Product: ANXA1 Antibody
Catalog: BF0046
Description: Mouse monoclonal antibody to ANXA1
Application: WB IHC ELISA
Reactivity: Human, Mouse, Monkey
Mol.Wt.: 38.7kDa; 39kD(Calculated).
Uniprot: P04083
RRID: AB_2834047

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Product Info

ELISA 1:10000, WB 1:500-1:2000, IHC 1:200-1:1000
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Monoclonal [AFB2025]
ANXA1 antibody detects endogenous levels of total ANXA1.
Cite Format: Affinity Biosciences Cat# BF0046, RRID:AB_2834047.
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


Annexin 1; Annexin A1; Annexin I (lipocortin I); Annexin I; Annexin-1; AnnexinA1; AnnexinI; ANX 1; ANX A1; ANX1; ANXA 1; ANXA1; ANXA1 protein; ANXA1_HUMAN; Calpactin 2; Calpactin II; Calpactin-2; CalpactinII; Chromobindin 9; Chromobindin-9; Chromobindin9; HGNC:533; Lipocortin 1; Lipocortin I; Lipocortin1; LipocortinI; LPC 1; LPC1; p35; Phospholipase A2 inhibitory protein;



Purified recombinant fragment of human ANXA1 expressed in E. Coli.


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.

Annexin I belongs to a family of Ca(2+)-dependent phospholipid binding proteins which have a molecular weight of approximately 35,000 to 40,000 and are preferentially located on the cytosolic face of the plasma membrane. Annexin I protein has an apparent relative molecular mass of 40 kDa, with phospholipase A2 inhibitory activity.

PTMs - P04083 As Substrate

Site PTM Type Enzyme
A2 Acetylation
S5 Phosphorylation Q96QT4 (TRPM7)
Y21 Phosphorylation P00519 (ABL1) , P12931 (SRC) , A0A173G4P4 (Abl fusion) , P00533 (EGFR)
T24 Phosphorylation
K26 Ubiquitination
S27 Phosphorylation P41743 (PRKCI) , P05129 (PRKCG) , P05771 (PRKCB) , P24723 (PRKCH) , P17252 (PRKCA)
S28 Phosphorylation P17252 (PRKCA) , P05771 (PRKCB)
K29 Ubiquitination
S34 Phosphorylation
S37 O-Glycosylation
S37 Phosphorylation
Y39 Phosphorylation
T41 Phosphorylation
S45 Phosphorylation
K53 Acetylation
K53 Ubiquitination
K58 Ubiquitination
T64 Phosphorylation
T70 Phosphorylation
K71 Acetylation
K71 Ubiquitination
K81 Ubiquitination
Y84 Phosphorylation
T88 Phosphorylation
K90 Acetylation
K90 Ubiquitination
T95 Phosphorylation
K97 Acetylation
K97 Ubiquitination
K98 Acetylation
K98 Ubiquitination
T101 Phosphorylation
K113 Ubiquitination
T114 Phosphorylation
K128 Ubiquitination
T132 Phosphorylation
T136 Phosphorylation
S143 Phosphorylation
K161 Acetylation
K161 Ubiquitination
K166 Acetylation
K166 Ubiquitination
T169 Phosphorylation
S170 Phosphorylation
T172 Phosphorylation
S173 Phosphorylation
S182 Phosphorylation
K185 Acetylation
K185 Ubiquitination
S189 Phosphorylation
S201 Phosphorylation
Y207 Phosphorylation
K214 Sumoylation
K214 Ubiquitination
T216 Phosphorylation P17612 (PRKACA) , P12931 (SRC)
T226 Phosphorylation
K239 Acetylation
K239 Ubiquitination
K245 Acetylation
K250 Acetylation
K250 Ubiquitination
K257 Ubiquitination
K274 Methylation
K274 Ubiquitination
K281 Acetylation
K281 Methylation
K281 Ubiquitination
K287 Ubiquitination
K294 Acetylation
K312 Acetylation
K312 Sumoylation
K312 Ubiquitination
K317 Ubiquitination
C324 S-Nitrosylation
K332 Sumoylation
K332 Ubiquitination
Y335 Phosphorylation
K337 Ubiquitination
C343 S-Nitrosylation

Research Backgrounds


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 (By similarity). Promotes resolution of inflammation and wound healing. 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. 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. 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. 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. 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).


Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment.


Subcellular Location:

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.
Note: Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles (PubMed:25664854). 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).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

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

Subunit Structure:

Homodimer; 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. Interacts with DYSF (By similarity). Interacts with EGFR (By similarity).


The full-length protein can bind eight Ca(2+) ions via the annexin repeats. Calcium binding causes a major conformation change that modifies dimer contacts and leads to surface exposure of the N-terminal phosphorylation sites; in the absence of Ca(2+), these sites are buried in the interior of the protein core. The N-terminal region becomes disordered in response to calcium-binding.

The N-terminal 26 amino acids are sufficient for its extracellular functions in the regulation of inflammation and wound healing (PubMed:25664854). Acylated peptides that contain the first 26 amino acids of the mature protein can activate signaling via the formyl peptide receptors (PubMed:15187149, PubMed:25664854).

Belongs to the annexin family.

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