BAAT (NM_001127610) Human Recombinant Protein

CAT#: TP325667

Recombinant protein of human bile acid Coenzyme A: amino acid N-acyltransferase (glycine N-choloyltransferase) (BAAT), transcript variant 2

Product Images

Coomassie blue staining of purified BAAT protein (Cat# TP325667). The protein was produced from HEK293T cells transfected with BAAT cDNA clone (Cat# RC225667) using MegaTran 2.0 (Cat# TT210002).

Specifications

Product Data

• Species: Human
• Expression Host: HEK293T
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  Recombinant protein was produced with TrueORF clone, RC225667. Click on the TrueORF clone link to view cDNA and protein sequences.
• Tag: C-Myc/DDK
• Predicted MW: 46.1 kDa
• Concentration: >50 ug/mL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol
• Preparation: Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
• Storage: Store at -80°C.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.

Reference Data

• RefSeq: NP_001121082
• Locus ID: 570
• UniProt ID: Q14032
• Cytogenetics: 9q31.1
• Refseq Size: 3377
• Refseq ORF: 1254
• Synonyms: BACAT; BAT
• Summary: '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. [provided by RefSeq, Jul 2008]'
• Protein Pathways: Biosynthesis of unsaturated fatty acids, Metabolic pathways, Primary bile acid biosynthesis, Taurine and hypotaurine metabolism