Anti-Acid phosphatase/ACP5 Antibody Picoband® Fluoro488 Conjugated

Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals. This gene encodes an iron containing glycoprotein which catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. It is the most basic of the acid phosphatases and is the only form not inhibited by L (+) -tartrate.

Expressed ubiquitously. Expression is highest in heart, skeletal muscle, kidney and liver, intermediate in brain, non-mucosal colon, spleen and placenta, and lowest in small intestine, thymus, lung and peripheral blood leukocytes.

Cancer, Cancer Metabolism, Energy Metabolism, Energy Transfer Pathways, Integration Of Energy, Integration Of Energy Metabolism, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Pathways and Processes, Signal Transduction

May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly (A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly (A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA.

1. Allen, B. S., Ketcham, C. M., Roberts, R. M., Nick, H. S., Ostrer, H. Localization of the human type 5, tartrate-resistant acid phosphatase gene by in situ hybridization. Genomics 4: 597-600, 1989. 2. Bilginer, Y., Duzova, A., Topaloglu, R., Batu, E. D., Boduroglu, K., Gucer, S., Bodur, I., Alanay, Y. Three cases of spondyloenchondrodysplasia (SPENCD) with systemic lupus erythematosus: a case series and review of the literature. Lupus 25: 760-765, 2016. 3. Briggs, T. A., Rice, G. I., Adib, N., Ades, L., Barete, S., Baskar, K., Baudouin, V., Cebeci, A. N., Clapuyt, P., Coman, D., De Somer, L., Finezilber, Y., and 19 others. Spondyloenchondrodysplasia due to mutations in ACP5: a comprehensive survey. J. Clin. Immun. 36: 220-234, 2016. Note: Erratum: J. Clin. Immun. 36: 529-530, 2016.