BAAT Blocking Peptide (N-Term)
€293.00
In stock
SKU
AC-BP22054a
Background:
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.
Other Names: Bile acid-CoA:amino acid N-acyltransferase, BACAT, BAT, 2.3.1.65, Glycine N-choloyltransferase, Long-chain fatty-acyl-CoA hydrolase, 3.1.2.2, BAAT
Target/Specificity:
The synthetic peptide sequence is selected from aa 83-95 of HUMAN BAAT
Type: Synthetic peptide
Primary Accession: Q14032
Gene ID: 570
Gene Name: BAAT
Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
Bio References:
Falany C.N.,et al.J. Biol. Chem. 269:19375-19379(1994).
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Humphray S.J.,et al.Nature 429:369-374(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Johnson M.R.,et al.J. Biol. Chem. 266:10227-10233(1991).
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.
Other Names: Bile acid-CoA:amino acid N-acyltransferase, BACAT, BAT, 2.3.1.65, Glycine N-choloyltransferase, Long-chain fatty-acyl-CoA hydrolase, 3.1.2.2, BAAT
Target/Specificity:
The synthetic peptide sequence is selected from aa 83-95 of HUMAN BAAT
Type: Synthetic peptide
Primary Accession: Q14032
Gene ID: 570
Gene Name: BAAT
Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
Bio References:
Falany C.N.,et al.J. Biol. Chem. 269:19375-19379(1994).
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Humphray S.J.,et al.Nature 429:369-374(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Johnson M.R.,et al.J. Biol. Chem. 266:10227-10233(1991).
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