Cell Signaling Technology

Product Pathways - Adhesion

βIG-H3 Antibody #2719

Applications Reactivity MW (kDa) Source
W IP IF-IC H (Mk) 70 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

βIG-H3 Antibody detects endogenous levels of total βIG-H3 protein.

Source / Purification

Polyclonal antibodies are produced by immunzing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues near the carboxyl terminus of human βIG-H3. Antibodies were purified by peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from A549 and OVCAR8 cells, untreated or treated with TGF-β overnight, using βIG-H3 Antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of A549 cells, untreated (left) or TGF-β-treated (right), using βIG-H3 Antibody (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).

Background

βIG-H3 (TGFBI/RGD-CAP/Kerato-epithelin) is a 683-amino acid secretory protein induced by TGF-β that plays a role in cell adhesion, differentiation, and apoptosis (1-4). βIG-H3 contains an internal cysteine-rich EMI domain followed by four fasciclin-1 domains and a carboxyl terminal RGD domain (1,2). It contributes to cell adhesion through interactions with integrins as well as a number of extracellular matrix (ECM) proteins including collagen, fibronectin, and laminin (5-7). ECM βIG-H3 is found in a wide variety of tissues (8-12). Mutations in the βIG-H3 gene as well as elevated protein levels are most notably associated with corneal dystrophies (13).

  1. Skonier, J. et al. (1992) DNA Cell Biol 11, 511-22.
  2. Skonier, J. et al. (1994) DNA Cell Biol 13, 571-84.
  3. Hashimoto, K. et al. (1997) Biochim Biophys Acta 1355, 303-14.
  4. Kim, J.E. et al. (2003) Oncogene 22, 2045-53.
  5. Kim, J.E. et al. (2002) Invest Ophthalmol Vis Sci 43, 656-61.
  6. Billings, P.C. et al. (2002) J Biol Chem 277, 28003-9.
  7. Hanssen, E. et al. (2003) J Biol Chem 278, 24334-41.
  8. Gibson, M.A. et al. (1997) J Histochem Cytochem 45, 1683-96.
  9. Billings, P.C. et al. (2000) Am J Respir Cell Mol Biol 22, 352-9.
  10. Gilbert, R.E. et al. (1998) Kidney Int 54, 1052-62.
  11. Rawe, I.M. et al. (1997) Invest Ophthalmol Vis Sci 38, 893-900.
  12. LeBaron, R.G. et al. (1995) J Invest Dermatol 104, 844-9.
  13. Munier, F.L. et al. (1997) Nat Genet 15, 247-51.

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