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Commit: f04ddd7fea9fb3592f59f61482fcb94610d25cbe
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Annexin A2 (D11G2) Rabbit mAb (PE Conjugate) #15161

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    Supporting Data

    REACTIVITY H M R Mk B Pg
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 
    • B-Bovine 
    • Pg-Pig 

    Product Information

    Product Description

    This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Annexin A2 (D11G2) Rabbit mAb #8235.

    Product Usage Information

    Application Dilution
    Flow Cytometry (Fixed/Permeabilized) 1:50

    Storage

    Supplied in PBS (pH 7.2), less than 0.1% sodium azide and 2 mg/ml BSA. Store at 4°C. Do not aliquot the antibodies. Protect from light. Do not freeze.

    Protocol

    Specificity / Sensitivity

    Annexin A2 (D11G2) Rabbit mAb (PE Conjugate) recognizes endogenous levels of total annexin A2 protein. This antibody is not known or predicted to cross-react with other annexin family members.

    Species Reactivity:

    Human, Mouse, Rat, Monkey, Bovine, Pig

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Dog, Horse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Phe307 of human annexin A2 protein.

    Background

    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.
    1. Barton, G.J. et al. (1991) Eur J Biochem 198, 749-60.
    2. Gerke, V. and Weber, K. (1985) EMBO J 4, 2917-20.
    3. Glenney, J.R. and Tack, B.F. (1985) Proc Natl Acad Sci USA 82, 7884-8.
    4. Gerke, V. and Weber, K. (1984) EMBO J 3, 227-33.
    5. Illien, F. et al. (2010) Biochim Biophys Acta 1798, 1790-6.
    6. Umbrecht-Jenck, E. et al. (2010) Traffic 11, 958-71.
    7. Jung, M.J. et al. (2010) Exp Cell Res 316, 1234-40.
    8. Filipenko, N.R. et al. (2004) J Biol Chem 279, 8723-31.
    9. Wright, J.F. et al. (1994) Biochem Biophys Res Commun 198, 983-9.
    10. Bhattacharjee, G. et al. (2008) Circ Res 102, 457-64.
    11. Pizzo, S.V. (2008) Circ Res 102, 389-91.
    12. Swisher, J.F. et al. (2007) J Leukoc Biol 82, 1174-84.
    13. Deora, A.B. et al. (2004) J Biol Chem 279, 43411-8.
    14. Huang, K.S. et al. (1986) Cell 46, 191-9.
    15. Erikson, E. et al. (1984) Mol Cell Biol 4, 77-85.
    16. Glenney, J.R. (1985) FEBS Lett 192, 79-82.
    17. Morel, E. and Gruenberg, J. (2009) J Biol Chem 284, 1604-11.
    18. de Graauw, M. et al. (2008) Mol Cell Biol 28, 1029-40.
    19. Nedjadi, T. et al. (2009) Br J Cancer 101, 1145-54.
    20. Zheng, L. et al. (2011) PLoS One 6, e19390.
    21. Gould, K.L. et al. (1986) Mol Cell Biol 6, 2738-44.
    22. Luo, W. et al. (2008) Mol Carcinog 47, 934-46.
    23. He, K.L. et al. (2011) J Biol Chem 286, 15428-39.
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    PhosphoSitePlus is a registered trademark of Cell Signaling Technology, Inc.
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