Technical Data
AcCoA Carboxylase 1 (ACC-1, Acetyl Coenzyme A Carboxylase 1)
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:
Western Blot: 1:1000-1:5000
ELISA: 1:10,000-1:100,000 using 50-100ng of control peptide/well.
Optimal dilutions to be determined by the researcher.

Recommended Control Peptide:
A0225-01: AcCoA Carboxylase 1, Human, Control Peptide (ACC-1)

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 at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
50ul-20CBlue IceHumanRabbit
Not determined
Synthetic peptide 15aa sequence mapping near the N-terminus of Human ACC-1 (KLH). Species Sequence Homology: mouse, rat, porcine, bovine, sheep: 100%; chicken: 86%.
Supplied as a liquid in 0.05% sodium azide.
Recognizes human Acetyl-CoA Carboxylase-1 (ACC-1). No significant sequence homology is seen with ACC-2 or any other protein.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Munday, M.R., et al., (1988) Eur. J. Biochem. 175: 331. 2. Abu-Elheiga, et al., (2000) PNAS 97: 1444. 3. Lee, et al., (2001) J. Biol. Chem. 276: 2,576. 3. Abu-Elheiga, et al., (1997) J. Biol. Chem. 272: 10,699. 4. Hoppel, et al., (2001) ABB 392: 321. 5. Fraser & Zammit, (1998) Biochem. J. 329: 225. 6. Stapleton, et al., (1996) J. Biol. Chem. 271: 611. 7. Mitchelhill, et al., (1997) J. Biol. Chem. 272: 24