ERBB2

Head and neck squamous cell carcinoma is quite common in the U.S., covering more than 4% of all cancers each year, and is most susceptible to individuals between 50 and 60 years of age.  Squamous cells are a type of epithelial cell that are located all over the body with concentrations in the mouth, throat, neck and cervix.  EGFR, or epidermal growth factor receptor, is a trans-membrane glycoprotein that oversees cellular proliferation through its intrinsic tyrosine kinase activity.  When EGFR is bound to its ligand, it is phosphorylated by inner tyrosine kinase activity, where down

c-Myc, a proto-oncogene, has documented involvement in cellular differentiation, cell growth, cell death and tumor formation.  Target genes of the Myc family include those that participate in cell survival, translation, transcription, metabolism and more.  On a more specific level, c-Myc is a transcription factor that can both activate and repress its target protein by way of DNA modifications.  This allows for the use of a c-Myc antibody in two manners; it can be used to monitor the actual c-Myc protein expression levels, or, it

Proliferating cell nuclear antigen (PCNA) plays a crucial role in nucleic acid metabolism as it pertains to DNA replication and repair.  Most noted for its activation of subunits of DNA polymerase, it has also been found to interact with cell-cycle progression proteins.  Modifications of PCNA as a result of cellular response put PCNA in a pivotal position with DNA replication, DNA damage, and chromatin structure and function.  In response to DNA damage, PCNA is ubiquitinated and becomes part of the RAD-6 dependent DNA repair pathway, where it acts as a substrate with a variety of p

Beta tubulin III, also known as Tuj-1, is a class III member of the beta tubulin protein family. Beta tubulins are one of two structural components that form our microtubule network.

Ki67, also known as MKI67, is best known as the leading marker of cellular proliferation. Ki67 is regulated by a balance between synthesis and degradation, and often carries a very short half-life.  First discovered to be located to dividing cells, Ki67 has since been specifically localized to the G1, S, G2 and M phases of mitosis. Soon after, it was discovered that there was a high correlation of Ki67 alongside the p53 (tumor suppressing protein 53), suggesting an implication in cancer. What’s more, the expression of Ki67 is higher in malignant cells versus control cells.