The Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys27 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. (Shipping Cost: €200.00)

Cadherin-LI/CDH17 [E86]

LI-Cadherin (Liver-intestine cadherin), also known as Cadherin 17 (CDH17), is a member of the cadherin family. Cadherins are Ca(2+)- dependent transmembrane glycoproteins that mediate cell-cell adhesion and are important for the structural integrity of epithelia. LIcadherin and the classical E-cadherin are the predominant two cadherins in the intestinal epithelium. LI-cadherin contains seven cadherin repeats and a short cytoplasmic domain that does not interact with catenins or the actin cytoskeleton. It is involved in intestinal peptide transport. In normal tissues, the CDH17 antibody labels epithelial cells in the gastrointestinal tract and pancreatic duct, but not in kidney, liver and other tissues. In tumors, CDH17 is also specifically expressed on adenocarcinoma of the digestive system including liver cancer. Less than 1% of non-GI tract tumors showed immunoreactivity with CDH17. CDH17 is thus considered to be a useful marker for tumors derived from the digestive system. It is a sensitive marker for the identification of gastric intestinal metaplasia and well differentiated adenocarcinomas.

Cadherin-LI/CDH17 [E86]