ACP2 Human Recombinant produced in E.Coli is a single, non-glycosylated
polypeptide chain containing 373 amino acids (31-380 a.a.) and having a
molecular mass of 42.9kDa.
ACP2 is localized to the lysosomal membrane and is chemically and genetically distinct from red cell acid phosphatase . It plays a crucial role in the lysosomal degradation pathway, where it functions optimally at an acidic pH. The enzyme catalyzes the hydrolysis of phosphate monoesters, releasing phosphate and alcohol .
The ACP2 gene is located on chromosome 11 and has several aliases, including LAP and EC 3.1.3.2 . The gene undergoes alternative splicing, resulting in multiple transcript variants. Additionally, a C-terminally extended isoform is predicted to be produced by the use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism .
ACP2 is essential for normal cellular function. Mice lacking this gene exhibit multiple defects, including bone structure alterations, lysosomal storage defects, and an increased tendency towards seizures . An enzymatically inactive allele of this gene in mice showed severe growth retardation, hair-follicle abnormalities, and an ataxia-like phenotype .
The enzyme’s activity is used as a biochemical marker in various clinical settings. For instance, different forms of acid phosphatase are found in different organs, and their serum levels are used to evaluate the success of surgical treatment for prostate cancer . In the past, acid phosphatase levels were also used to diagnose prostate cancer .