Synthesized phospho-peptide around the phosphorylation site of human Annexin A1 (phospho Tyr21)

Phospho-Annexin A1 (Y21) Polyclonal Antibody detects endogenous levels of Annexin A1 protein only when phosphorylated at Y21.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):QEyVQ

ANXA1

Annexin A1

ANXA1 ;
ANX1 ;
LPC1 ;
Annexin A1 ;
Annexin I ;
Annexin-1 ;
Calpactin II ;
Calpactin-2 ;
Chromobindin-9 ;
Lipocortin I ;
Phospholipase A2 inhibitory protein ;
p35

This gene encodes 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. [provided by RefSeq, Dec 2014],

Domain:A pair of annexin repeats may form one binding site for calcium and phospholipid.,Function:Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.,PTM:Phosphorylated by protein kinase C, epidermal growth factor receptor/kinase and TRPM7. Phosphorylation results in loss of the inhibitory activity.,similarity:Belongs to the annexin family.,similarity:Contains 1 annexin repeat.,similarity:Contains 2 annexin repeats.,similarity:Contains 4 annexin repeats.,subcellular location:Found in the cilium, nucleus and basolateral cell membrane of ciliated cells in the tracheal endothelium (By similarity). Found in the cytoplasm of type II pneumocytes and alveolar macrophages.,subunit:Homodimer in placenta (20%); linked by transglutamylation. Interacts with DYSF.,

Nucleus . Cytoplasm . Cell projection, cilium . Cell membrane . Membrane ; Peripheral membrane protein . Endosome membrane ; Peripheral membrane protein . Basolateral cell membrane . Apical cell membrane . Lateral cell membrane . Secreted . Secreted, extracellular space . Cell membrane ; Peripheral membrane protein ; Extracellular side . Secreted, extracellular exosome . Cytoplasmic vesicle, secretory vesicle lumen . Cell projection, phagocytic cup . Early endosome . Cytoplasmic vesicle membrane ; Peripheral membrane protein . 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). .

Detected in resting neutrophils (PubMed:10772777). Detected in peripheral blood T-cells (PubMed:17008549). Detected in extracellular vesicles in blood serum from patients with inflammatory bowel disease, but not in serum from healthy donors (PubMed:25664854). Detected in placenta (at protein level) (PubMed:2532504). Detected in liver.