APEH polyclonal antibody detects endogenous levels of APEH protein.
APEH (Acyl-peptide hydrolase), also known as APH, OPH or ACPH, is a 732 amino acid cytoplasmic protein that exists as a homotetramer and functions to catalyze the hydrolysis of N-terminal acetylated amino acids from small acetylated peptides. Once hydrolyzed from the target peptide, the acetyl amino acid is further processed by an aminoacylase to produce acetate and a free amino acid. The gene encoding human APEH maps to a region on chromosome 3 that is deleted in various types of cancers, including renal cell carcinoma and small cell lung carcinoma, suggesting that APEH may be involved in tumor transformation events. Chromosome 3 is made up of about 214 million bases encoding over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci. Key tumor suppressing genes on chromosome 3 include those that encode the apoptosis mediator RASSF1, the cell migration regulator HYAL1 and the angiogenesis suppressor SEMA3B.
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