Product Pathways - Ca / cAMP / Lipid Signaling
Annexin A2 (D11G2) Rabbit mAb #8235
|W IHC-P IF-IC F||H M R Mk B Pg (Dg) (Hr)||Endogenous||38||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey B=Bovine Dg=Dog Pg=Pig Hr=Horse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Annexin A2 (D11G2) Rabbit mAb recognizes endogenous levels of total annexin A2 protein. This antibody is not known or predicted to cross-react with other annexin family members.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Phe307 of human annexin A2 protein.
Western blot analysis of extracts from various cell lines using Annexin A2 (D11G2) Rabbit mAb (upper) and GAPDH (14C10) Rabbit mAb #2118 (lower).
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Annexin A2 (D11G2) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human lung carcinoma using Annexin A2 (D11G2) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded mouse kidney using Annexin A2 (D11G2) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded MCF7 (left) or LNCaP (right) cell pellets using Annexin A2 (D11G2) Rabbit mAb.
Flow cytometric analysis of HL-60 (blue) and K-562 (green) cells using Annexin A2 (D11G2) Rabbit mAb.
Annexin A2 (ANXA2), also known as lipocortin II or calpactin-1 heavy chain, is a 36 kDa member of the annexin superfamily that binds phospholipids and other proteins in a calcium-dependent manner via annexin repeats (1). Annexin A2 contains four such repeats through which it mediates protein-protein and protein-lipid interactions (1-4). It forms a constitutive heterotetramer with S100A10, acting as a bridge between the actin cytoskeleton, plasma membrane, and endocytotic vesicle machinery (5-7). Originally identified as a protein inhibitor of phospholipase A2, annexin A2 has subsequently been shown to interact with an array of protein and non-protein partners, including F-actin, spectrin, SNARE complexes, RNA, and virus particles (4,6,8,9). Annexin A2 has also been shown to have receptor-like activity and is detected on the surface of macrophages and vascular endothelial cells where it mediates macrophage activation and Factor Xa signaling, respectively (10-13). Upregulation of annexin A2 at the cell surface is thought to be modulated by phosphorylation at Tyr23 by Src (14-18). Interestingly, phosphorylation at Tyr23 has recently been shown to be required for cell surface expression of annexin A2 where it mediates motility, invasiveness, and overall metastatic potential of certain pancreatic cancer cells (19,20). Annexin A2 has also been shown to be heavily phosphorylated on serine residues in response to PKC activation via a pleiotropic mechanism (21-23). For a complete list of curated phosphorylation sites on annexin A2, please see PhosphoSitePlus® at www.phosphosite.org.
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For Research Use Only. Not For Use In Diagnostic Procedures.