Anti-ACACA Antibody Picoband®, Dylight550 Conjugate

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.

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.

Western blot, 0.25-0.5 μg/ml, Human<br> Immunocytochemistry/Immunofluorescence, 5 μg/ml, Human<br> Flow Cytometry (Fixed), 1-3 μg/1x10⁶ cells, Human<br> ELISA, 0.1-0.5 μg/ml, -<br>