Technical Data
AcCoA Carboxylase 2 (ACC-2, Acetyl Coenzyme A Carboxylase 2)
In cells, excess of metabolic fuel is converted into fatty acids in cytosol and oxidized later in mitochondria to generate ATP and acetyl-CoA. In fatty acid synthesis, catalytic formation of malonyl-CoA (precursor for long-chain fatty acyl-CoA, LCFA-CoA) from acetyl-CoA by Acetyl-CoA carboxylase (ACC-1) is the rate limiting step. The translocation of LCFA-CoA from cytosol to mitochondria is catalyzed by two carnitine palmitoyl transferases (CPT-1 & CPT-2) and regulated by ACC-2, the rate limiting step of mitochondrial fatty acid b-oxidation. Activities of ACC-1 and -2 are regulated by their phosphorylation by 5'-AMP-activated protein kinase (AMPK). Diabetes deranges AMPK master-switch and represses the ACC-1 gene-expression and stimulates excessive fatty acid oxidation which in turn interferes with glucose metabolism.

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilution:
ELISA: 1:10,000-1:100,000 using 50-100ng of A0225-03B per well
Western Blot: 1-10ug/ml using ECL.
Optimal dilutions to be determined by the researcher.

Recommended Control Peptide:
A0225-03B: AcCoA Carboxylase 2, Control Peptide, Rat

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
50ug-20CBlue IceRatRabbit
Synthetic peptide consisting of 20aa sequence near the N-terminus of rat ACC-2, KLH conjugated. Species Sequence Homology: mouse, 75%; human, 60%.
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, 0.1% BSA, 0.05% sodium azide.
Recognizes rat AcCoA Carboxylase 2. No significant sequence homology is seen with ACC-1 or any other protein.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
US Biological Application References: 1. Siddiqui, S.M.K., et al., Nutrition Reserarch 28: 783-790 (2008). General References: 1. Abe, K., et al., BBA 1398: 347-352 (1998). 2. Widemer, J., et al., Biochem. J. 316: 915-922 (1997). 3. Abu-Elheiga, et al., J. Biol. Chem. 272: 10,699 (1997). 4. Abu-Elheiga, et al., PNAS 97: 1444 (2000). 5. Lee, et al., J. Biol. Chem. 276: 2576 (2001). 6. Hoppel, et al., ABB 392: 321 (2001). 7. Fraser & Zammit, Biochem. J. 329: 225 (1998). 8. Stapleton, et al., J. Biol. Chem. 271: 611 (1996). 9. Mitchelhill, et al., J. Biol. Chem. 272: 24,475 (1997).