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BAAT Antibody (N-Term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - BAAT Antibody (N-Term) AP22054a
    Anti-BAAT Antibody (N-Term) at 1:2000 dilution + rat liver lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 46 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q14032
Reactivity Rat
Host Rabbit
Clonality polyclonal
Isotype Rabbit Ig
Calculated MW 46299 Da
Additional info
Gene ID 570
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 This BAAT antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 63-95 amino acids from human BAAT.
Dilution WB~~1:2000
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsBAAT Antibody (N-Term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name BAAT
Function 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.
Cellular Location Cytoplasm.
Tissue Location Expressed in liver, gallbladder mucosa and pancreas.
Research Areas

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.

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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