Human ACP6 Alexa Fluor™ Plus 555-conjugated Antibody

ACP6 (Acid Phosphatase 6, lysophosphatidic; also lysophosphatidic acid phosphatase type 6, LPAP and ACPL1) is a 44-47 kDa monomeric member of the histidine acid phosphatase family of proteins. It is widely expressed, being found in almost all tissues, particularly in mitochondria-rich cells. ACP6 has been described as being both secreted and mitochondrial in location, and plays a critical role in the regulation of lysophosphatidic acid (LPA). LPA is the most structurally simple, biologically active phospholipid in nature (mono-[variable length] acyl-phosphoglycerol). It exists both inside and outside the cell, serving intracellularly as a modulator of lipid rafts, and extracellularly as a signaling molecule that promotes cell growth and fibroblast chemotaxis. ACP6 hydrolyzes LPA, generating monoacylglycerol and phosphate. This presumably eliminates its bioactivity. Human ACP6 precursor is 428 amino acids (aa) in length. It contains a putative signal sequence (aa 1-32) plus a 396 aa mature region (aa 33-428) that possesses one histidine phosphatase domain (aa 120-379). There is one isoform variant that contains an 11 aa substitution for aa 261-428. Mature human ACP6 shares 76% aa sequence identity with mouse ACP6.