO_Central
Regulation of cell shape Source: UniProtKB
Regulation of hormone secretion Source: UniProtKB
Regulation of inflammatory response Source: UniProtKB
Regulation of interleukin-1 production Source: UniProtKB
Regulation of leukocyte migration Source: UniProtKB
Response to drug Source: GO_Central
Response to estradiol Source: GO_Central
Response to interleukin-1 Source: GO_Central
Response to peptide hormone Source: GO_Central
Response to X-ray Source: GO_Central
Signal transduction Source: UniProtKB

Secreted; Extracellular space; Extracellular exosome; Endosome membrane; Early endosome; Cytoplasm; Nucleus; Cell membrane; Basolateral cell membrane; Apical cell membrane; Lateral cell membrane; Cell membrane; Cilium; Secretory vesicle lumen; Phagocytic cup; Cytoplasmic vesicle membrane. Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles (PubMed:25664854). Alternatively, the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in the protein translocation from the cytoplasm into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). Detected in gelatinase granules in resting neutrophils (PubMed:10772777). Secretion is increased in response to wounding and inflammation (PubMed:25664854). Secretion is increased upon T-cell activation (PubMed:17008549). Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect (PubMed:10772777). Colocalizes with actin fibers at phagocytic cups (By similarity). Displays calcium-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678).

Phosphorylated by protein kinase C, EGFR and TRPM7 (PubMed:2457390, PubMed:15485879). Phosphorylated in response to EGF treatment (PubMed:2532504).
Sumoylated.