BAAT Protein (AA 1-418) (Strep Tag)

Catalog No. ABIN3089918

Product Details

Target: BAAT (Bile Acid CoA: Amino Acid N-Acyltransferase (Glycine N-Choloyltransferase) (BAAT))

Protein Type: Recombinant

Protein Characteristics: AA 1-418

Origin: Human

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This BAAT protein is labelled with Strep Tag.

Application: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Sequence: MIQLTATPVS ALVDEPVHIR ATGLIPFQMV SFQASLEDEN GDMFYSQAHY RANEFGEVDL NHASSLGGDY MGVHPMGLFW SLKPEKLLTR LLKRDVMNRP FQVQVKLYDL ELIVNNKVAS APKASLTLER WYVAPGVTRI KVREGRLRGA LFLPPGEGLF PGVIDLFGGL GGLLEFRASL LASRGFASLA LAYHNYEDLP RKPEVTDLEY FEEAANFLLR HPKVFGSGVG VVSVCQGVQI GLSMAIYLKQ VTATVLINGT NFPFGIPQVY HGQIHQPLPH SAQLISTNAL GLLELYRTFE TTQVGASQYL FPIEEAQGQF LFIVGEGDKT INSKAHAEQA IGQLKRHGKN NWTLLSYPGA GHLIEPPYSP LCCASTTHDL RLHWGGEVIP HAAAQEHAWK EIQRFLRKHL IPDVTSQL
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us.

Characteristics: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
• These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

Expression System:

• ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
• During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Concentration:

• The concentration of our recombinant proteins is measured using the absorbance at 280nm.
• The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
• We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

Purification: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Purity: >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Grade: Crystallography grade

Application Details

Application Notes: In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.

Comment:

ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: Unlimited (if stored properly)

Target Details

Target: BAAT (Bile Acid CoA: Amino Acid N-Acyltransferase (Glycine N-Choloyltransferase) (BAAT))

Alternative Name: BAAT (BAAT Products)

Synonyms: BACAT Protein, BAT Protein, AI118337 Protein, AI158864 Protein, kan-1 Protein, BAAT Protein, bile acid-CoA:amino acid N-acyltransferase Protein, Bile acid-CoA:amino acid N-acyltransferase Protein, bile acid-Coenzyme A: amino acid N-acyltransferase Protein, bile acid CoA:amino acid N-acyltransferase Protein, BAAT Protein, RPIC_RS10270 Protein, Bcav_2277 Protein, Rpic12D_1765 Protein, Baat Protein, LOC481635 Protein, LOC100054567 Protein, LOC786798 Protein

Background: Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2),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). {ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576, ECO:0000269|PubMed:8034703, ECO:0000303|PubMed:12810727, ECO:0000303|PubMed:8034703}.

Molecular Weight: 46.3 kDa

UniProt: Q14032