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Human Aspartyl (Asparaginyl) β-Hydroxylase (HAAH) is a cancer biomarker.

HAAH is an enzyme that catalyzes a protein modification, the β-hydroxylation of aspartyl and/or asparaginyl residues found in epidermal growth factor (EGF) -like domains of blood clotting factors, proteins of the extracellular matrix and various cellular signaling proteins. Despite the large number and extensive distribution of protein substrates for HAAH, it has been demonstrated that HAAH is not necessary for normal cellular function. Generally, HAAH is expressed at very low levels and is resident in the endoplasmic reticulum of the cell. HAAH has been established as an excellent biomarker for cancer diagnosis based on its biochemical and cellular properties, and known biological function:

• HAAH over-expression has been identified in more than 20 different types of cancer. HAAH is not detected to an appreciable extent in normal tissues including non-cancerous (benign) proliferative disorders.

• Over-expression of HAAH is sufficient to cause cancer. When HAAH overexpressing cells are injected into a mouse, they form tumors.

• Loss of HAAH function is not detrimental to normal cellular function; requirement for its activity is restricted to trophoblastic cells and malignancies.

• In tumor cells HAAH over-expression results in its relocalization from an internal cellular compartment to the cell surface. Tissue staining for HAAH is both diagnostic and prognostic for cancer.

• The HAAH protein has been identified in the serum of cancer patients. The protein is undetectable in sera from non-diseased individuals and thus elevated serum protein levels of HAAH are diagnostic for cancer.

• Over expression of HAAH can also be detected at the mRNA level in cancer cells; therefore qRT-PCR may be useful in diagnosing and monitoring cancer.