Mouse ANXA1 Protein 3742

Additional Information:
accession P10107|express systemE.coli|product tagC-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundAtherosclerosis, characterized by the formation of fat-laden plaques, is a chronic inflammatory disease. ABCA1 promotes cholesterol efflux, reduces cellular cholesterol accumulation, and regulates anti-inflammatory activities in an apoA-I- or ANXA1-dependent manner. The latter activity occurs by mediating the efflux of ANXA1, which plays a critical role in anti-inflammatory effects, cholesterol transport, exosome and microparticle secretion, and apoptotic cell clearance.|molecular weightThe protein has a predicted MW of 39.6 kDa same as Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Mouse ANXA1 Protein 3742proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceAtherosclerosis, characterized by the formation of fat-laden plaques, is a chronic inflammatory disease. ABCA1 promotes cholesterol efflux, reduces cellular cholesterol accumulation, and regulates anti-inflammatory activities in an apoA-I- or ANXA1-dependent manner. The latter activity occurs by mediating the efflux of ANXA1, which plays a critical role in anti-inflammatory effects, cholesterol transport, exosome and microparticle secretion, and apoptotic cell clearance.Protein namesAnnexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) [Cleaved into: Annexin Ac2-26]Gene namesAnxa1,Anxa1 Anx1 Lpc-1 Lpc1Protein familyAnnexin familyMass10090DaFunctionPlays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:12475898). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (PubMed:12475898). 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:17948261). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17948261). Has no effect on unstimulated T-cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (By similarity). Plays a role in the formation of phagocytic cups and phagosomes (PubMed:21245195). Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (PubMed:21245195).; [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2.Catalytic activityBINDING 59; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”1″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 60; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”1″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 62; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”1″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 97; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 100; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 105; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 127; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”3″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 129; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”3″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 131; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”3″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 132; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”4″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 134; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”4″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 171; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”3″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 210; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”5″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 213; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”5″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 215; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”5″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 253; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”6″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 255; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”5″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 256; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”6″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 261; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”6″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 286; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”7″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 288; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”7″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 290; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”7″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 328; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”8″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 330; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”7″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 331; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”8″; /evidence=”ECO:0000250|UniProtKB:P19619″; BINDING 336; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”8″; /evidence=”ECO:0000250|UniProtKB:P19619″Subellular locationNucleus. Cytoplasm. Cell projection, cilium. Basolateral cell membrane. Lateral cell membrane. Cell membrane ; Peripheral membrane protein. Apical cell membrane. Membrane ; Peripheral membrane protein. Early endosome. Cytoplasmic vesicle membrane ; Peripheral membrane protein. Endosome membrane ; Peripheral membrane protein. Secreted. Secreted, extracellular space. Cell membrane ; Peripheral membrane protein ; Extracellular side. Secreted, extracellular exosome. Cytoplasmic vesicle, secretory vesicle lumen. Cell projection, phagocytic cup. Note=Colocalizes with actin fibers at phagocytic cups (PubMed:21245195). Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles (PubMed:25664854). Secretion is increased in response to wounding and inflammation (PubMed:25664854). Detected in gelatinase granules in resting neutrophils. Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect. Displays calcium-dependent binding to phospholipid membranes (By similarity).TissuesDetected in lung (PubMed:12475898, PubMed:17384087). Detected at the apical membrane of airway epithelial cells (PubMed:17384087). Detected in intestinal epithelial cells (PubMed:18802107). Detected in skeletal muscle (PubMed:14506282). Detected in prostate (PubMed:23727357). Detected in thymus (at protein level) (PubMed:12475898). Detected in stomach, lung, spleen, ovary and uterus, and at lower levels in kidney, thymus and heart (PubMed:12475898).StructureHomodimer; non-covalently linked (By similarity). Homodimer; linked by transglutamylation. Homodimers linked by transglutamylation are observed in placenta, but not in other tissues. Interacts with S100A11. Heterotetramer, formed by two molecules each of S100A11 and ANXA1 (By similarity). Interacts with DYSF (PubMed:14506282). Interacts with EGFR (By similarity).Post-translational modificationPhosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment.; Sumoylated.; Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26.DomainThTarget Relevance information above includes information from UniProt accession: P10107The UniProt Consortium|