Human/Mouse Acetyl-CoA Carboxylase alpha /ACACA Antibody Summary
Accession # Q13085
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human and Mouse Acetyl-CoA Carboxylase alpha /ACACA by Western Blot. Western blot shows lysates of A431 human epithelial carcinoma cell line, HCT-116 human colorectal carcinoma cell line, HepG2 human hepatocellular carcinoma cell line, and C2C12 mouse myoblast cell line. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human/Mouse Acetyl-CoA Carboxylase a/ACACA Monoclonal Antibody (Catalog # MAB6898) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for Acetyl-CoA Carboxylase a/ACACA at approximately 250 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Acetyl-CoA Carboxylase alpha/ACACA
ACAC-A (Acetyl-CoA carboxylase alpha/1; also ACC-1 and biotin carboxylase) is a 260-265 kDa cytoplasmic, phosphorylated biotinyl-enzyme. It is widely expressed, and found to be concentrated in hepatocytes, adipocytes and lactating mammary epithelium. It is one of two gene products (ACAC-B/beta being the other) that catalyze the formation of malonyl-CoA from acetyl-CoA. The formation of malonyl-CoA by ACAC-A is a rate-limiting step in fatty acid synthesis; malonyl-CoA formed by ACAC-B acts as a regulator of CPT-1 during fatty acidoxidation. Human ACAC-A is 2346 amino acids (aa ) in length. It contains an N-terminal acetylated Met, one ATP-Grasp domain (aa 275-466) with an embedded biotin carboxylation domain (aa 117-618), a biotinyl-binding region (aa 752-818), and a carboxyltransferase domain (aa 1698-2194). There are at least 17 utilized phosphorylation sites, and two acetylated Lys. ACAC-A exists as either a dimer or higher-order oligomer. Multiple splice variants exist. One possesses an alternative start site at Met79, a second utilizes an alternative start site 37 aa upstream of the standard site, and a third (called PIII) shows a 17 aa substitution for aa 1-75. Over aa 1185-1352, human ACAC-A shares 95% aa identity with mouse ACAC-A, and 97% aa identity with both ovine and bovine ACAC-A.
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