Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Fascin (55K-2) Mouse mAb (IHC Formulated) #99978

No. Size Price
99978S 100 µl ( 100 sections ) ¥3,100.00 现货查询 购买询价
99978 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
IHC-P 1:100 Human,Mouse, Endogenous Mouse IgG1

Species cross-reactivity is determined by western blot.

Applications Key: IHC-P=Immunohistochemistry (Paraffin),

Specificity / Sensitivity

Fascin (55K-2) Mouse mAb (IHC Formulated) recognizes endogenous levels of total fascin protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with fascin protein purified from HeLa cells.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded ovarian serous carcinoma using Fascin (55K-2) Mouse mAb (IHC Formulated).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded HeLa (left) and HT-29 (right) cell pellets using Fascin (55K-2) Mouse mAb (IHC Formulated).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded non-small cell lung carcinoma using Fascin (55K-2) Mouse mAb (IHC Formulated).

Background

Fascin is a monomeric, globular protein that plays a central role in regulating the structure and function of the cortical actin cytoskeleton (1). Fascin promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration (2). It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions (3), though less is known about this mechanism of action. Research studies have shown that increased fascin expression is associated with increased motility and invasiveness of neoplastic cells, including breast, colon, prostate, and esophageal squamous cell carcinomas (4-6). Fascin binds to the armadillo-repeat domain of β-catenin in vitro and in vivo, and has been shown to co-localize with β-catenin and cadherins at the leading edge of migratory cells (7).

  1. Hoelzle, M.K. and Svitkina, T. (2012) Mol Biol Cell 23, 310-23.
  2. Adams, J.C. (2004) Curr Opin Cell Biol 16, 590-6.
  3. Zanet, J. et al. (2012) J Cell Biol 197, 477-86.
  4. Hashimoto, Y. et al. (2005) Int J Biochem Cell Biol 37, 1787-804.
  5. Stewart, C.J. et al. (2012) J Clin Pathol 65, 213-7.
  6. Alam, H. et al. (2012) BMC Cancer 12, 32.
  7. Tao, Y.S. et al. (1996) J Cell Biol 134, 1271-81.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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