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Annexin 1 (ANXA - 1, Ac 2 - 12)
Synthetic Peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q92108 |
|---|---|
| Other Accession | Q92040, P04083, P46193, Q5REL2, P51662 |
| Sequence | Ac-AMVSEFLKQAW-COOH |
| Other Names | Annexin A1, Annexin I, Annexin-1, Calpactin II, Calpactin-2, Chromobindin-9, Lipocortin I, Phospholipase A2 inhibitory protein, p35, ANXA1, ANX1 |
|---|---|
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ANXA1 |
|---|---|
| Synonyms | ANX1 |
| 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. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Promotes resolution of inflammation and wound healing (By similarity). 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 (By similarity). 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. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. 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. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). |
| Cellular Location | Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000250|UniProtKB:P10107}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Cell membrane {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10107}. Apical cell membrane {ECO:0000250|UniProtKB:P10107}. Membrane {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10107}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. Endosome membrane {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07150}. Secreted {ECO:0000250|UniProtKB:P10107}. Secreted, extracellular space {ECO:0000250|UniProtKB:P04083}. Cell membrane {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04083}; Extracellular side {ECO:0000250|UniProtKB:P04083}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10107}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:P10107}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P10107}. Note=Colocalizes with actin fibers at phagocytic cups. Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles. Secretion is increased in response to wounding and inflammation (By similarity). 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 (By similarity). 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) {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107} |
Research Areas
Citations (0)
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$ 277.78
Cat# SP2134a
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