Anti-ACACA Antibody Picoband® Fluoro488 Conjugated

Acetyl-CoA carboxylase 1 also known as ACC-alpha or ACCa is an enzyme that in humans is encoded by the ACACA gene. Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. Multiple alternatively spliced transcript variants divergent in the 5' sequence and encoding distinct isoforms have been found for this gene.

Widely expressed, with strongest expression in placenta (at protein level) . Secreted by synovial fibroblasts. Up- regulated in osteoarthritis and rheumatoid arthritis synovial fluids and cartilage as compared with non-arthritic (at protein level) .

Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.

1. Abu-Elheiga, L., Brinkley, W. R., Zhong, L., Chirala, S. S., Woldegiorgis, G., Wakil, S. J. The subcellular localization of acetyl-CoA carboxylase 2. Proc. Nat. Acad. Sci. 97: 1444-1449, 2000. 2. Abu-Elheiga, L., Jayakumar, A., Baldini, A., Chirala, S. S., Wakil, S. J. Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc. Nat. Acad. Sci. 92: 4011-4015, 1995. 3. Abu-Elheiga, L., Matzuk, M. M., Kordari, P., Oh, W., Shaikenov, T., Gu, Z., Wakil, S. J. Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal. Proc. Nat. Acad. Sci. 102: 12011-12016, 2005.