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

Catalog No. ABIN3089918

This Recombinant BAAT protein is expressed in Cell-free protein synthesis (CFPS).

Quick Overview for BAAT Protein (AA 1-418) (Strep Tag) (ABIN3089918)

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

Protein Type: Recombinant

Origin: Human

Source: Cell-free protein synthesis (CFPS)

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

Purity: approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Grade: custom-made

Product Details

Protein Characteristics: AA 1-418

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

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 with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If 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 in one-step affinity chromatography
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a predefined custom protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.

The big advantage of ordering our predefined custom 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 against its specific reference buffer.
• We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

Purification: One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).

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.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

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

Alternative Name: BAAT

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