Technical Data
A4001-35C
ATP-Citrate Lyase, phosphorylated (Ser455) (ACL, ATP Citrate (pro-S) Lyase, ATP Citrate Synthase, Citrate Cleavage Enzyme, EC 2.3.3.8)
Description:
ATP citrate lyase (ACL) is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer of four identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. One of these products, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. NDPK has been found to phosphorylate ACL and insulin to increase phosphorylation of ACL (2).

Applications:
Suitable for use in Western Blotting, Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Western Blot: 1:5000
Immunoprecipitation: 1:20
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
TypeIsotypeCloneGrade
MabIgG9E152Supernatant
SizeStorageShippingSourceHost
100ul-20°CBlue IceHumanRabbit
Concentration:
Not determined
Immunogen:
A synthetic phosphopeptide corresponding to residues surrounding S455 of human ATP citrate lyase
Purity:
Supernatant
Form
Supplied as a liquid in 50mM Tris-glycine, pH 7.4, 0.15M sodium chloride, 40% glycerol, 0.01% sodium azide, 0.05% BSA.
Specificity:
Recognizes human ATP-Citrate Lyase when phosphorylated at Ser455.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Elshourbagy et al. Europ. J. Biochem. 204: 491-499, 1992. 2. Benjamin, W. B., and Singer, I. (1974) Biochim. Biophys. Acta 251, 28-422.