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Mouse Anti-BAAT Recombinant Antibody (CBYY-0105) (CBMAB-0105-YY)

This product is mouse antibody that recognizes BAAT. The antibody CBYY-0105 can be used for immunoassay techniques such as: ELISA, WB
See all BAAT antibodies
Published Data
Mouse Anti-BAAT Recombinant Antibody (CBYY-0105) in Immunoblot
Immunoblot analyses of liver extracts from control mice and mice subjected to sepsis by PCI (a) and quantitation of phospho-Akt (pAkt)/Akt levels normalised to sham control (b). ...View More
Beer, A. J., Hertz, D., Seemann, E., Beretta, M., Westermann, M., Bauer, R., ... & Qualmann, B. (2020). Reduced Mrp2 surface availability as PI3Kγ-mediated hepatocytic dysfunction reflecting a hallmark of cholestasis in sepsis. Scientific Reports, 10(1), 13110.

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-0105
Antibody Isotype
IgG1, κ
Application
ELISA, WB, IP

Basic Information

Immunogen
Recombinant BAAT of human origin.
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
ELISA1:100-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
N-terminus

Target

Full Name
bile acid Coenzyme A: amino acid N-acyltransferase (glycine N-choloyltransferase)
Introduction
The protein encoded by this gene is a liver enzyme that catalyzes the transfer of C24 bile acids from the acyl-CoA thioester to either glycine or taurine, the second step in the formation of bile acid-amino acid conjugates. The bile acid conjugates then act as a detergent in the gastrointestinal tract, which enhances lipid and fat-soluble vitamin absorption. Defects in this gene are a cause of familial hypercholanemia (FHCA). Two transcript variants encoding the same protein have been found for this gene.
Entrez Gene ID
570
UniProt ID
Q14032
Alternative Names
Bile Acid-CoA:Amino Acid N-Acyltransferase; Bile Acid CoA: Amino Acid N-Acyltransferase (Glycine N-Choloyltransferase); Long-Chain Fatty-Acyl-CoA Hydrolase; Glycine N-Choloyltransferase; BACAT; BAT;
Function
Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine (PubMed:12810727, PubMed:8034703, PubMed:2037576, PubMed:12239217).
More than 95% of the BAs are N-acyl amidates with glycine and taurine (PubMed:8034703).
Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (PubMed:12810727).
This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (PubMed:12810727).
May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (PubMed:12810727, PubMed:8034703, PubMed:12239217).
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 (PubMed:12810727).
Biological Process
Acyl-CoA metabolic process Source: UniProtKB
Animal organ regeneration Source: Ensembl
Bile acid biosynthetic process Source: UniProtKB
Bile acid conjugation Source: UniProtKB
Bile acid metabolic process Source: Reactome
Fatty acid metabolic process Source: GO_Central
Glycine metabolic process Source: UniProtKB
Liver development Source: Ensembl
Protein localization Source: Reactome
Taurine metabolic process Source: UniProtKB
Cellular Location
Cytosol; Peroxisome
Involvement in disease
Familial hypercholanemia (FHCA): A disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.

Qin, X., Zhang, Y., Lu, J., Huang, S., Liu, Z., & Wang, X. (2021). CYP3A deficiency alters bile acid homeostasis and leads to changes in hepatic susceptibility in rats. Toxicology and Applied Pharmacology, 115703.

Alrehaili, B. D., Lee, M., Takahashi, S., Gonzalez, F. J., & Lee, Y. K. (2020). Mice with Bile acid‐CoA: amino acid N‐acyltransferase deletion are Protected from Obesity. The FASEB Journal, 34(S1), 1-1.

Alonso-Peña, M., Geier, A., & Hermanns, H. (2020). Suppression of bile acid-CoA: amino acid N-acyltransferase gene expression by Oncostatin M. Zeitschrift für Gastroenterologie, 58(01), 3-29.

Civitello, M. L., Denton, R., Zasloff, M. A., & Malone, J. H. (2019). Activation of the Bile Acid Pathway and No Observed Antimicrobial Peptide Sequences in the Skin of a Poison Frog. G3: Genes, Genomes, Genetics, 9(2), 581-589.

Alonso-Pena, M., Geier, A., & Hermanns, H. M. (2019). Suppression of bile acid-CoA: amino acid N-acyltransferase gene expression by the interleukin-6-type cytokine Oncostatin M. Zeitschrift für Gastroenterologie, 57(01), P1-1.

Obuz, U. B., & Lay, I. (2019). Pathways and Inborn Errors of Bile Acid Synthesis. Acta Medica, 50(4), 48-56.

Kirilenko, B. M., Hagey, L. R., Barnes, S., Falany, C. N., & Hiller, M. (2019). Evolutionary analysis of bile acid-conjugating enzymes reveals a complex duplication and reciprocal loss history. Genome biology and evolution, 11(11), 3256-3268.

Nittono, H., Kimura, A., Takei, H., Kurosawa, T., & Iida, T. (2017). Bile Acids and Cholestatic Liver Disease 3: Inborn Errors of Bile Acid Synthesis. In Bile Acids in Gastroenterology (pp. 135-144). Springer, Tokyo.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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