Anti-S100A10 mAb

  • Applications
    • ELISA
    • WB
  • Target S100A10
  • Host Species Mouse
  • Species Reactivities Human
  • Code # CY-M1036
  • Size 100 μg
  • Price
    $401.02
Specifications

Background

S100A10, a member of the S100 family of Ca2+-binding proteins, is a dimeric protein composed of two 11-kDa subunits. The protein is cytosolic when present as a dimer. Typically, S100A10 is found in most cells bound to annexin A2 as the heterotetrameric (S100A10)2-(annexin A2)2 complex, AIIt, in a calcium-independent manner (1). The formation of AIIt results in the translocation of S100A10 to the plasma membrane (2-4). S100A10 has been shown to regulate plasma membrane ion channels (5, 6) as well as cytosolic phospholipase A2 (7). In addition to an intracellular distribution, it has also been established that the heterotetrameric form of S100A10 is present on the extracellular surface of many cells (8–14). Extracellularly, the S100A10 subunit functions as a plasminogen receptor (15, 16). The penultimate and ultimate carboxyl-terminal lysines of this subunit bind tPA and plasminogen (17) and regulate the stimulation of tPA-dependent plasminogen activation (18).
  • Antibody Type:
    Monoclonal
  • Application:
    ELISA, WB
  • Clone Number:
    YK-1B12
  • Concentration:
    1.0 mg/mL
  • Conjugate:
    Unlabeled
  • Description:

    Monoclonal Antibody of 100 μg targeting S100A10 for ELISA, WB.

  • Formulation:
    Supplied in 20mM phosphatase buffer (pH 7.5), 300mM NaCl, 50% glycerol.
  • Host Species:
    Mouse
  • Immunogen:
    Recombinant human S100A10
  • Isotype:
    IgG1
  • Product Type:
    Antibody
  • Research Area:
    Cell Biology
  • Short Description:

    Anti-S100A10 Monoclonal Antibody.

  • Size:
    100 μg
  • Species Reactivity:
    Human
  • Storage Temperature:
    -20°C
  • Target:
    S100A10
References
  1. Donato, R. (2001) Int. J. Biochem. Cell Biol. 33, 637–668
  2. Gerke, V., and Moss, S. E. (2002) Physiol. Rev. 82, 331–371
  3. Donato, R., and Russo-Marie, F. (1999) Cell Calcium 26, 85–89
  4. Seaton, B. A., and Dedman, J. R. (1998) Biometals 11, 399–404
  5. Girard, C. et al. (2002) EMBO J. 21, 4439–4448
  6. Okuse, K. et al. (2002) Nature 417, 653–656
  7. Wu, T. et al. (1997) J. Biol. Chem. 272, 17145–17153
  8. Yeatman, T. J. et al. (1993) Clin. Exp. Metastasis 11, 37–44
  9. Tressler, R. J. et al. (1993) J. Cell. Biochem. 53, 265–276
  10. Balch, C., and Dedman, J. R. (1997) Exp. Cell Res. 237, 259–263
  11. Siever, D. A., and Erickson, H. P. (1997) Int. J. Biochem. Cell Biol. 29, 1219–1223
  12. Falcone, D. J. et al. (2001) Blood 97, 777–784
  13. Kassam, G. et al. (1998) J. Biol. Chem. 273, 4790–4799
  14. Mai, J. et al. (2000) J. Biol. Chem. 275, 12806–12812
  15. Kassam, G. et al. (1998) Biochemistry 37, 16958–16966
  16. Choi, K. S. et al. (2003) FASEB J. 17, 235–246
  17. MacLeod, T. J. et al. (2003) J. Biol. Chem. 278, 25577–25584
  18. Fogg, D. K et al. (2002) Biochemistry 41, 4953–4961