• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to induce ERK1/ERK2 phosphorylation in Jurkat human acute T cell leukemia cells. 5-15 μg/mL of Recombinant Human TFF1 can effectively induce ERK1/2 phosphorylation.

• Source

  Chinese Hamster Ovary cell line, CHO-derived Glu25-Phe84 with a C-terminal 6-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Glu25

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  7.5 kDa

• SDS-PAGE

  12-15 kDa, reducing conditions

Background: TFF1

Trefoil Factor 1 (TFF1), also known as pS2, is one of three structurally related secreted proteins that contain trefoil domains. These domains adopt a three-leaved conformation held together by conserved intrachain disulfide bonds. TFF1 is an approximately 7 kDa peptide that plays an important role in epithelial regeneration and wound healing (1). Mature human TFF1 shares 67% amino acid sequence identity with mouse and rat TFF1. It is expressed by goblet cells of the gastric and intestinal mucosa and by conjunctival goblet cells (2-5). TFF1 is a copper-binding protein that can form disulfide-linked homodimers, associate into disulfide-linked complexes with Gastrokine 2, and form non-covalent complexes with the mucin MUC5AC (4, 6-8). Copper enhances TFF1 homodimerization as well as its ability to promote epithelial cell motility, wound healing, and the colonization of   H. pylori in stomach and colon epithelia (9, 10). TFF1 is down-regulated during the progression from gastritis to gastric dysplasia to gastric cancer, although it is up-regulated in breast and prostate cancers (11-13). TFF1 inhibits the formation of calcium oxalate crystals, and its excretion in the urine is reduced in patients with kidney stones (14).

• References:

1. Kjellev, S. (2009) Cell. Mol. Life Sci. 66:1350.

2. Madsen, J. et al. (2007) J. Histochem. Cytochem. 55:505.

3. Rio, M.C. et al. (1988) Science 241:705.

4. Newton, J.L. et al. (2000) Gut 46:312.

5. Langer, G. et al. (1999) Invest. Opthalmol. Visual Sci. 40:2220.

6. Chadwick, M.P. et al. (1997) Biochem. Biophys. Res. Commun. 327:117.

7. Westley, B.R. et al. (2005) Biochemistry 44:7967.

8. Ruchaud-Sparagano, M.H. et al. (2004) Cell. Mol. Life Sci. 61:1946.

9. Tosco, A. et al. (2010) Cell. Mol. Life Sci. 67:1943.

10. Montefusco, S. et al. (2013) PLoS ONE 8:e79455.

11. Soutto, M. et al. (2011) J. Clin. Invest. 121:1753.

12. Kida, N. et al. (1989) Cancer Res. 49:3494.

13. Vestergaard, E.M. et al. (2006) Clin. Cancer Res. 12:807.

14. Chutipongtanate, S. et al. (2005) J. Clin. Invest. 115:3613.

• Long Name:

  Trefoil Factor 1

• Entrez Gene IDs:

  7031 (Human); 100041004 (Mouse); 117270 (Rat)

• Alternate Names:

  BCEI; BCEIbreast cancer, estrogen-inducible sequence expressed in; Breast cancer estrogen-inducible protein; breast cancer estrogen-inducible sequence; D21S21; gastrointestinal trefoil protein pS2; hP1.A; HPS2; PNR-2; Polypeptide P1.A; Protein pS2; PS2; TFF1; trefoil factor 1; trefoil factor, BCE1, human pS2 induced by estrogen from human breast cancercell line M10HP1.A